|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
85-598 |
0e+00 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239454 [Multi-domain] Cd Length: 515 Bit Score: 993.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 85 QDRDKPSQIRFSNISAGKAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEAGD 164
Cdd:cd03338 1 TDKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 165 GTTSVVVIAGALLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVELSDRETLLNSATTSLNSKVVCQYSSLLS 244
Cdd:cd03338 81 GTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 245 PMSVDAVMKVIDPTTANSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANT--GVTRVEKAKIGLIQFCLSAPKTDMDN 322
Cdd:cd03338 161 PIAVDAVLKVIDPATATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKagGPTRIEKAKIGLIQFCLSPPKTDMDN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 323 QIVVSDYAQMDRVLREERAYILNLVKQIKKAGCNVLLIQKSILRDALSDLALHFLNKMKIMVVKDIERDDIEFICKTIGT 402
Cdd:cd03338 241 NIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQKSILRDAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 403 KPVAHIDQFTPDMLGSAELAEEVNLnGSGKLIKITGCTNPGKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKRALI 482
Cdd:cd03338 321 KPVASIDHFTEDKLGSADLVEEVSL-GDGKIVKITGVKNPGKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 483 AGGGAPEIELALRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISN 562
Cdd:cd03338 400 PGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITN 479
|
490 500 510
....*....|....*....|....*....|....*.
gi 699669686 563 ILEELVVQPLLVSLSALTLATETVRSILKIDDVVNT 598
Cdd:cd03338 480 ILEENVVQPLLVSTSAITLATETVRMILKIDDIVLA 515
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
85-599 |
0e+00 |
|
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT delta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274083 Cd Length: 517 Bit Score: 917.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 85 QDRDKPSQIRFSNISAGKAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEAGD 164
Cdd:TIGR02342 2 QDKDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 165 GTTSVVVIAGALLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVELSDRETLLNSATTSLNSKVVCQYSSLLS 244
Cdd:TIGR02342 82 GTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 245 PMSVDAVMKVIDPTTANSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKV--ANTGVTRVEKAKIGLIQFCLSAPKTDMDN 322
Cdd:TIGR02342 162 PLAVDAVLKVIDPENAKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKAskSAGGPTRIEKAKIGLIQFQISPPKTDMEN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 323 QIVVSDYAQMDRVLREERAYILNLVKQIKKAGCNVLLIQKSILRDALSDLALHFLNKMKIMVVKDIERDDIEFICKTIGT 402
Cdd:TIGR02342 242 QIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSILRDAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIGC 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 403 KPVAHIDQFTPDMLGSAELAEEVNLNGsGKLIKITGCTNPGKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKRALI 482
Cdd:TIGR02342 322 KPIASIDHFTADKLGSAELVEEVDSDG-GKIIKITGIQNAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 483 AGGGAPEIELALRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISN 562
Cdd:TIGR02342 401 AGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITN 480
|
490 500 510
....*....|....*....|....*....|....*..
gi 699669686 563 ILEELVVQPLLVSLSALTLATETVRSILKIDDVVNTR 599
Cdd:TIGR02342 481 MLEEHVLQPLLVTTSAITLASETVRSILKIDDIVFTR 517
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
86-596 |
0e+00 |
|
chaperonin families, type I and type II. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.
Pssm-ID: 238189 Cd Length: 464 Bit Score: 594.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 86 DRDKPSQIRFSNISAGKAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEAGDG 165
Cdd:cd00309 2 EREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 166 TTSVVVIAGALLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVELSDRETLLNSATTSLNSKVVCQYSSLLSP 245
Cdd:cd00309 82 TTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 246 MSVDAVMKVIDPTtaNSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANTGV-TRVEKAKIGLIQFCLSapktdmdnqi 324
Cdd:cd00309 162 LVVDAVLKVGKEN--GDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMpKRLENAKILLLDCKLE---------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 325 vvsdyaqmdrvlreerayilnlvkqikkagcNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIERDDIEFICKTIGTKP 404
Cdd:cd00309 230 -------------------------------YVVIAEKGI-----DDEALHYLAKLGIMAVRRVRKEDLERIAKATGATI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 405 VAHIDQFTPDMLGSAELAEEVNLnGSGKLIKITGCTNpGKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKRALIAG 484
Cdd:cd00309 274 VSRLEDLTPEDLGTAGLVEETKI-GDEKYTFIEGCKG-GKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 485 GGAPEIELALRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNIL 564
Cdd:cd00309 352 GGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMK 431
|
490 500 510
....*....|....*....|....*....|..
gi 699669686 565 EELVVQPLLVSLSALTLATETVRSILKIDDVV 596
Cdd:cd00309 432 EAGIIDPLKVKRQALKSATEAASLILTIDDII 463
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
104-599 |
0e+00 |
|
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.
Pssm-ID: 395068 [Multi-domain] Cd Length: 489 Bit Score: 568.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 104 VADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEAGDGTTSVVVIAGALLDACSRL 183
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 184 LQKGIHPTIISESFQKALDKGIEVLSNM-AQPVELSDRETLLNSATTSLNSKVVCQYSSLLSPMSVDAVMKVidPTTANS 262
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAI--PKNDGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 263 VDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANTG-VTRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDRVLREERA 341
Cdd:pfam00118 159 FDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDmPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 342 YILNLVKQIKKAGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIERDDIEFICKTIGTKPVAHIDQFTPDMLGSAEL 421
Cdd:pfam00118 239 QILEIVEKIIDSGVNVVVCQKGI-----DDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 422 AEEVNLnGSGKLIKITGCTNPgKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELALRLNEYAR 501
Cdd:pfam00118 314 VEEEKI-GDEKYTFIEGCKSP-KAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 502 TLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNILEELVVQPLLVSLSALTL 581
Cdd:pfam00118 392 SVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
|
490
....*....|....*...
gi 699669686 582 ATETVRSILKIDDVVNTR 599
Cdd:pfam00118 472 ATEAASTILRIDDIIKAK 489
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
96-596 |
0e+00 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 557.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 96 SNISAGKAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEAGDGTTSVVVIAGA 175
Cdd:NF041082 21 NNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 176 LLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVELSDRETLLNSATTSLNSKVVCQYSSLLSPMSVDAVMKVI 255
Cdd:NF041082 101 LLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVKAVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 256 DPTTANSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANTGV-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDR 334
Cdd:NF041082 181 EKDGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMpKRVENAKIALLDAPLEVKKTEIDAKISITDPDQLQA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 335 VLREERAYILNLVKQIKKAGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIERDDIEFICKTIGTKPVAHIDQFTPD 414
Cdd:NF041082 261 FLDQEEKMLKEMVDKIADSGANVVFCQKGI-----DDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSIDDLSPE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 415 MLGSAELAEEVNLNGSgKLIKITGCTNPgKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELAL 494
Cdd:NF041082 336 DLGYAGLVEERKVGGD-KMIFVEGCKNP-KAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEVELAL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 495 RLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNILEELVVQPLLV 574
Cdd:NF041082 414 RLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVVEPLRV 493
|
490 500
....*....|....*....|..
gi 699669686 575 SLSALTLATETVRSILKIDDVV 596
Cdd:NF041082 494 KTQAIKSATEAAVMILRIDDVI 515
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
96-596 |
0e+00 |
|
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. Archaeal cpn60 (thermosome), together with TF55 from thermophilic bacteria and the eukaryotic cytosol chaperonin (CTT), belong to the type II group of chaperonins. Cpn60 consists of two stacked octameric rings, which are composed of one or two different subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.
Pssm-ID: 239459 [Multi-domain] Cd Length: 517 Bit Score: 548.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 96 SNISAGKAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEAGDGTTSVVVIAGA 175
Cdd:cd03343 19 MNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 176 LLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVELSDRETLLNSATTSLNSKVVCQYSSLLSPMSVDAVMKVI 255
Cdd:cd03343 99 LLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAEAAKDKLADLVVDAVLQVA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 256 DPTTAN-SVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANTGV-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMD 333
Cdd:cd03343 179 EKRDGKyVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMpKRVENAKIALLDAPLEVKKTEIDAKIRITSPDQLQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 334 RVLREERAYILNLVKQIKKAGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIERDDIEFICKTIGTKPVAHIDQFTP 413
Cdd:cd03343 259 AFLEQEEAMLKEMVDKIADTGANVVFCQKGI-----DDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTNIDDLTP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 414 DMLGSAELAEEVNLNGSgKLIKITGCTNPgKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELA 493
Cdd:cd03343 334 EDLGEAELVEERKVGDD-KMVFVEGCKNP-KAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGAVEIELA 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 494 LRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNILEELVVQPLL 573
Cdd:cd03343 412 KRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVDMLEKGVIEPLR 491
|
490 500
....*....|....*....|...
gi 699669686 574 VSLSALTLATETVRSILKIDDVV 596
Cdd:cd03343 492 VKKQAIKSATEAATMILRIDDVI 514
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
87-596 |
0e+00 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 526.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 87 RDKPSQIRFSNISAGKAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEAGDGT 166
Cdd:NF041083 12 RTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 167 TSVVVIAGALLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVELSDRETLLNSATTSLNSKVVCQYSSLLSPM 246
Cdd:NF041083 92 TTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKGVEEARDYLAEI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 247 SVDAVMKVIDPTTA-NSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANTGV-TRVEKAKIGLIQFCLSAPKTDMDNQI 324
Cdd:NF041083 172 AVKAVKQVAEKRDGkYYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMpKRVENAKIALLDAPLEVKKTEIDAEI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 325 VVSDYAQMDRVLREERAYILNLVKQIKKAGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIERDDIEFICKTIGTKP 404
Cdd:NF041083 252 RITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGI-----DDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 405 VAHIDQFTPDMLGSAELAEEVNLnGSGKLIKITGCTNPgKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKRALIAG 484
Cdd:NF041083 327 VTNIDDLTPEDLGYAELVEERKV-GDDKMVFVEGCKNP-KAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 485 GGAPEIELALRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNIL 564
Cdd:NF041083 405 GGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVDMW 484
|
490 500 510
....*....|....*....|....*....|..
gi 699669686 565 EELVVQPLLVSLSALTLATETVRSILKIDDVV 596
Cdd:NF041083 485 ELGVIEPLRVKTQAIKSATEAATMILRIDDVI 516
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
96-596 |
0e+00 |
|
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather than eukaryotic form of the group II chaperonin (counterpart to the group I chaperonin, GroEL/GroES, in bacterial), a torroidal, ATP-dependent molecular chaperone that assists in the folding or refolding of nascent or denatured proteins. Various homologous subunits, one to five per archaeal genome, may be designated alpha, beta, etc., but phylogenetic analysis does not show distinct alpha subunit and beta subunit lineages traceable to ancient paralogs. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274080 Cd Length: 519 Bit Score: 525.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 96 SNISAGKAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEAGDGTTSVVVIAGA 175
Cdd:TIGR02339 20 NNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 176 LLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVELSDRETLLNSATTSLNSKVVCQYS-SLLSPMSVDAVMKV 254
Cdd:TIGR02339 100 LLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSKASAEVAkDKLADLVVEAVKQV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 255 IDPTTANS--VDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANTGV-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQ 331
Cdd:TIGR02339 180 AELRGDGKyyVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMpKRVENAKIALLDAPLEVEKTEIDAKIRITDPDQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 332 MDRVLREERAYILNLVKQIKKAGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIERDDIEFICKTIGTKPVAHIDQF 411
Cdd:TIGR02339 260 IKKFLDQEEAMLKEMVDKIASAGANVVICQKGI-----DDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVSSIDEI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 412 TPDMLGSAELAEEVNLnGSGKLIKITGCTNPgKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKRALIAGGGAPEIE 491
Cdd:TIGR02339 335 TESDLGYAELVEERKV-GEDKMVFVEGCKNP-KAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVAGGGAVEIE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 492 LALRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNILEELVVQP 571
Cdd:TIGR02339 413 LALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTGEIEDMLELGVIEP 492
|
490 500
....*....|....*....|....*
gi 699669686 572 LLVSLSALTLATETVRSILKIDDVV 596
Cdd:TIGR02339 493 LRVKEQAIKSATEAATMILRIDDVI 517
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
96-596 |
1.99e-148 |
|
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: 438.66 E-value: 1.99e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 96 SNISAGKAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEAGDGTTSVVVIAGA 175
Cdd:cd03339 27 SHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 176 LLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVELS--DRETLLNSATTSLNSKVVCQYSSLLSPMSVDAVMK 253
Cdd:cd03339 107 LLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSpdNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAVLS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 254 VIDpTTANSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANTGVTR-VEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQM 332
Cdd:cd03339 187 VAD-LERKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKeVKDAKIAILTCPFEPPKPKTKHKLDITSVEDY 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 333 DRVLREERAYILNLVKQIKKAGCNVLLIQKsilrdALSDLALHFLNKMKIMVVKDIERDDIEFICKTIGTKPVAHIDQFT 412
Cdd:cd03339 266 KKLQEYEQKYFREMVEQVKDAGANLVICQW-----GFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFEDLS 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 413 PDMLGSAELAEEVNLNGS-GKLIKITGCTNpGKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKRALIAGGGAPEIE 491
Cdd:cd03339 341 PEKLGKAGLVREISFGTTkDKMLVIEGCPN-SKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGGGAAEIS 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 492 LALRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRH-AQGEKTAGINVRKGGISNILEELVVQ 570
Cdd:cd03339 420 CSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPHLGIDCLGRGTNDMKEQKVFE 499
|
490 500
....*....|....*....|....*.
gi 699669686 571 PLLVSLSALTLATETVRSILKIDDVV 596
Cdd:cd03339 500 TLISKKQQILLATQVVKMILKIDDVI 525
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
85-596 |
5.88e-132 |
|
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: 396.48 E-value: 5.88e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 85 QDRDKPSQIR-----FSNISAGKAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQD 159
Cdd:TIGR02343 15 KDQDNKKRLKgleakKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 160 IEAGDGTTSVVVIAGALLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVELSD--RETLLNSATTSLNSKVVC 237
Cdd:TIGR02343 95 DEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNnnREPLIQAAKTSLGSKIVS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 238 QYSSLLSPMSVDAVMKVIDpTTANSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANTGVTR-VEKAKIGLIQFCLSAP 316
Cdd:TIGR02343 175 KCHRRFAEIAVDAVLNVAD-MERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKeVEDAKIAILTCPFEPP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 317 KTDMDNQIVVSDYAQMDRVLREERAYILNLVKQIKKAGCNVLLIQKsilrdALSDLALHFLNKMKIMVVKDIERDDIEFI 396
Cdd:TIGR02343 254 KPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQW-----GFDDEANHLLLQNDLPAVRWVGGQELELI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 397 CKTIGTKPVAHIDQFTPDMLGSAELAEEVNLNGSG-KLIKITGCTNpGKTVTIVVRGSNKLVLEEAERSIHDALCVIRCL 475
Cdd:TIGR02343 329 AIATGGRIVPRFQELSKDKLGKAGLVREISFGTTKdRMLVIEQCKN-SKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 476 VKKRALIAGGGAPEIELALRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQGEKTA-GIN 554
Cdd:TIGR02343 408 IKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNlGVD 487
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 699669686 555 VRKGGISNILEELVVQPLLVSLSALTLATETVRSILKIDDVV 596
Cdd:TIGR02343 488 CLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVI 529
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
91-596 |
6.85e-127 |
|
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: 383.18 E-value: 6.85e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 91 SQIrFSNISAGKAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEAGDGTTSVV 170
Cdd:cd03340 16 GQL-ISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 171 VIAGALLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVELSD----RETLLNSATTSLNSKVVCQYSSLLSPM 246
Cdd:cd03340 95 VLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDkeeqRELLEKCAATALNSKLIASEKEFFAKM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 247 SVDAVMKVIDpttanSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANTGV----TRVEKAKIGLIQFCLSApKTDMDN 322
Cdd:cd03340 175 VVDAVLSLDD-----DLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAGFeqqpKKFKNPKILLLNVELEL-KAEKDN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 323 -QIVVSDYAQMDRVLREERAYILNLVKQIKKAGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIERDDIEFICKTIG 401
Cdd:cd03340 249 aEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPI-----GDLATQYFADRDIFCAGRVPEEDLKRVAQATG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 402 TKPVAHIDQFTPDMLGSAELAEEVNLnGSGKLIKITGCTNpGKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKRAL 481
Cdd:cd03340 324 GSIQTTVSNITDDVLGTCGLFEERQV-GGERYNIFTGCPK-AKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 482 IAGGGAPEIELALRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQGEKT-AGINVRKGGI 560
Cdd:cd03340 402 VAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKwYGVDINNEGI 481
|
490 500 510
....*....|....*....|....*....|....*.
gi 699669686 561 SNILEELVVQPLLVSLSALTLATETVRSILKIDDVV 596
Cdd:cd03340 482 ADNFEAFVWEPSLVKINALTAATEAACLILSVDETI 517
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
86-596 |
3.01e-122 |
|
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: 371.23 E-value: 3.01e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 86 DRDKPSQIRFSNISAGKAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEAGDG 165
Cdd:cd03335 2 ERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 166 TTSVVVIAGALLDACSRLLQKGIHPTIISESFQKALDKGIEVLS-NMAQPVELSDRETLLNSATTSLNSKVVCQYSSLLS 244
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKeHLSISVDNLGKESLINVAKTSMSSKIIGADSDFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 245 PMSVDAVM--KVIDPTTANSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANTGV-TRVEKAKIGLIQFCLSAPKTDMD 321
Cdd:cd03335 162 NMVVDAILavKTTNEKGKTKYPIKAVNILKAHGKSAKESYLVNGYALNCTRASQGMpTRVKNAKIACLDFNLQKTKMKLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 322 NQIVVSDYAQMDRVLREERAYILNLVKQIKKAGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIERDDIEFICKTIG 401
Cdd:cd03335 242 VQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGI-----DDMCLKYFVEAGAMAVRRVKKEDLRRIAKATG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 402 TKPVAHI------DQFTPDMLGSAELAEEVNLnGSGKLIKITGCTNpGKTVTIVVRGSNKLVLEEAERSIHDALCVIRCL 475
Cdd:cd03335 317 ATLVSTLanlegeETFDPSYLGEAEEVVQERI-GDDELILIKGTKK-RSSASIILRGANDFMLDEMERSLHDALCVVKRT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 476 VKKRALIAGGGAPEIELALRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHA--------QG 547
Cdd:cd03335 395 LESNSVVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAaaqvkpdkKH 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 699669686 548 EKTAGINVRKGGISNILEELVVQPLLVSLSALTLATETVRSILKIDDVV 596
Cdd:cd03335 475 LKWYGLDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLI 523
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
84-596 |
3.92e-121 |
|
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: 367.01 E-value: 3.92e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 84 SQDRDKPSQIRFSNISAGKAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEAG 163
Cdd:cd03337 8 NTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 164 DGTTSVVVIAGALLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVELSDRETLLNSATTSLNSKVVCQYSSLL 243
Cdd:cd03337 88 DGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFVSRWSDLM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 244 SPMSVDAVMKVI--DPTTANSVDL-RDIKIVKKLGGTIDDCELVEGLVLtqkvaNTGVTrvekakigliqfclsapktdm 320
Cdd:cd03337 168 CNLALDAVKTVAveENGRKKEIDIkRYAKVEKIPGGEIEDSRVLDGVML-----NKDVT--------------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 321 dnqivvsdYAQMDRVLREERAYILNlvkqikkagCNVLLIqkSILRDALSDLALHFLNKMKIMVVKDIERDDIEFICKTI 400
Cdd:cd03337 222 --------HPKMRRRIENPRIVLLD---------CPLEYL--VITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARAC 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 401 GTKPVAHIDQFTPDMLGSAELAEEVNLNGSGKLIKITGCTNPgKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKRA 480
Cdd:cd03337 283 GATIVNRPEELTESDVGTGAGLFEVKKIGDEYFTFITECKDP-KACTILLRGASKDVLNEVERNLQDAMAVARNIILNPK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 481 LIAGGGAPEIELALRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQGEK-TAGINVRKGG 559
Cdd:cd03337 362 LVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENsTWGIDGETGD 441
|
490 500 510
....*....|....*....|....*....|....*..
gi 699669686 560 ISNILEELVVQPLLVSLSALTLATETVRSILKIDDVV 596
Cdd:cd03337 442 IVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
83-596 |
5.76e-121 |
|
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: 368.28 E-value: 5.76e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 83 LSQDRDKPSQIRFSNISAGKAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEA 162
Cdd:TIGR02340 3 LGGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 163 GDGTTSVVVIAGALLDACSRLLQKGIHPTIISESFQKALDKGIEVLS-NMAQPVELSDRETLLNSATTSLNSKVVCQYSS 241
Cdd:TIGR02340 83 GDGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKeNLSVSVDELGREALINVAKTSMSSKIIGLDSD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 242 LLSPMSVDAVM--KVIDPTTANSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANTGV-TRVEKAKIGLIQFCLSAPKT 318
Cdd:TIGR02340 163 FFSNIVVDAVLavKTTNENGETKYPIKAINILKAHGKSARESMLVKGYALNCTVASQQMpKRIKNAKIACLDFNLQKAKM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 319 DMDNQIVVSDYAQMDRVLREERAYILNLVKQIKKAGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIERDDIEFICK 398
Cdd:TIGR02340 243 ALGVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGI-----DDMCLKYFVEAGAMGVRRCKKEDLKRIAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 399 TIGTKPVAHI------DQFTPDMLGSAELAEEVNLnGSGKLIKITGcTNPGKTVTIVVRGSNKLVLEEAERSIHDALCVI 472
Cdd:TIGR02340 318 ATGATLVSTLadlegeETFEASYLGFADEVVQERI-ADDECILIKG-TKKRKSASIILRGANDFMLDEMERSLHDALCVV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 473 RCLVKKRALIAGGGAPEIELALRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHA------- 545
Cdd:TIGR02340 396 KRTLESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAaaqlkpe 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 699669686 546 -QGEKTAGINVRKGGISNILEELVVQPLLVSLSALTLATETVRSILKIDDVV 596
Cdd:TIGR02340 476 kKHLKWYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLI 527
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
96-596 |
8.09e-118 |
|
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: 359.84 E-value: 8.09e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 96 SNISAGKAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEAGDGTTSVVVIAGA 175
Cdd:TIGR02345 22 SNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 176 LLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVELSD---RETLLNSATTSLNSKVVCQYSSLLSPMSVDAVM 252
Cdd:TIGR02345 102 LLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqRELLEKCAATALSSKLISHNKEFFSKMIVDAVL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 253 KVIDpttaNSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANTGV----TRVEKAKIGLIQFCLSApKTDMDN-QIVVS 327
Cdd:TIGR02345 182 SLDR----DDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAGFeqqpKKFANPKILLLNVELEL-KAEKDNaEIRVE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 328 DYAQMDRVLREERAYILNLVKQIKKAGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIERDDIEFICKTIGTKPVAH 407
Cdd:TIGR02345 257 DVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPI-----GDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQST 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 408 IDQFTPDMLGSAELAEEVNLnGSGKLIKITGCTNpGKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKRALIAGGGA 487
Cdd:TIGR02345 332 TSDLEADVLGTCALFEERQI-GSERYNYFTGCPH-AKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 488 PEIELALRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNILEEL 567
Cdd:TIGR02345 410 IEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFEAF 489
|
490 500
....*....|....*....|....*....
gi 699669686 568 VVQPLLVSLSALTLATETVRSILKIDDVV 596
Cdd:TIGR02345 490 VWEPALVKINALKAAFEAACTILSVDETI 518
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
94-596 |
2.61e-116 |
|
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: 355.87 E-value: 2.61e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 94 RFSNISAGKAVADAIRTSLGPKGMDKMIQ--DAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEAGDGTTSVVV 171
Cdd:cd03336 15 RLSSFVGAIAIGDLVKTTLGPKGMDKILQsvGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDGTTSVTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 172 IAGALLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVELSD---RETLLNSATTSLNSKVVCQYSSLLSPMSV 248
Cdd:cd03336 95 LAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEeafREDLLNIARTTLSSKILTQDKEHFAELAV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 249 DAVMKVIDpttanSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANTGVTRVEKAKIgLIQfclsapKTDMDN------ 322
Cdd:cd03336 175 DAVLRLKG-----SGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQPKRIENAKI-LIA------NTPMDTdkikif 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 323 --QIVVSDYAQMDRVLREERAYILNLVKQIKKAGCNVLliqksILRDALSDLALHFLNKMKIMVVKDIERDDIEFICKTI 400
Cdd:cd03336 243 gaKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCF-----INRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 401 GTKPVAHIDQFTPDMLGSAELAEEVNLnGSGKLIKITGCTNpGKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKRA 480
Cdd:cd03336 318 GGEIASTFDHPELVKLGTCKLIEEIMI-GEDKLIRFSGVAA-GEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 481 LIAGGGAPEIELALRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGI 560
Cdd:cd03336 396 VVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTV 475
|
490 500 510
....*....|....*....|....*....|....*.
gi 699669686 561 SNILEELVVQPLLVSLSALTLATETVRSILKIDDVV 596
Cdd:cd03336 476 GDMKELGITESFKVKRQVLLSASEAAEMILRVDDII 511
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
94-596 |
1.21e-115 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 353.23 E-value: 1.21e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 94 RFSNISAGKAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHP----AAKMLVELSKAQDIEAGDGTTSV 169
Cdd:COG0459 12 RRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTTTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 170 VVIAGALLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVElsDRETLLNSATTSLNSKvvcqysSLLSPMSVD 249
Cdd:COG0459 92 TVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVD--DKEELAQVATISANGD------EEIGELIAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 250 AVMKVidptTANSVdlrdIKIVKKlGGTIDDCELVEGLVLTQKVANTGvtrvekakigliqfclsapktdmdnqiVVSDY 329
Cdd:COG0459 164 AMEKV----GKDGV----ITVEEG-KGLETELEVVEGMQFDKGYLSPY---------------------------FVTDP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 330 AQMDRVLreERAYIL-------------NLVKQIKKAGCNVLLIQKSIlrdalSDLALHFL--NKM----KIMVVK---- 386
Cdd:COG0459 208 EKMPAEL--ENAYILltdkkissiqdllPLLEKVAQSGKPLLIIAEDI-----DGEALATLvvNGIrgvlRVVAVKapgf 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 387 -DIERDDIEFICKTIGTKPVAH-----IDQFTPDMLGSAELAEEvnlnGSGKLIKITGCTNPgKTVTIVVRGSNKLVLEE 460
Cdd:COG0459 281 gDRRKAMLEDIAILTGGRVISEdlglkLEDVTLDDLGRAKRVEV----DKDNTTIVEGAGNP-KAIVILVGAATEVEVKE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 461 AERSIHDALCVIRCLVKKRaLIAGGGAPEIELALRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTEL 540
Cdd:COG0459 356 RKRRVEDALHATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKV 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 699669686 541 RnrhAQGEKTAGINVRKGGISNILEELVVQPLLVSLSALTLATETVRSILKIDDVV 596
Cdd:COG0459 435 R---AAKDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVI 487
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
95-596 |
7.06e-115 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239457 [Multi-domain] Cd Length: 472 Bit Score: 350.37 E-value: 7.06e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 95 FSNISAGKAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEAGDGTTSVVVIAG 174
Cdd:cd03341 11 LRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 175 ALLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMA-QPVE-LSDRETLLNSATTSLNSKVVcQYSSLLSPMSVDAVM 252
Cdd:cd03341 91 ELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVvYKIEdLRNKEEVSKALKTAIASKQY-GNEDFLSPLVAEACI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 253 KVIdPTTANSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANTgVTRVEKAKIGLiqfclsapktdmdnqivvsdyaqm 332
Cdd:cd03341 170 SVL-PENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKREPEGS-VKRVKKAKVAV------------------------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 333 drvlreeraYILNLvkqikKAGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIERDDIEFICKTIGTKPVAHIDQFT 412
Cdd:cd03341 224 ---------FSCPF-----DIGVNVIVAGGSV-----GDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 413 PDMLGSAELA--EEVnlnGSGKLIKITGCTNPGKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKRALIAGGGAPEI 490
Cdd:cd03341 285 PEEIGYCDSVyvEEI---GDTKVVVFRQNKEDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 491 ELALRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKG--GISNILEELV 568
Cdd:cd03341 362 ELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGdeGTKDAKEAGI 441
|
490 500
....*....|....*....|....*...
gi 699669686 569 VQPLLVSLSALTLATETVRSILKIDDVV 596
Cdd:cd03341 442 FDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
97-596 |
8.20e-115 |
|
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: 352.48 E-value: 8.20e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 97 NISAGKAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEAGDGTTSVVVIAGAL 176
Cdd:TIGR02346 23 NIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 177 LDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMA--QPVELSDRETLLNSATTSLNSKvvcQYSS--LLSPMSVDAVM 252
Cdd:TIGR02346 103 LNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVvwEVKDLRDKDELIKALKASISSK---QYGNedFLAQLVAQACS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 253 KVIdPTTANSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKvANTGVTRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQM 332
Cdd:TIGR02346 180 TVL-PKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNRE-AEGSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNAEEL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 333 DRVLREERAYILNLVKQIKKAGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIERDDIEFICKTIGTKPVAHIDQFT 412
Cdd:TIGR02346 258 LNYSKGEENQIEAMIKAIADSGVNVIVTGGSV-----GDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 413 PDMLGSAELA--EEVnlnGSGKLIKITGCTNPGKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKRALIAGGGAPEI 490
Cdd:TIGR02346 333 PEEIGYVDSVyvSEI---GGDKVTVFKQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEI 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 491 ELALRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKG--GISNILEELV 568
Cdd:TIGR02346 410 ELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAEsdGVKDASEAGI 489
|
490 500
....*....|....*....|....*...
gi 699669686 569 VQPLLVSLSALTLATETVRSILKIDDVV 596
Cdd:TIGR02346 490 YDMLATKKWAIKLATEAAVTVLRVDQII 517
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
88-596 |
3.34e-113 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 348.17 E-value: 3.34e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 88 DKPSQIRFSNISAGKAVADAIRTSLGPKGMDKMIQDAK-----GDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEA 162
Cdd:PTZ00212 18 EKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMSegprsGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 163 GDGTTSVVVIAGALLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVELSD---RETLLNSATTSLNSKVVCQY 239
Cdd:PTZ00212 98 GDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEekfKEDLLNIARTTLSSKLLTVE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 240 SSLLSPMSVDAVMKVidpttANSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANTGVTRVEKAKIgliqfcLSApKTD 319
Cdd:PTZ00212 178 KDHFAKLAVDAVLRL-----KGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVGQPKRLENCKI------LVA-NTP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 320 MDN--------QIVVSDYAQMDRVLREERAYILNLVKQIKKAGCNVLliqksILRDALSDLALHFLNKMKIMVVKDIERD 391
Cdd:PTZ00212 246 MDTdkikiygaKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVF-----INRQLIYNYPEQLFAEAGIMAIEHADFD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 392 DIEFICKTIGTKPVAHIDQFTPDMLGSAELAEEVnLNGSGKLIKITGCTNpGKTVTIVVRGSNKLVLEEAERSIHDALCV 471
Cdd:PTZ00212 321 GMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEI-MIGEDKLIRFSGCAK-GEACTIVLRGASTHILDEAERSLHDALCV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 472 IRCLVKKRALIAGGGAPEIELALRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQGEKTA 551
Cdd:PTZ00212 399 LSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTA 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 699669686 552 GINVRKGGISNILEELVVQPLLVSLSALTLATETVRSILKIDDVV 596
Cdd:PTZ00212 479 GIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDII 523
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
84-596 |
3.69e-112 |
|
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: 345.18 E-value: 3.69e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 84 SQDRDKPSQIRFSNISAGKAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEAG 163
Cdd:TIGR02344 8 NTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 164 DGTTSVVVIAGALLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVELSDRETLLNSATTSLNSKVVCQYSSLL 243
Cdd:TIGR02344 88 DGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRWSDLM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 244 SPMSVDAVMKV-IDPTTANSVDL-RDIKIVKKLGGTIDDCELVEGLVLTQKVANTGVTR-VEKAKIGLIQFCLSAPKTDM 320
Cdd:TIGR02344 168 CDLALDAVRTVqRDENGRKEIDIkRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRyIENPRIVLLDCPLEYKKGES 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 321 DNQIVVSDYAQMDRVLREERAYILNLVKQIKKAGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIERDDIEFICKTI 400
Cdd:TIGR02344 248 QTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGV-----SDLAQHYLLKANITAIRRVRKTDNNRIARAC 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 401 GTKPVAHIDQFTPDMLGSAELAEEVNLNGSGKLIKITGCTNPgKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKRA 480
Cdd:TIGR02344 323 GATIVNRPEELRESDVGTGCGLFEVKKIGDEYFTFITECKDP-KACTILLRGASKDILNEVERNLQDAMAVARNVLLDPK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 481 LIAGGGAPEIELALRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQGEK-TAGINVRKGG 559
Cdd:TIGR02344 402 LVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNcTWGIDGETGK 481
|
490 500 510
....*....|....*....|....*....|....*..
gi 699669686 560 ISNILEELVVQPLLVSLSALTLATETVRSILKIDDVV 596
Cdd:TIGR02344 482 IVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
84-599 |
7.01e-89 |
|
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: 284.83 E-value: 7.01e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 84 SQDRDKPSQIRFSNISAGKAVADAIRTSLGPKGMDKMIQDA--KGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIE 161
Cdd:TIGR02341 6 GADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSssDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 162 AGDGTTSVVVIAGALLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAqpVELSD-----RETLLNSATTSLNSKVV 236
Cdd:TIGR02341 86 VGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSA--VDNGSdevkfRQDLMNIARTTLSSKIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 237 CQYSSLLSPMSVDAVMKVidpttANSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANTGVTRVEKAKIGLIQFCLSAP 316
Cdd:TIGR02341 164 SQHKDHFAQLAVDAVLRL-----KGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 317 KTDM-DNQIVVSDYAQMDRVLREERAYILNLVKQIKKAGCNVLliqksILRDALSDLALHFLNKMKIMVVKDIERDDIEF 395
Cdd:TIGR02341 239 KVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCF-----INRQLIYNYPEQLFADAGVMAIEHADFEGVER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 396 ICKTIGTKPVAHIDQFTPDMLGSAELAEEVNLnGSGKLIKITGCtNPGKTVTIVVRGSNKLVLEEAERSIHDALCVIRCL 475
Cdd:TIGR02341 314 LALVTGGEIVSTFDHPELVKLGSCDLIEEIMI-GEDKLLKFSGV-KLGEACTIVLRGATQQILDEAERSLHDALCVLSQT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 476 VKKRALIAGGGAPEIELALRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINV 555
Cdd:TIGR02341 392 VKESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDM 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 699669686 556 RKGGISNILEELVVQPLLVSLSALTLATETVRSILKIDDVVNTR 599
Cdd:TIGR02341 472 NEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAA 515
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
97-596 |
1.30e-86 |
|
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: 277.60 E-value: 1.30e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 97 NISAGKAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEAGDGTTSVVVIAGAL 176
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 177 LDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVE-LSDRETLLNSATTSLNSKVVCQYSSLLSPMSVDAVMKVI 255
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEiDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 256 DPTTanSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANTGV-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSdyaqmdr 334
Cdd:cd03342 177 KPDE--PIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMpKRVENAYILTCNVSLEYEKTEVNSGFFYS------- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 335 vlreerayilnlvkqikkagcnVLLIQKSIlrDALSdlaLHFLNKMKIMVVKDIERDDIEFICKTIGTKPVAHIDQFTPD 414
Cdd:cd03342 248 ----------------------VVINQKGI--DPPS---LDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 415 MLGSAELAEEVNLnGSGKLIKITGCTNPgKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELAL 494
Cdd:cd03342 301 CLGYAGLVYERTL-GEEKYTFIEGVKNP-KSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 495 RLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNILEELVVQPLLV 574
Cdd:cd03342 379 HLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSV 458
|
490 500
....*....|....*....|..
gi 699669686 575 SLSALTLATETVRSILKIDDVV 596
Cdd:cd03342 459 KRQILHSATVIASQLLLVDEII 480
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
97-596 |
7.05e-82 |
|
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: 266.60 E-value: 7.05e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 97 NISAGKAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVELSKAQDIEAGDGTTSVVVIAGAL 176
Cdd:TIGR02347 21 NINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 177 LDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVELS-DRETLLNSATTSLNSKVVCQYSSLLSPMSVDAVMKVI 255
Cdd:TIGR02347 101 LKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEvDREFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 256 DPTTAnsVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANTGV-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDR 334
Cdd:TIGR02347 181 KDGED--IDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMpRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQREK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 335 VLREERAYILNLVKQI---KKAGCN-------VLLIQKSIlrDALSdlaLHFLNKMKIMVVKDIERDDIEFICKTIGTKP 404
Cdd:TIGR02347 259 LVKAERKFVDDRVKKIielKKKVCGkspdkgfVVINQKGI--DPPS---LDLLAKEGIMALRRAKRRNMERLTLACGGEA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 405 VAHIDQFTPDMLGSAELAEEVNLnGSGKLIKITGCTNPgKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKRALIAG 484
Cdd:TIGR02347 334 LNSVEDLTPECLGWAGLVYETTI-GEEKYTFIEECKNP-KSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPG 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 485 GGAPEIELALRLNEYARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNIL 564
Cdd:TIGR02347 412 AGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGVDLNTGEPIDPE 491
|
490 500 510
....*....|....*....|....*....|..
gi 699669686 565 EELVVQPLLVSLSALTLATETVRSILKIDDVV 596
Cdd:TIGR02347 492 IKGIWDNYRVKKQLIQSATVIASQLLLVDEVM 523
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
220-477 |
1.40e-66 |
|
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: 215.79 E-value: 1.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 220 RETLLNSATTSLNSKVVcQYSSLLSPMSVDAVMKVIDPTtaNSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANTGV- 298
Cdd:cd03333 1 RELLLQVATTSLNSKLS-SWDDFLGKLVVDAVLKVGPDN--RMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 299 TRVEKAKIGLIQFCLSapktdmdnqivvsdyaqmdrvlreerayilnlvkqikkagcNVLLIQKSIlrdalSDLALHFLN 378
Cdd:cd03333 78 KRLENAKILLLDCPLE-----------------------------------------YVVIAEKGI-----DDLALHYLA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 379 KMKIMVVKDIERDDIEFICKTIGTKPVAHIDQFTPDMLGSAELAEEVNLnGSGKLIKITGCTNpGKTVTIVVRGSNKLVL 458
Cdd:cd03333 112 KAGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKI-GEEKLTFIEGCKG-GKAATILLRGATEVEL 189
|
250
....*....|....*....
gi 699669686 459 EEAERSIHDALCVIRCLVK 477
Cdd:cd03333 190 DEVKRSLHDALCAVRAAVE 208
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
84-583 |
4.77e-23 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 103.07 E-value: 4.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 84 SQDRDKPSQIRFSN-----ISAG-KAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILK------QMQVLhpAAKML 151
Cdd:PTZ00114 8 SRYRFKGKEIRFGDearqsLLKGiERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKaiefsdRFENV--GAQLI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 152 VELSKAQDIEAGDGTTSVVVIAGALLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVElsDRETLLNSATTSL 231
Cdd:PTZ00114 86 RQVASKTNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVK--TKEDILNVATISA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 232 NSKVVcqysslLSPMSVDAVMKVidpttansvdLRDIKIVKKLGGTIDD-CELVEGLVLTQK------VANTGVTRVEka 304
Cdd:PTZ00114 164 NGDVE------IGSLIADAMDKV----------GKDGTITVEDGKTLEDeLEVVEGMSFDRGyispyfVTNEKTQKVE-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 305 kigliqfcLSAPktdmdnQIVVSDY--AQMDRVLReerayILNLVKQIKKagcNVLLIQKSILRDALSDLAlhfLNKM-- 380
Cdd:PTZ00114 226 --------LENP------LILVTDKkiSSIQSILP-----ILEHAVKNKR---PLLIIAEDVEGEALQTLI---INKLrg 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 381 --KIMVVK-----DIERDDIEFICKTIGTKPV------AHIDQFTPDMLGSAELA-----EEVNLNGSG--KLIK----- 435
Cdd:PTZ00114 281 glKVCAVKapgfgDNRKDILQDIAVLTGATVVsednvgLKLDDFDPSMLGSAKKVtvtkdETVILTGGGdkAEIKervel 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 436 ----ITGCTN--------------PGKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELALRLn 497
Cdd:PTZ00114 361 lrsqIERTTSeydkeklkerlaklSGGVAVIKVGGASEVEVNEKKDRIEDALNATRAAVEE-GIVPGGGVALLRASKLL- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 498 EYARTLRGMDSycVRAYG-----DALEVIPSTLAENAGLNPISTVTELRNRhaqGEKTAGINVRKGGISNILEELVVQPL 572
Cdd:PTZ00114 439 DKLEEDNELTP--DQRTGvkivrNALRLPTKQIAENAGVEGAVVVEKILEK---KDPSFGYDAQTGEYVNMFEAGIIDPT 513
|
570
....*....|.
gi 699669686 573 LVSLSALTLAT 583
Cdd:PTZ00114 514 KVVRSALVDAA 524
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
102-582 |
2.61e-18 |
|
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: 88.28 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 102 KAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHP----AAKMLVELSKAQDIEAGDGTTSVVVIAGALL 177
Cdd:cd03344 18 NKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLARAII 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 178 DACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVelSDRETLLNSATTSLNSkvvcqySSLLSPMSVDAVMKVidp 257
Cdd:cd03344 98 KEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPV--KTKEEIAQVATISANG------DEEIGELIAEAMEKV--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 258 ttansvdLRDIKIVKKLGGTIDD-CELVEGlvltqkvantgvtrvekakiglIQF---CLSaPK--TDMDNQIVVSdyaq 331
Cdd:cd03344 167 -------GKDGVITVEEGKTLETeLEVVEG----------------------MQFdrgYLS-PYfvTDPEKMEVEL---- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 332 mdrvlreERAYIL------NLVKQI-------KKAGCNVLLIQKSILRDALSDLALHFL-NKMKIMVVK-----DiER-- 390
Cdd:cd03344 213 -------ENPYILltdkkiSSIQELlpilelvAKAGRPLLIIAEDVEGEALATLVVNKLrGGLKVCAVKapgfgD-RRka 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 391 --DDI------EFICKTIGTKpvahIDQFTPDMLGSAELA-----EEVNLNGSGKLIKITG----------CTNP----- 442
Cdd:cd03344 285 mlEDIailtggTVISEELGLK----LEDVTLEDLGRAKKVvvtkdDTTIIGGAGDKAAIKAriaqirkqieETTSdydke 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 443 ----------GKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKrALIAGGG------APEIELALRLNEYARTlrGM 506
Cdd:cd03344 361 klqerlaklsGGVAVIKVGGATEVELKEKKDRVEDALNATRAAVEE-GIVPGGGvallraSPALDKLKALNGDEKL--GI 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 699669686 507 DsyCVRaygDALEVIPSTLAENAGLNP---ISTVTELRNRHaqgektaGINVRKGGISNILEELVVQPLLVSLSALTLA 582
Cdd:cd03344 438 E--IVR---RALEAPLRQIAENAGVDGsvvVEKVLESPDGF-------GYDAATGEYVDMIEAGIIDPTKVVRSALQNA 504
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
261-472 |
2.71e-18 |
|
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: 84.97 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 261 NSVDLRD-IKIVKKLGGTIDDCELVEGLVLTQKVANTGV-TRVEKAKIGLIQFCLsapktdmDNQIVVSDYAQMDRVLRE 338
Cdd:cd03334 42 DDMDIRQyVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMpSKIKNPRILLLQGPL-------EYQRVENKLLSLDPVILQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 339 ERAYILNLVKQIKKAGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIERDDIEFICKTIGTKPVAHID-QFTPDMLG 417
Cdd:cd03334 115 EKEYLKNLVSRIVALRPDVILVEKSV-----SRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDdLLTSPKLG 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 699669686 418 SAELAEE---VNLNGSGK-LIKITGCTNPGKTvTIVVRGSNKLVLEEAERSIHDALCVI 472
Cdd:cd03334 190 TCESFRVrtyVEEHGRSKtLMFFEGCPKELGC-TILLRGGDLEELKKVKRVVEFMVFAA 247
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
103-233 |
8.05e-16 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 80.62 E-value: 8.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 103 AVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHP----AAKMLVE-LSKAQDIeAGDGTTSVVVIAGALL 177
Cdd:PRK12849 21 KLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEvASKTNDV-AGDGTTTATVLAQALV 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 699669686 178 DACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVelSDRETLLNSATTSLNS 233
Cdd:PRK12849 100 QEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPV--SGSEEIAQVATISANG 153
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
91-586 |
1.12e-15 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 80.17 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 91 SQIRFSNISAGK------AVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHP----AAKMLVEL-SKAQD 159
Cdd:PRK12851 4 KEVKFHVEAREKmlrgvnILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVaSKTND 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 160 IeAGDGTTSVVVIAGALLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVElsDRETLLNSATTSLNSkvvcqy 239
Cdd:PRK12851 84 V-AGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVT--TNAEIAQVATISANG------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 240 ssllspmsvdavmkvidpttansvdlrDIKIVKKLGGTIDdcelveglvltqKVANTGVTRVEKAKIGL--------IQF 311
Cdd:PRK12851 155 ---------------------------DAEIGRLVAEAME------------KVGNEGVITVEESKTAEtelevvegMQF 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 312 clsapktdmDNQIV----VSDYAQMDRVLreERAYIL-------------NLVKQIKKAGCNVLLIQKSILRDALSDLAl 374
Cdd:PRK12851 196 ---------DRGYLspyfVTDADKMEAEL--EDPYILihekkisnlqdllPVLEAVVQSGKPLLIIAEDVEGEALATLV- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 375 hfLNKM----KIMVVK--------DIERDDI------EFICKTIGTKpvahIDQFTPDMLGSAE--LAEEVN---LNGSG 431
Cdd:PRK12851 264 --VNKLrgglKVAAVKapgfgdrrKAMLEDIailtggTVISEDLGIK----LENVTLEQLGRAKkvVVEKENttiIDGAG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 432 KLIKITG-----------CTNP--------------GKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKrALIAGGG 486
Cdd:PRK12851 338 SKTEIEGrvaqiraqieeTTSDydreklqerlaklaGGVAVIRVGASTEVEVKEKKDRVDDALHATRAAVEE-GIVPGGG 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 487 APEIELALRLNEyARTLRGMDSYCVRAYGDALEVIPSTLAENAGLNPISTVTELRNrhaqGEKTAGINVRKGGISNILEE 566
Cdd:PRK12851 417 VALLRAVKALDK-LETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLRE----KPGGYGFNAATNEYGDLYAQ 491
|
570 580
....*....|....*....|....*....
gi 699669686 567 LVVQPLLV---------SLSALTLATETV 586
Cdd:PRK12851 492 GVIDPVKVvrtalqnaaSVAGLLLTTEAM 520
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
90-586 |
1.86e-15 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 79.38 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 90 PSQIRFSNISAGK------AVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVEL-----SKAQ 158
Cdd:PRK12850 3 AKEIRFSTDARDRllrgvnILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMvkevaSKTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 159 DIeAGDGTTSVVVIAGALLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVElsDRETLLNSATTSLNSkvvcq 238
Cdd:PRK12850 83 DL-AGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVT--SSKEIAQVATISANG----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 239 yssllspmsvdavmkvidpttansvdlrDIKIVKKLGGTIDdcelveglvltqKVANTGVTRVEKAK-IGL-------IQ 310
Cdd:PRK12850 155 ----------------------------DESIGEMIAEAMD------------KVGKEGVITVEEAKtLGTeldvvegMQ 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 311 FclsapktdmDNQIV----VSDYAQMDRVLreERAYIL-------------NLVKQIKKAGCNVLLIQKSILRDALSDLA 373
Cdd:PRK12850 195 F---------DRGYLspyfVTNPEKMRAEL--EDPYILlhekkisnlqdllPILEAVVQSGRPLLIIAEDVEGEALATLV 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 374 LHFLNK-MKIMVVK--------DIERDDI------EFICKTIGTKpvahIDQFTPDMLGSAE--LAEEVN---LNGSGKL 433
Cdd:PRK12850 264 VNKLRGgLKSVAVKapgfgdrrKAMLEDIavltggQVISEDLGIK----LENVTLDMLGRAKrvLITKENttiIDGAGDK 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 434 IKITGCTN-------------------------PGKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKrALIAGGGap 488
Cdd:PRK12850 340 KNIEARVKqiraqieettsdydreklqerlaklAGGVAVIRVGGATEVEVKEKKDRVDDALHATRAAVEE-GIVPGGG-- 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 489 eielaLRLNEYARTLRGMDSycvrAYGD----------ALEVIPSTLAENAGLNP---ISTVTELRNRHaqgektaGINV 555
Cdd:PRK12850 417 -----VALLRARSALRGLKG----ANADetagidivrrALEEPLRQIATNAGFEGsvvVGKVAELPGNF-------GFNA 480
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 699669686 556 RKGGISNILEELVVQPLLV---------SLSALTLATETV 586
Cdd:PRK12850 481 QTGEYGDMVEAGIIDPAKVtrtalqdaaSIAALLITTEAM 520
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
90-233 |
1.11e-14 |
|
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES cytosolic chaperonin. It is found in bacteria, organelles derived from bacteria, and occasionally in the Archaea. The bacterial GroEL/GroES group I chaperonin is replaced a group II chaperonin, usually called the thermosome in the Archaeota and CCT (chaperone-containing TCP) in the Eukaryota. GroEL, thermosome subunits, and CCT subunits all fall under the scope of pfam00118. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274089 Cd Length: 524 Bit Score: 76.95 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 90 PSQIRFSN-----ISAG-KAVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHP----AAKMLVEL-SKAQ 158
Cdd:TIGR02348 1 AKQIKFDEearkaLLRGvDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVaSKTN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 699669686 159 DIeAGDGTTSVVVIAGALLDACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVElsDRETLLNSATTSLNS 233
Cdd:TIGR02348 81 DV-AGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVK--GKKEIAQVATISANN 152
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
105-590 |
9.13e-13 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 70.90 E-value: 9.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 105 ADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVEL-----SKAQDIeAGDGTTSVVVIAGALLDA 179
Cdd:CHL00093 23 AEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALirqaaSKTNDV-AGDGTTTATVLAYAIVKQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 180 CSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVElsDRETLLNSATTSL-NSKVVCQyssllspMSVDAVMKVidpt 258
Cdd:CHL00093 102 GMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVE--DIQAITQVASISAgNDEEVGS-------MIADAIEKV---- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 259 tansvdLRDIKIVKKLG-GTIDDCELVEGLvltqkvantgvtRVEKAKIgliqfclsAPktdmdnqIVVSDYAQMDRVLr 337
Cdd:CHL00093 169 ------GREGVISLEEGkSTVTELEITEGM------------RFEKGFI--------SP-------YFVTDTERMEVVQ- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 338 eERAYIL------NLVKQ--------IKKAGCNVLLIQKSILRDALSDLalhFLNKMK--IMVVK-------DIERDDIE 394
Cdd:CHL00093 215 -ENPYILltdkkiTLVQQdllpileqVTKTKRPLLIIAEDVEKEALATL---VLNKLRgiVNVVAvrapgfgDRRKAMLE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 395 FICKTIGTKPVAH-----IDQFTPDMLGSA--------------------------ELAEEVNLNGSG--------KLIK 435
Cdd:CHL00093 291 DIAILTGGQVITEdaglsLETIQLDLLGQArriivtkdsttiiadgneeqvkarceQLRKQIEIADSSyekeklqeRLAK 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 436 ITGctnpGKTVtIVVRGSNKLVLEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELALRLNEYART-LRGMDSYCVRAY 514
Cdd:CHL00093 371 LSG----GVAV-IKVGAATETEMKDKKLRLEDAINATKAAVEE-GIVPGGGATLVHLSENLKTWAKNnLKEDELIGALIV 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 699669686 515 GDALEVIPSTLAENAGLNPISTVTELRNRhaqgEKTAGINVRKGGISNILEELVVQPLLVSLSALTLATETVRSIL 590
Cdd:CHL00093 445 ARAILAPLKRIAENAGKNGSVIIEKVQEQ----DFEIGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMIL 516
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
104-579 |
9.35e-13 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 71.03 E-value: 9.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 104 VADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVL----HPAAKMLVEL-SKAQDIeAGDGTTSVVVIAGALLD 178
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVaSKTNDL-AGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 179 ACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVELSdrETLLNSATTSLNSkvvcqyssllspmsvdavmkvidpt 258
Cdd:PRK12852 102 EGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASS--AEIAQVGTISANG------------------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 259 tansvdlrDIKIVKKLGGTIddcelveglvltQKVANTGVTRVEKAKigliqfclsapktDMDNQIVVSDYAQMDR---- 334
Cdd:PRK12852 155 --------DAAIGKMIAQAM------------QKVGNEGVITVEENK-------------SLETEVDIVEGMKFDRgyls 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 335 ----------VLREERAYIL-------------NLVKQIKKAGCNVLLIQKSILRDALSDLALHFLNK-MKIMVVK---- 386
Cdd:PRK12852 202 pyfvtnaekmTVELDDAYILlhekklsglqamlPVLEAVVQSGKPLLIIAEDVEGEALATLVVNRLRGgLKVAAVKapgf 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 387 -DIERDDIEFICKTIGTKPVAH-----IDQFTPDMLGSAE--LAEEVN---LNGSGKLIKITGCTN-------------- 441
Cdd:PRK12852 282 gDRRKAMLEDIAILTGGQLISEdlgikLENVTLKMLGRAKkvVIDKENttiVNGAGKKADIEARVGqikaqieettsdyd 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 442 -----------PGKTVTIVVRGSNKLVLEEAERSIHDALCVIRCLVKKrALIAGGGAPeielALRLNEYARTLRGMDS-- 508
Cdd:PRK12852 362 reklqerlaklAGGVAVIRVGGATEVEVKEKKDRVEDALNATRAAVQE-GIVPGGGVA----LLRAKKAVGRINNDNAdv 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 699669686 509 -YCVRAYGDALEVIPSTLAENAGLNPISTVTELRNRHAQgekTAGINVRKGGISNILEELVVQPLLVSLSAL 579
Cdd:PRK12852 437 qAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSE---TFGFDAQTEEYVDMVAKGIIDPAKVVRTAL 505
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
103-233 |
1.05e-12 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 70.54 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 103 AVADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVEL-----SKAQDIeAGDGTTSVVVIAGALL 177
Cdd:PRK00013 21 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLvkevaSKTNDV-AGDGTTTATVLAQAIV 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 699669686 178 DACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVElsDRETLLNSATTSLNS 233
Cdd:PRK00013 100 REGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVE--DKEEIAQVATISANG 153
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
104-219 |
8.12e-10 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 61.48 E-value: 8.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 104 VADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQVLHPAAKMLVEL-----SKAQDIeAGDGTTSVVVIAGALLD 178
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLvrqaaAKTNDL-AGDGTTTSVVLAQGLIA 156
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 699669686 179 ACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVELSD 219
Cdd:PLN03167 157 EGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE 197
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
104-586 |
1.60e-08 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 57.35 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 104 VADAIRTSLGPKGMDKMIQDAKGDVTITNDGATILKQMQV----LHPAAKMLVEL-SKAQDIeAGDGTTSVVVIAGALLD 178
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVaSKSADA-AGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 179 ACSRLLQKGIHPTIISESFQKALDKGIEVLSNMAQPVelSDRETLLNSATTSLNSkvvcqySSLLSPMSVDAVMKVIDPT 258
Cdd:PRK14104 102 EGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKV--TSNDEIAQVGTISANG------DAEIGKFLADAMKKVGNEG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 259 TANSVDLRDIKIvkklggtidDCELVEGLVLTQK-VANTGVTRVEKAKIgliqfclsapktDMDNQIVVSDYAQMDRvLR 337
Cdd:PRK14104 174 VITVEEAKSLET---------ELDVVEGMQFDRGyISPYFVTNADKMRV------------EMDDAYILINEKKLSS-LN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 338 EerayILNLVKQIKKAGCNVLLIQKSILRDALSDLALHFL-NKMKIMVVK-----DIERDDIEFICKTIGTKPVAH---- 407
Cdd:PRK14104 232 E----LLPLLEAVVQTGKPLVIVAEDVEGEALATLVVNRLrGGLKVAAVKapgfgDRRKAMLQDIAILTGGQAISEdlgi 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 408 -IDQFTPDMLGSAE--LAEEVN---LNGSGKLIKITGCTN-------------------------PGKTVTIVVRGSNKL 456
Cdd:PRK14104 308 kLENVTLQMLGRAKkvMIDKENttiVNGAGKKADIEARVAqikaqieettsdydreklqerlaklAGGVAVIRVGGATEV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699669686 457 VLEEAERSIHDALCVIRCLVKKRALIAGGGApeielALRLNEYARTLRGMD---SYCVRAYGDALEVIPSTLAENAGLNP 533
Cdd:PRK14104 388 EVKERKDRVDDAMHATRAAVEEGIVPGGGVA-----LLRASEQLKGIKTKNddqKTGVEIVRKALSAPARQIAINAGEDG 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 699669686 534 ISTVTELRNRHaqgEKTAGINVRKGGISNILEELVVQPLLV---------SLSALTLATETV 586
Cdd:PRK14104 463 SVIVGKILEKE---QYSYGFDSQTGEYGNLVSKGIIDPTKVvrtaiqnaaSVAALLITTEAM 521
|
|
| |
