|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
5-523 |
0e+00 |
|
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: 988.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 5 PIILLKDGTENKQGKGQIISNINACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDIAR 84
Cdd:cd03340 1 PIILLKEGTDTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 85 SQDAEVGDGTTSVVVLAAEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGET--ELREMLVKCAATTLS 162
Cdd:cd03340 81 SQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDkeEQRELLEKCAATALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 163 SKLVSQERLFFANMIVDAVNTLDAHLPLNMIGIKKVNGGNLHESRLIKGVAFQKAFSYAGFEMQPKKYSNVKVALLNIEL 242
Cdd:cd03340 161 SKLIASEKEFFAKMVVDAVLSLDDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAGFEQQPKKFKNPKILLLNVEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 243 ELKAEKENAEMRLTNVSDFQAVVDAEWNILYDKLQKIHDSGANVVLSKLPIGDVATQWFADRDMFCAGRIPQDDLDRLMS 322
Cdd:cd03340 241 ELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 323 ACGGSVLTTVSQIDDSVLGKCGKFYEQQVGSERYNFFEDCSKAQACTLLLRGGAEQFIAETERSLHDAIMIVRRAKKNDS 402
Cdd:cd03340 321 ATGGSIQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 403 IVAGGGAIEMELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHAQGE-KWAGIDIHREA 481
Cdd:cd03340 401 VVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGgKWYGVDINNEG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 17564182 482 VGDNLVACVWEPSIVKRNAITAATEAACLVLSIDQTVKNVRT 523
Cdd:cd03340 481 IADNFEAFVWEPSLVKINALTAATEAACLILSVDETIKNPKS 522
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
3-520 |
0e+00 |
|
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: 803.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 3 RPPIILLKDGTENKQGKGQIISNINACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDI 82
Cdd:TIGR02345 1 RPTIVLLKEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 83 ARSQDAEVGDGTTSVVVLAAEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGET-ELREMLVKCAATTL 161
Cdd:TIGR02345 81 AKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgEQRELLEKCAATAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 162 SSKLVSQERLFFANMIVDAVNTLDAH-LPLNMIGIKKVNGGNLHESRLIKGVAFQKAFSYAGFEMQPKKYSNVKVALLNI 240
Cdd:TIGR02345 161 SSKLISHNKEFFSKMIVDAVLSLDRDdLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAGFEQQPKKFANPKILLLNV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 241 ELELKAEKENAEMRLTNVSDFQAVVDAEWNILYDKLQKIHDSGANVVLSKLPIGDVATQWFADRDMFCAGRIPQDDLDRL 320
Cdd:TIGR02345 241 ELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 321 MSACGGSVLTTVSQIDDSVLGKCGKFYEQQVGSERYNFFEDCSKAQACTLLLRGGAEQFIAETERSLHDAIMIVRRAKKN 400
Cdd:TIGR02345 321 IKACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 401 DSIVAGGGAIEMELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHAQGEKWAGIDIHRE 480
Cdd:TIGR02345 401 KKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTE 480
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 17564182 481 AVGDNLVACVWEPSIVKRNAITAATEAACLVLSIDQTVKN 520
Cdd:TIGR02345 481 DIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITN 520
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
32-519 |
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: 569.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 32 VADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDIARSQDAEVGDGTTSVVVLAAEILKQMKPF 111
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 112 IEDGVHPQLLIRAIGKACEKTLKNLADLeIKINGETELREMLVKCAATTLSSKLVSQERLFFANMIVDAVNTL---DAHL 188
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSI-ISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIpknDGSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 189 PLNMIGIKKVNGGNLHESRLIKGVAFQKAFSYagfEMQPKKYSNVKVALLNIELELKAEKENAEMRLTNVSDFQAVVDAE 268
Cdd:pfam00118 160 DLGNIGVVKILGGSLEDSELVDGVVLDKGPLH---PDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 269 WNILYDKLQKIHDSGANVVLSKLPIGDVATQWFADRDMFCAGRIPQDDLDRLMSACGGSVLTTVSQIDDSVLGKCGKFYE 348
Cdd:pfam00118 237 EEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 349 QQVGSERYNFFEDCSKAQACTLLLRGGAEQFIAETERSLHDAIMIVRRAKKNDSIVAGGGAIEMELSRLIREHSKGIEGK 428
Cdd:pfam00118 317 EKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 429 DQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHAQGEKWAGIDIHREAVGDNLVACVWEPSIVKRNAITAATEAA 508
Cdd:pfam00118 397 EQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAA 476
|
490
....*....|.
gi 17564182 509 CLVLSIDQTVK 519
Cdd:pfam00118 477 STILRIDDIIK 487
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
13-519 |
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: 537.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 13 TENKQGKGQIISNINACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDIARSQDAEVGD 92
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 93 GTTSVVVLAAEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGETelREMLVKCAATTLSSKLVSQERLF 172
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVED--REELLKVATTSLNSKLVSGGDDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 173 FANMIVDAVNTL---DAHLPLNMIGIKKVNGGNLHESRLIKGVAFQKAFSYAGFemqPKKYSNVKVALLNIELElkaeke 249
Cdd:cd00309 159 LGELVVDAVLKVgkeNGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYM---PKRLENAKILLLDCKLE------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 250 naemrltnvsdfqavvdaewnilydklqkihdsgaNVVLSKLPIGDVATQWFADRDMFCAGRIPQDDLDRLMSACGGSVL 329
Cdd:cd00309 230 -----------------------------------YVVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 330 TTVSQIDDSVLGKCGKFYEQQVGSERYNFFEDCSKAQACTLLLRGGAEQFIAETERSLHDAIMIVRRAKKNDSIVAGGGA 409
Cdd:cd00309 275 SRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 410 IEMELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHAQGEKWAGIDIHREAVGDNLVAC 489
Cdd:cd00309 355 AEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKEAG 434
|
490 500 510
....*....|....*....|....*....|
gi 17564182 490 VWEPSIVKRNAITAATEAACLVLSIDQTVK 519
Cdd:cd00309 435 IIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
5-515 |
2.29e-155 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 453.57 E-value: 2.29e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 5 PIILLKDGTENKQGKGQIISNINACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDIAR 84
Cdd:NF041082 2 PILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 85 SQDAEVGDGTTSVVVLAAEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGETelREMLVKCAATTLSSK 164
Cdd:NF041082 82 TQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDD--KETLKKIAATAMTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 165 LVSQERLFFANMIVDAVNTL-----DAHLPLNMIGIKKVNGGNLHESRLIKGVAFQKAFSYAGfeMqPKKYSNVKVALLN 239
Cdd:NF041082 160 GAEAAKDKLADLVVDAVKAVaekdgGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPG--M-PKRVENAKIALLD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 240 IELELKAEKENAEMRLTNVSDFQAVVDAEWNILYDKLQKIHDSGANVVLSKLPIGDVATQWFADRDMFCAGRIPQDDLDR 319
Cdd:NF041082 237 APLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 320 LMSACGGSVLTTVSQIDDSVLGKCGKFYEQQVGSERYNFFEDCSKAQACTLLLRGGAEQFIAETERSLHDAIMIVRRAKK 399
Cdd:NF041082 317 LAKATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 400 NDSIVAGGGAIEMELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHAQGEKWAGIDIHR 479
Cdd:NF041082 397 DGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYT 476
|
490 500 510
....*....|....*....|....*....|....*.
gi 17564182 480 EAVGDNLVACVWEPSIVKRNAITAATEAACLVLSID 515
Cdd:NF041082 477 GKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRID 512
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
5-515 |
6.91e-153 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 447.47 E-value: 6.91e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 5 PIILLKDGTENKQGKGQIISNINACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDIAR 84
Cdd:NF041083 2 PVLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 85 SQDAEVGDGTTSVVVLAAEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGETelREMLVKCAATTLSSK 164
Cdd:NF041083 82 TQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDD--RETLKKIAETSLTSK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 165 LVSQERLFFANMIVDAVNTL------DAHLPLNMIGIKKVNGGNLHESRLIKGVAFQKAFSYAGFemqPKKYSNVKVALL 238
Cdd:NF041083 160 GVEEARDYLAEIAVKAVKQVaekrdgKYYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGM---PKRVENAKIALL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 239 NIELELKAEKENAEMRLTNVSDFQAVVDAEWNILYDKLQKIHDSGANVVLSKLPIGDVATQWFADRDMFCAGRIPQDDLD 318
Cdd:NF041083 237 DAPLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDME 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 319 RLMSACGGSVLTTVSQIDDSVLGKCGKFYEQQVGSERYNFFEDCSKAQACTLLLRGGAEQFIAETERSLHDAIMIVRRAK 398
Cdd:NF041083 317 KLAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 399 KNDSIVAGGGAIEMELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHAQGEKWAGIDIH 478
Cdd:NF041083 397 EDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVF 476
|
490 500 510
....*....|....*....|....*....|....*..
gi 17564182 479 REAVGDNLVACVWEPSIVKRNAITAATEAACLVLSID 515
Cdd:NF041083 477 TGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRID 513
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
5-515 |
6.77e-152 |
|
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: 444.90 E-value: 6.77e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 5 PIILLKDGTENKQGKGQIISNINACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDIAR 84
Cdd:TIGR02339 1 PVFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 85 SQDAEVGDGTTSVVVLAAEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGETelREMLVKCAATTLSSK 164
Cdd:TIGR02339 81 TQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPED--RDLLKKIAYTSLTSK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 165 LVSQERL-FFANMIVDAVNTLDAHLP-------LNMIGIKKVNGGNLHESRLIKGVAFQKAFSYAGFemqPKKYSNVKVA 236
Cdd:TIGR02339 159 ASAEVAKdKLADLVVEAVKQVAELRGdgkyyvdLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGM---PKRVENAKIA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 237 LLNIELELKAEKENAEMRLTNVSDFQAVVDAEWNILYDKLQKIHDSGANVVLSKLPIGDVATQWFADRDMFCAGRIPQDD 316
Cdd:TIGR02339 236 LLDAPLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 317 LDRLMSACGGSVLTTVSQIDDSVLGKCGKFYEQQVGSERYNFFEDCSKAQACTLLLRGGAEQFIAETERSLHDAIMIVRR 396
Cdd:TIGR02339 316 IEKLARATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVAN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 397 AKKNDSIVAGGGAIEMELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHAQGEKWAGID 476
Cdd:TIGR02339 396 ALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGIN 475
|
490 500 510
....*....|....*....|....*....|....*....
gi 17564182 477 IHREAVGDNLVACVWEPSIVKRNAITAATEAACLVLSID 515
Cdd:TIGR02339 476 VFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRID 514
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
6-515 |
1.93e-151 |
|
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: 443.63 E-value: 1.93e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 6 IILLKDGTENKQGKGQIISNINACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDIARS 85
Cdd:cd03343 1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 86 QDAEVGDGTTSVVVLAAEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGETelREMLVKCAATTLSSKL 165
Cdd:cd03343 81 QDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDD--KDTLRKIAKTSLTGKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 166 VSQERLFFANMIVDAVNTL------DAHLPLNMIGIKKVNGGNLHESRLIKGVAFQKAFSYAGFemqPKKYSNVKVALLN 239
Cdd:cd03343 159 AEAAKDKLADLVVDAVLQVaekrdgKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGM---PKRVENAKIALLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 240 IELELKAEKENAEMRLTNVSDFQAVVDAEWNILYDKLQKIHDSGANVVLSKLPIGDVATQWFADRDMFCAGRIPQDDLDR 319
Cdd:cd03343 236 APLEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 320 LMSACGGSVLTTVSQIDDSVLGKCGKFYEQQVGSERYNFFEDCSKAQACTLLLRGGAEQFIAETERSLHDAIMIVRRAKK 399
Cdd:cd03343 316 LARATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 400 NDSIVAGGGAIEMELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHAQGEKWAGIDIHR 479
Cdd:cd03343 396 DGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYT 475
|
490 500 510
....*....|....*....|....*....|....*.
gi 17564182 480 EAVGDNLVACVWEPSIVKRNAITAATEAACLVLSID 515
Cdd:cd03343 476 GEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRID 511
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
25-519 |
1.94e-125 |
|
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: 377.40 E-value: 1.94e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 25 NINACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDIARSQDAEVGDGTTSVVVLAAEI 104
Cdd:cd03335 13 NVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 105 LKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADlEIKINGETELREMLVKCAATTLSSKLVSQERLFFANMIVDAVNTL 184
Cdd:cd03335 93 LKRANELVKQKIHPTTIISGYRLACKEAVKYIKE-HLSISVDNLGKESLINVAKTSMSSKIIGADSDFFANMVVDAILAV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 185 -------DAHLPLNMIGIKKVNGGNLHESRLIKGVAFQKafSYAGFEMqPKKYSNVKVALLNIELELKAEKENAEMRLTN 257
Cdd:cd03335 172 kttnekgKTKYPIKAVNILKAHGKSAKESYLVNGYALNC--TRASQGM-PTRVKNAKIACLDFNLQKTKMKLGVQVVVTD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 258 VSDFQAVVDAEWNILYDKLQKIHDSGANVVLSKLPIGDVATQWFADRDMFCAGRIPQDDLDRLMSACGGSVLTTVSQI-- 335
Cdd:cd03335 249 PEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVSTLANLeg 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 336 ----DDSVLGKCGKFYEQQVGSERYNFFEDCSKAQACTLLLRGGAEQFIAETERSLHDAIMIVRRAKKNDSIVAGGGAIE 411
Cdd:cd03335 329 eetfDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGGAVE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 412 MELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHA--------QGEKWAGIDIHREAVG 483
Cdd:cd03335 409 TALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAaaqvkpdkKHLKWYGLDLINGKVR 488
|
490 500 510
....*....|....*....|....*....|....*.
gi 17564182 484 DNLVACVWEPSIVKRNAITAATEAACLVLSIDQTVK 519
Cdd:cd03335 489 DNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
12-519 |
5.78e-120 |
|
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: 363.66 E-value: 5.78e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 12 GTENKQGKGQIISNINACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDIARSQDAEVG 91
Cdd:TIGR02340 4 GGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 92 DGTTSVVVLAAEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADlEIKINGETELREMLVKCAATTLSSKLVSQERL 171
Cdd:TIGR02340 84 DGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKE-NLSVSVDELGREALINVAKTSMSSKIIGLDSD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 172 FFANMIVDAVNTL-------DAHLPLNMIGIKKVNGGNLHESRLIKGVAFQKafSYAGFEMqPKKYSNVKVALLNIELEL 244
Cdd:TIGR02340 163 FFSNIVVDAVLAVkttnengETKYPIKAINILKAHGKSARESMLVKGYALNC--TVASQQM-PKRIKNAKIACLDFNLQK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 245 KAEKENAEMRLTNVSDFQAVVDAEWNILYDKLQKIHDSGANVVLSKLPIGDVATQWFADRDMFCAGRIPQDDLDRLMSAC 324
Cdd:TIGR02340 240 AKMALGVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKAT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 325 GGSVLTTVSQI------DDSVLGKCGKFYEQQVGSERYNFFEDCSKAQACTLLLRGGAEQFIAETERSLHDAIMIVRRAK 398
Cdd:TIGR02340 320 GATLVSTLADLegeetfEASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 399 KNDSIVAGGGAIEMELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHA--------QGE 470
Cdd:TIGR02340 400 ESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAaaqlkpekKHL 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 17564182 471 KWAGIDIHREAVGDNLVACVWEPSIVKRNAITAATEAACLVLSIDQTVK 519
Cdd:TIGR02340 480 KWYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIK 528
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
5-518 |
2.12e-114 |
|
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: 347.36 E-value: 2.12e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 5 PIILLKDGTENKQGKGQIISNINACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDIAR 84
Cdd:cd03337 1 PVLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 85 SQDAEVGDGTTSVVVLAAEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINgeTELREMLVKCAATTLSSK 164
Cdd:cd03337 81 TQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVD--VNDRAQMLKIIKSCIGTK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 165 LVSQERLFFANMIVDAVNTldAHLPLNM----IGIK------KVNGGNLHESRLIKGVAFQKAFSYAGfeMQpKKYSNVK 234
Cdd:cd03337 159 FVSRWSDLMCNLALDAVKT--VAVEENGrkkeIDIKryakveKIPGGEIEDSRVLDGVMLNKDVTHPK--MR-RRIENPR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 235 VALLNIELElkaekenaemrltnvsdfqavvdaewnilYdklqkihdsganVVLSKLPIGDVATQWFADRDMFCAGRIPQ 314
Cdd:cd03337 234 IVLLDCPLE-----------------------------Y------------LVITEKGVSDLAQHYLVKAGITALRRVRK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 315 DDLDRLMSACGGSVLTTVSQIDDSVLGKCGKFYE-QQVGSERYNFFEDCSKAQACTLLLRGGAEQFIAETERSLHDAIMI 393
Cdd:cd03337 273 TDNNRIARACGATIVNRPEELTESDVGTGAGLFEvKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 394 VRRAKKNDSIVAGGGAIEMELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHAQGEKWA 473
Cdd:cd03337 353 ARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENST 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 17564182 474 -GIDIHREAVGDNLVACVWEPSIVKRNAITAATEAACLVLSIDQTV 518
Cdd:cd03337 433 wGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
24-518 |
3.28e-113 |
|
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: 345.43 E-value: 3.28e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 24 SNINACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDIARSQDAEVGDGTTSVVVLAAE 103
Cdd:cd03338 12 SNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 104 ILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKIngETELREMLVKCAATTLSSKLVSQERLFFANMIVDAV-- 181
Cdd:cd03338 92 LLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPV--DLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVlk 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 182 ---NTLDAHLPLNMIGIKKVNGGNLHESRLIKGVAF-QKAFSYAGfemQPKKYSNVKVALlnIELELKAEKENAEMRLTn 257
Cdd:cd03338 170 vidPATATNVDLKDIRIVKKLGGTIEDTELVDGLVFtQKASKKAG---GPTRIEKAKIGL--IQFCLSPPKTDMDNNIV- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 258 VSDFQA---VVDAEWNILYDKLQKIHDSGANVVL---SKL--PIGDVATQWFADRDMFCAGRIPQDDLDRLMSACGGSVL 329
Cdd:cd03338 244 VNDYAQmdrILREERKYILNMCKKIKKSGCNVLLiqkSILrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 330 TTVSQIDDSVLGKCGKFYEQQVGSERYNFFEDC-SKAQACTLLLRGGAEQFIAETERSLHDAIMIVRRAKKNDSIVAGGG 408
Cdd:cd03338 324 ASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVkNPGKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 409 AIEMELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHAQGEKWAGIDIHREAVGDNLVA 488
Cdd:cd03338 404 APEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITNILEE 483
|
490 500 510
....*....|....*....|....*....|
gi 17564182 489 CVWEPSIVKRNAITAATEAACLVLSIDQTV 518
Cdd:cd03338 484 NVVQPLLVSTSAITLATETVRMILKIDDIV 513
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
5-522 |
2.58e-111 |
|
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: 340.95 E-value: 2.58e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 5 PIILLKDGTENKQGKGQIISNINACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDIAR 84
Cdd:TIGR02344 1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 85 SQDAEVGDGTTSVVVLAAEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINgeTELREMLVKCAATTLSSK 164
Cdd:TIGR02344 81 TQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVD--VNDDAAMLKLIQSCIGTK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 165 LVSQERLFFANMIVDAVNTLDAHLPLNM-IGIK------KVNGGNLHESRLIKGVAFQKAFSYAgfEMQpKKYSNVKVAL 237
Cdd:TIGR02344 159 FVSRWSDLMCDLALDAVRTVQRDENGRKeIDIKryakveKIPGGDIEDSCVLKGVMINKDVTHP--KMR-RYIENPRIVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 238 LNIELELKAEKENAEMRLTNVSDFQAVVDAEWNILYDKLQKIHDSGANVVLSKLPIGDVATQWFADRDMFCAGRIPQDDL 317
Cdd:TIGR02344 236 LDCPLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 318 DRLMSACGGSVLTTVSQIDDSVLG-KCGKFYEQQVGSERYNFFEDCSKAQACTLLLRGGAEQFIAETERSLHDAIMIVRR 396
Cdd:TIGR02344 316 NRIARACGATIVNRPEELRESDVGtGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 397 AKKNDSIVAGGGAIEMELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHAQGEK-WAGI 475
Cdd:TIGR02344 396 VLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNcTWGI 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 17564182 476 DIHREAVGDNLVACVWEPSIVKRNAITAATEAACLVLSIDQTVKNVR 522
Cdd:TIGR02344 476 DGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVSGVK 522
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-521 |
2.43e-110 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 338.54 E-value: 2.43e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 1 MMRPPIILLKDGTENKQGKGQIISNINACQVVADSIRTTLGPRGLDKLIVDSK-----GATTISNDGATILKLLDIVFPA 75
Cdd:PTZ00212 3 MANVPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMSegprsGNVTVTNDGATILKSVWLDNPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 76 ASTMVDIARSQDAEVGDGTTSVVVLAAEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADL-EIKINGETELREMLV 154
Cdd:PTZ00212 83 AKILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIaFDHGSDEEKFKEDLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 155 KCAATTLSSKLVSQERLFFANMIVDAVNTLDAHLPLNMIGIKKVNGGNLHESRLIKGVAFQKAFSYAgfemQPKKYSNVK 234
Cdd:PTZ00212 163 NIARTTLSSKLLTVEKDHFAKLAVDAVLRLKGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVG----QPKRLENCK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 235 VALLNIELEL-KAEKENAEMRLTNVSDFQAVVDAEWNILYDKLQKIHDSGANVVLSKLPIGDVATQWFADRDMFCAGRIP 313
Cdd:PTZ00212 239 ILVANTPMDTdKIKIYGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHAD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 314 QDDLDRLMSACGGSVLTTVSQIDDSVLGKCGKFYEQQVGSERYNFFEDCSKAQACTLLLRGGAEQFIAETERSLHDAIMI 393
Cdd:PTZ00212 319 FDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 394 VRRAKKNDSIVAGGGAIEMELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHAQGEKWA 473
Cdd:PTZ00212 399 LSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTA 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 17564182 474 GIDIHREAVGDNLVACVWEPSIVKRNAITAATEAACLVLSIDQTVKNV 521
Cdd:PTZ00212 479 GIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRCA 526
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
24-518 |
4.87e-103 |
|
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: 319.42 E-value: 4.87e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 24 SNINACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDIARSQDAEVGDGTTSVVVLAAE 103
Cdd:TIGR02342 13 SNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 104 ILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKIngETELREMLVKCAATTLSSKLVSQERLFFANMIVDAVNT 183
Cdd:TIGR02342 93 LLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPV--DLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVLK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 184 L-----DAHLPLNMIGIKKVNGGNLHESRLIKGVAF-QKAFSYAGfemQPKKYSNVKVALlnIELELKAEKENAEMRLTn 257
Cdd:TIGR02342 171 VidpenAKNVDLNDIKVVKKLGGTIDDTELIEGLVFtQKASKSAG---GPTRIEKAKIGL--IQFQISPPKTDMENQII- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 258 VSDFQA---VVDAEWNILYDKLQKIHDSGANVVLSKLPI-----GDVATQWFADRDMFCAGRIPQDDLDRLMSACGGSVL 329
Cdd:TIGR02342 245 VNDYAQmdrVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 330 TTVSQIDDSVLGKCGKFYEQQVGSERYNFFEDC-SKAQACTLLLRGGAEQFIAETERSLHDAIMIVRRAKKNDSIVAGGG 408
Cdd:TIGR02342 325 ASIDHFTADKLGSAELVEEVDSDGGKIIKITGIqNAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 409 AIEMELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHAQGEKWAGIDIHREAVGDNLVA 488
Cdd:TIGR02342 405 APEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITNMLEE 484
|
490 500 510
....*....|....*....|....*....|
gi 17564182 489 CVWEPSIVKRNAITAATEAACLVLSIDQTV 518
Cdd:TIGR02342 485 HVLQPLLVTTSAITLASETVRSILKIDDIV 514
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
9-519 |
2.22e-102 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239452 [Multi-domain] Cd Length: 517 Bit Score: 317.73 E-value: 2.22e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 9 LKDGTENKQGKGQIISNINACQVVADSIRTTLGPRGLDKLI--VDSKGATTISNDGATILKLLDIVFPAASTMVDIARSQ 86
Cdd:cd03336 2 LKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 87 DAEVGDGTTSVVVLAAEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGETEL-REMLVKCAATTLSSKL 165
Cdd:cd03336 82 DDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEAfREDLLNIARTTLSSKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 166 VSQERLFFANMIVDAVNTLDAHLPLNMIGIKKVNGGNLHESRLIKGVAFQKAFSYAgfemQPKKYSNVKVALLNIELEL- 244
Cdd:cd03336 162 LTQDKEHFAELAVDAVLRLKGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVN----QPKRIENAKILIANTPMDTd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 245 KAEKENAEMRLTNVSDFQAVVDAEWNILYDKLQKIHDSGANVVLSKLPIGDVATQWFADRDMFCAGRIPQDDLDRLMSAC 324
Cdd:cd03336 238 KIKIFGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 325 GGSVLTTVSQIDDSVLGKCGKFYEQQVGSERYNFFEDCSKAQACTLLLRGGAEQFIAETERSLHDAIMIVRRAKKNDSIV 404
Cdd:cd03336 318 GGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRVV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 405 AGGGAIEMELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHAQGEKWAGIDIHREAVGD 484
Cdd:cd03336 398 LGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTVGD 477
|
490 500 510
....*....|....*....|....*....|....*
gi 17564182 485 NLVACVWEPSIVKRNAITAATEAACLVLSIDQTVK 519
Cdd:cd03336 478 MKELGITESFKVKRQVLLSASEAAEMILRVDDIIK 512
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
5-519 |
1.29e-101 |
|
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: 315.78 E-value: 1.29e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 5 PIILLKDGTENKQGKGQ--IISNINACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDI 82
Cdd:cd03339 6 PFIIVREQEKKKRLKGLeaHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 83 ARSQDAEVGDGTTSVVVLAAEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGETELREMLVKCAATTLS 162
Cdd:cd03339 86 SKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPDNKEPLIQTAMTSLG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 163 SKLVSQERLFFANMIVDAVNTLdAHLP-----LNMIGIKKVNGGNLHESRLIKGVAFQKAFSYAgfEMqPKKYSNVKVAL 237
Cdd:cd03339 166 SKIVSRCHRQFAEIAVDAVLSV-ADLErkdvnFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHP--QM-PKEVKDAKIAI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 238 LNIELELKAEKENAEMRLTNVSDFQAVVDAEWNILYDKLQKIHDSGANVVLSKLPIGDVATQWFADRDMFCAGRIPQDDL 317
Cdd:cd03339 242 LTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 318 DRLMSACGGSVLTTVSQIDDSVLGKCGKFYEQQVG--SERYNFFEDCSKAQACTLLLRGGAEQFIAETERSLHDAIMIVR 395
Cdd:cd03339 322 ELIAIATGGRIVPRFEDLSPEKLGKAGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 396 RAKKNDSIVAGGGAIEMELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRH-AQGEKWAG 474
Cdd:cd03339 402 NLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPHLG 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 17564182 475 IDIHREAVGDNLVACVWEPSIVKRNAITAATEAACLVLSIDQTVK 519
Cdd:cd03339 482 IDCLGRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
5-520 |
7.15e-99 |
|
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: 309.04 E-value: 7.15e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 5 PIILLKDGTENKQGKGQ--IISNINACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDI 82
Cdd:TIGR02343 10 PFIIIKDQDNKKRLKGLeaKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 83 ARSQDAEVGDGTTSVVVLAAEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGETELREMLVKCAATTLS 162
Cdd:TIGR02343 90 SKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREPLIQAAKTSLG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 163 SKLVSQERLFFANMIVDAV-NTLDAH---LPLNMIGIKKVNGGNLHESRLIKGVAFQKAFSYAgfEMqPKKYSNVKVALL 238
Cdd:TIGR02343 170 SKIVSKCHRRFAEIAVDAVlNVADMErrdVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHP--QM-PKEVEDAKIAIL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 239 NIELELKAEKENAEMRLTNVSDFQAVVDAEWNILYDKLQKIHDSGANVVLSKLPIGDVATQWFADRDMFCAGRIPQDDLD 318
Cdd:TIGR02343 247 TCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 319 RLMSACGGSVLTTVSQIDDSVLGKCGKFYEQQVGS--ERYNFFEDCSKAQACTLLLRGGAEQFIAETERSLHDAIMIVRR 396
Cdd:TIGR02343 327 LIAIATGGRIVPRFQELSKDKLGKAGLVREISFGTtkDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRN 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 397 AKKNDSIVAGGGAIEMELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHAQGEKWA-GI 475
Cdd:TIGR02343 407 LIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNlGV 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 17564182 476 DIHREAVGDNLVACVWEPSIVKRNAITAATEAACLVLSIDQTVKN 520
Cdd:TIGR02343 487 DCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVISP 531
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
20-518 |
1.02e-93 |
|
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: 293.74 E-value: 1.02e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 20 GQIISNINACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDIARSQDAEVGDGTTSVVV 99
Cdd:cd03341 8 EAVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 100 LAAEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGETELREMLVKCAATTLSSKLVSQErLFFANMIVD 179
Cdd:cd03341 88 LAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLRNKEEVSKALKTAIASKQYGNE-DFLSPLVAE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 180 AVNTLdahLPLNM-------IGIKKVNGGNLHESRLIKGVAFQKafsyaGFEMQPKKYSNVKVALLNIELELkaekenae 252
Cdd:cd03341 167 ACISV---LPENIgnfnvdnIRVVKILGGSLEDSKVVRGMVFKR-----EPEGSVKRVKKAKVAVFSCPFDI-------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 253 mrltnvsdfqavvdaewnilydklqkihdsGANVVLSKLPIGDVAtQWFADRDMFCAGRIPQD-DLDRLMSACGGSVLTT 331
Cdd:cd03341 231 ------------------------------GVNVIVAGGSVGDLA-LHYCNKYGIMVIKINSKfELRRLCRTVGATPLPR 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 332 VSQIDDSVLGKCGKFYEQQVGSERYNFFEDC-SKAQACTLLLRGGAEQFIAETERSLHDAIMIVRRAKKNDSIVAGGGAI 410
Cdd:cd03341 280 LGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNkEDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGAT 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 411 EMELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHAQGEKWAGIDIHR--EAVGDNLVA 488
Cdd:cd03341 360 EIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESgdEGTKDAKEA 439
|
490 500 510
....*....|....*....|....*....|
gi 17564182 489 CVWEPSIVKRNAITAATEAACLVLSIDQTV 518
Cdd:cd03341 440 GIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
8-531 |
3.05e-91 |
|
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: 289.31 E-value: 3.05e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 8 LLKDGTENKQG-KGQIISNINACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDIARSQ 86
Cdd:TIGR02346 5 LLKEGYRHFSGlEEAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 87 DAEVGDGTTSVVVLAAEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADL-EIKINGETELREmLVKCAATTLSSKL 165
Cdd:TIGR02346 85 ENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELvVWEVKDLRDKDE-LIKALKASISSKQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 166 VSQERlFFANMIVDAVNTL----DAHLPLNMIGIKKVNGGNLHESRLIKGVAFQKAfsyagFEMQPKKYSNVKVALLNIE 241
Cdd:TIGR02346 164 YGNED-FLAQLVAQACSTVlpknPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNRE-----AEGSVKSVKNAKVAVFSCP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 242 LELKAEKENAEMRLTNVSDFQAVVDAEWNILYDKLQKIHDSGANVVLSKLPIGDVAtQWFADRDMFCAGRIPQD-DLDRL 320
Cdd:TIGR02346 238 LDTATTETKGTVLIHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMA-LHYLNKYNIMVLKIPSKfELRRL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 321 MSACGGSVLTTVSQIDDSVLGKCGKFYEQQVGSERYNFFEDCSK-AQACTLLLRGGAEQFIAETERSLHDAIMIVRRAKK 399
Cdd:TIGR02346 317 CKTVGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGdSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 400 NDSIVAGGGAIEMELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHAQGEKWAGIDIHR 479
Cdd:TIGR02346 397 DGRLLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEA 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 17564182 480 EAVG--DNLVACVWEPSIVKRNAITAATEAACLVLSIDQTVknVRTPSGGAMPG 531
Cdd:TIGR02346 477 ESDGvkDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQII--MAKPAGGPKPP 528
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
8-519 |
7.39e-86 |
|
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: 274.81 E-value: 7.39e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 8 LLKDGTENKQGKGQIISNINACQVVADSIRTTLGPRGLDKLIV--DSKGATTISNDGATILKLLDIVFPAASTMVDIARS 85
Cdd:TIGR02341 2 IFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 86 QDAEVGDGTTSVVVLAAEILKQMKPFIEDGVHPQLLI----RAIGKACEKTLKNLADleiKINGETELREMLVKCAATTL 161
Cdd:TIGR02341 82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIagyrEATKAARDALLKSAVD---NGSDEVKFRQDLMNIARTTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 162 SSKLVSQERLFFANMIVDAVNTLDAHLPLNMIGIKKVNGGNLHESRLIKGVAFQKAFSYagfeMQPKKYSNVKVALLNIE 241
Cdd:TIGR02341 159 SSKILSQHKDHFAQLAVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGV----NQPKRIENAKILIANTG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 242 LEL-KAEKENAEMRLTNVSDFQAVVDAEWNILYDKLQKIHDSGANVVLSKLPIGDVATQWFADRDMFCAGRIPQDDLDRL 320
Cdd:TIGR02341 235 MDTdKVKIFGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 321 MSACGGSVLTTVSQIDDSVLGKCGKFYEQQVGSERYNFFEDCSKAQACTLLLRGGAEQFIAETERSLHDAIMIVRRAKKN 400
Cdd:TIGR02341 315 ALVTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 401 DSIVAGGGAIEMELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHAQGEKWAGIDIHRE 480
Cdd:TIGR02341 395 SRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEG 474
|
490 500 510
....*....|....*....|....*....|....*....
gi 17564182 481 AVGDNLVACVWEPSIVKRNAITAATEAACLVLSIDQTVK 519
Cdd:TIGR02341 475 TIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIK 513
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
24-528 |
8.00e-86 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 273.88 E-value: 8.00e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 24 SNINACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFP----AASTMVDIARSQDAEVGDGTTSVVV 99
Cdd:COG0459 14 ANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTTTATV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 100 LAAEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGetelREMLVKCAATTLSSKlvsqERLffANMIVD 179
Cdd:COG0459 94 LAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDD----KEELAQVATISANGD----EEI--GELIAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 180 AVNTldahlplnmIGIKKV-----NGGNLHESRLIKGVAFQKAFSYAGF----EMQPKKYSNVKVALLNIELELKAEken 250
Cdd:COG0459 164 AMEK---------VGKDGVitveeGKGLETELEVVEGMQFDKGYLSPYFvtdpEKMPAELENAYILLTDKKISSIQD--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 251 aemrltnvsdfqavvdaewniLYDKLQKIHDSGANVVLSKLPIGDVATQWFADRDMF-----CAGRIP------QDDLDR 319
Cdd:COG0459 232 ---------------------LLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRgvlrvVAVKAPgfgdrrKAMLED 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 320 LMSACGGSVLT-----TVSQIDDSVLGKCGKFYeqqVGSERYNFFEDCSKAQACTLLLRGGAEQFIAETERSLHDAIMIV 394
Cdd:COG0459 291 IAILTGGRVISedlglKLEDVTLDDLGRAKRVE---VDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALHAT 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 395 RRAKKnDSIVAGGGAIEMELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRhrhAQGEKWAG 474
Cdd:COG0459 368 RAAVE-EGIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVR---AAKDKGFG 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 17564182 475 IDIHREAVGDNLVACVWEPSIVKRNAITAATEAACLVLSIDQTVKNVRTPSGGA 528
Cdd:COG0459 444 FDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
25-519 |
1.02e-80 |
|
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: 260.27 E-value: 1.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 25 NINACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDIARSQDAEVGDGTTSVVVLAAEI 104
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 105 LKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINgETELREMLVKCAATTLSSKLVSQERLFFANMIVDAVNTL 184
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVE-IDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 185 ---DAHLPLNMIGIKKVNGGNLHESRLIKGVAFQKAFSYAgfEMqPKKYSNVKVALLNIELELkaekENAEMrltNVSDF 261
Cdd:cd03342 176 ykpDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHP--DM-PKRVENAYILTCNVSLEY----EKTEV---NSGFF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 262 QAVVdaeWNilydklQKIHDSGANVVLSKLPIgdvatqwFADRdmfcagRIPQDDLDRLMSACGGSVLTTVSQIDDSVLG 341
Cdd:cd03342 246 YSVV---IN------QKGIDPPSLDMLAKEGI-------LALR------RAKRRNMERLTLACGGVAMNSVDDLSPECLG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 342 KCGKFYEQQVGSERYNFFEDCSKAQACTLLLRGGAEQFIAETERSLHDAIMIVRRAKKNDSIVAGGGAIEMELSRLIREH 421
Cdd:cd03342 304 YAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHLKEF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 422 SKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHAQGEKWAGIDIHREAVGDNLVACVWEPSIVKRNAI 501
Cdd:cd03342 384 KKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQIL 463
|
490
....*....|....*...
gi 17564182 502 TAATEAACLVLSIDQTVK 519
Cdd:cd03342 464 HSATVIASQLLLVDEIIR 481
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
25-519 |
2.92e-78 |
|
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: 255.43 E-value: 2.92e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 25 NINACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDIARSQDAEVGDGTTSVVVLAAEI 104
Cdd:TIGR02347 21 NINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 105 LKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGETElREMLVKCAATTLSSKLVSQERLFFANMIVDAVNTL 184
Cdd:TIGR02347 101 LKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEVD-REFLLNVARTSLRTKLPADLADQLTEIVVDAVLAI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 185 ---DAHLPLNMIGIKKVNGGNLHESRLIKGVAFQKAFSYAGFemqPKKYSNVKVALLNIELELKAEKENAEMRLTNVSDF 261
Cdd:TIGR02347 180 kkdGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDM---PRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 262 QAVVDAEWNILYDKLQKIHD-------SGAN---VVLSKLPIGDVATQWFADRDMFCAGRIPQDDLDRLMSACGGSVLTT 331
Cdd:TIGR02347 257 EKLVKAERKFVDDRVKKIIElkkkvcgKSPDkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEALNS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 332 VSQIDDSVLGKCGKFYEQQVGSERYNFFEDCSKAQACTLLLRGGAEQFIAETERSLHDAIMIVRRAKKNDSIVAGGGAIE 411
Cdd:TIGR02347 337 VEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAGAFE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 412 MELSRLIREHSKGIEGKDQAFWMAYGQAFEIIPRQLCQNAGLDALDVLNKLRHRHAQGEKWAGIDIHREAVGDNLVACVW 491
Cdd:TIGR02347 417 IAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGVDLNTGEPIDPEIKGIW 496
|
490 500
....*....|....*....|....*...
gi 17564182 492 EPSIVKRNAITAATEAACLVLSIDQTVK 519
Cdd:TIGR02347 497 DNYRVKKQLIQSATVIASQLLLVDEVMR 524
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
150-400 |
2.25e-60 |
|
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: 198.07 E-value: 2.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 150 REMLVKCAATTLSSKlVSQERLFFANMIVDAVNTL---DAHLPLNMIGIKKVNGGNLHESRLIKGVAFQKAFSYAGFemq 226
Cdd:cd03333 1 RELLLQVATTSLNSK-LSSWDDFLGKLVVDAVLKVgpdNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYM--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 227 PKKYSNVKVALLNIELElkaekenaemrltnvsdfqavvdaewnilydklqkihdsgaNVVLSKLPIGDVATQWFADRDM 306
Cdd:cd03333 77 PKRLENAKILLLDCPLE-----------------------------------------YVVIAEKGIDDLALHYLAKAGI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 307 FCAGRIPQDDLDRLMSACGGSVLTTVSQIDDSVLGKCGKFYEQQVGSERYNFFEDCSKAQACTLLLRGGAEQFIAETERS 386
Cdd:cd03333 116 MAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRS 195
|
250
....*....|....
gi 17564182 387 LHDAIMIVRRAKKN 400
Cdd:cd03333 196 LHDALCAVRAAVEE 209
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
29-150 |
3.07e-16 |
|
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: 81.35 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 29 CQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKllDIVFP------AASTMVDIARSQDAEVGDGTTSVVVLAA 102
Cdd:cd03344 17 VNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAK--EIELEdpfenmGAQLVKEVASKTNDVAGDGTTTATVLAR 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 17564182 103 EILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGETELR 150
Cdd:cd03344 95 AIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIA 142
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
174-375 |
1.44e-15 |
|
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. Fab1p is important for vacuole size regulation, presumably by modulating PtdIns(3,5)P2 effector activity. In the human homolog p235/PIKfyve deletion of this domain leads to loss of catalytic activity. However no exact function this domain has been defined. In general, chaperonins are involved in productive folding of proteins.
Pssm-ID: 239450 [Multi-domain] Cd Length: 261 Bit Score: 76.88 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 174 ANMIVDAVNTLDAHLPLNMIGIKKVNGGNLHESRLIKGVAFQKAFSYAGfeMqPKKYSNVKVALLNIELELKaekenaem 253
Cdd:cd03334 31 ASNVKPDVRAGDDMDIRQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKR--M-PSKIKNPRILLLQGPLEYQ-------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 254 RLTN-VSDFQAVVDAEWNILYDKLQKIHDSGANVVLSKLPIGDVATQWFADRDMFCAGRIPQDDLDRLMSACGGSVLTT- 331
Cdd:cd03334 100 RVENkLLSLDPVILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSm 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17564182 332 VSQIDDSVLGKCGKFYEQQVGSER-----YNFFEDCSKAQACTLLLRGG 375
Cdd:cd03334 180 DDLLTSPKLGTCESFRVRTYVEEHgrsktLMFFEGCPKELGCTILLRGG 228
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
26-149 |
5.24e-15 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 77.65 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 26 INACQVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKllDIVFP------AASTMVDIARSQDAEVGDGTTSVVV 99
Cdd:PTZ00114 28 LKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAK--AIEFSdrfenvGAQLIRQVASKTNDKAGDGTTTATI 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 17564182 100 LAAEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGETEL 149
Cdd:PTZ00114 106 LARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDI 155
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
30-534 |
4.38e-14 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 74.68 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 30 QVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILK---LLDIVFPAASTMVDIARSQDAEV-GDGTTSVVVLAAEIL 105
Cdd:PRK14104 21 DILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKeieLEDKFENMGAQMVREVASKSADAaGDGTTTATVLAQAIV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 106 KQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGETELREMlvkcaaTTLSSKLVSQERLFFANMIVDAVNTld 185
Cdd:PRK14104 101 REGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQV------GTISANGDAEIGKFLADAMKKVGNE-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 186 ahlplnmiGIKKVNGGNLHESRL--IKGVAFQKAFsyagfeMQPKKYSNVKvallnielELKAEKENA-----EMRLTNV 258
Cdd:PRK14104 173 --------GVITVEEAKSLETELdvVEGMQFDRGY------ISPYFVTNAD--------KMRVEMDDAyilinEKKLSSL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 259 SD----FQAVV-----------DAEWNILYDKLQKIHDSGANVVLSKLP-IGDVATQWFADRDMFCAGRIPQDDL----- 317
Cdd:PRK14104 231 NEllplLEAVVqtgkplvivaeDVEGEALATLVVNRLRGGLKVAAVKAPgFGDRRKAMLQDIAILTGGQAISEDLgikle 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 318 DRLMSACGGSVLTTVSQIDDSVLGKCGK--------------FYEQQVGSERYNFFEDCSKAQACTLLLR-GGAEQFIAE 382
Cdd:PRK14104 311 NVTLQMLGRAKKVMIDKENTTIVNGAGKkadiearvaqikaqIEETTSDYDREKLQERLAKLAGGVAVIRvGGATEVEVK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 383 TERSLHDAIMIVRRAKKNDSIVAGGGAIEMELSrlirEHSKGI--EGKDQAFWMA-YGQAFEIIPRQLCQNAGLDALDVL 459
Cdd:PRK14104 391 ERKDRVDDAMHATRAAVEEGIVPGGGVALLRAS----EQLKGIktKNDDQKTGVEiVRKALSAPARQIAINAGEDGSVIV 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17564182 460 NKLRHRhaqgEKWA-GIDIHREAVGDNLVACVWEPSIVKRNAITAATEAACLVLSIDQTVKNV--RTPSGGAMPGLPG 534
Cdd:PRK14104 467 GKILEK----EQYSyGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELpkKGGAGPAMPPGGG 540
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
33-150 |
4.70e-13 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 71.38 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 33 ADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLD-----------IVFPAASTMVDIArsqdaevGDGTTSVVVLA 101
Cdd:PRK12849 23 ADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIEledpfenlgaqLVKEVASKTNDVA-------GDGTTTATVLA 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 17564182 102 AEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGETELR 150
Cdd:PRK12849 96 QALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIA 144
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
31-532 |
2.26e-12 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 69.49 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 31 VVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILK---LLDIVFPAASTMVDIARSQDAEV-GDGTTSVVVLAAEILK 106
Cdd:PRK12852 22 ILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKeieLEDKFENMGAQMVREVASKTNDLaGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 107 QMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGETELREMlvkcaaTTLSSKLVSQerlfFANMIVDAVNTLDA 186
Cdd:PRK12852 102 EGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQV------GTISANGDAA----IGKMIAQAMQKVGN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 187 HlplnmiGIKKVNGGNLHESRL--IKGVAFQKAFSYAGFEMQPKKysnvkvallnieleLKAEKENA-----EMRLTNVS 259
Cdd:PRK12852 172 E------GVITVEENKSLETEVdiVEGMKFDRGYLSPYFVTNAEK--------------MTVELDDAyillhEKKLSGLQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 260 D----FQAVVDAEWNILYDKLQKIHDSGANVVLSK----LPIGDVATQWFADRD--------MFCAGRIPQDDL-----D 318
Cdd:PRK12852 232 AmlpvLEAVVQSGKPLLIIAEDVEGEALATLVVNRlrggLKVAAVKAPGFGDRRkamlediaILTGGQLISEDLgikleN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 319 RLMSACGGSVLTTVSQIDDSVLGKCGKF--YEQQVGSERYNFFE-----DCSKAQACTLLLRGG---------AEQFIAE 382
Cdd:PRK12852 312 VTLKMLGRAKKVVIDKENTTIVNGAGKKadIEARVGQIKAQIEEttsdyDREKLQERLAKLAGGvavirvggaTEVEVKE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 383 TERSLHDAIMIVRRAKKnDSIVAGGGaieMELSRlIREHSKGIEGKD---QAFWMAYGQAFEIIPRQLCQNAGLDALDVL 459
Cdd:PRK12852 392 KKDRVEDALNATRAAVQ-EGIVPGGG---VALLR-AKKAVGRINNDNadvQAGINIVLKALEAPIRQIAENAGVEGSIVV 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 460 NKLRHRhaQGEKWaGIDIHREAVGDNLVACVWEPSIVKRNAITAATEAACLVLSIDQTV-------KNVRTPSGGAMPGL 532
Cdd:PRK12852 467 GKILEN--KSETF-GFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVaelpkkdAAPAMPAGGGMGGM 543
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
33-151 |
3.44e-12 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 68.59 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 33 ADSIRTTLGPRGLDKLIVDSKGATTISNDGATILK---LLDIVFPAASTMV-DIARSQDAEVGDGTTSVVVLAAEILKQM 108
Cdd:PRK12850 24 ANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKeieLEDKFENMGAQMVkEVASKTNDLAGDGTTTATVLAQAIVREG 103
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 17564182 109 KPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGETELRE 151
Cdd:PRK12850 104 AKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQ 146
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
31-151 |
8.50e-12 |
|
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: 67.32 E-value: 8.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 31 VVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILK---LLD--------IVFPAASTMVDIArsqdaevGDGTTSVVV 99
Cdd:TIGR02348 20 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKeieLEDkfenmgaqLVKEVASKTNDVA-------GDGTTTATV 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 17564182 100 LAAEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGETELRE 151
Cdd:TIGR02348 93 LAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQ 144
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
31-149 |
1.63e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 66.69 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 31 VVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAA---STMVDIARSQDAEV-GDGTTSVVVLAAEILK 106
Cdd:PRK12851 22 ILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFEnmgAQMVREVASKTNDVaGDGTTTATVLAQAIVR 101
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 17564182 107 QMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGETEL 149
Cdd:PRK12851 102 EGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEI 144
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
31-148 |
4.39e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 62.06 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 31 VVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILK---LLD--------IVFPAASTMVDIArsqdaevGDGTTSVVV 99
Cdd:PRK00013 21 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKeieLEDpfenmgaqLVKEVASKTNDVA-------GDGTTTATV 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 17564182 100 LAAEILKQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADLEIKINGETE 148
Cdd:PRK00013 94 LAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEE 142
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
30-139 |
4.42e-09 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 58.96 E-value: 4.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 30 QVVADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDIAR---SQDAEV-GDGTTSVVVLAAEIL 105
Cdd:CHL00093 20 DILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRqaaSKTNDVaGDGTTTATVLAYAIV 99
|
90 100 110
....*....|....*....|....*....|....
gi 17564182 106 KQMKPFIEDGVHPQLLIRAIGKACEKTLKNLADL 139
Cdd:CHL00093 100 KQGMKNVAAGANPISLKRGIEKATQYVVSQIAEY 133
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
32-526 |
4.02e-08 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 56.09 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 32 VADSIRTTLGPRGLDKLIVDSKGATTISNDGATILKLLDIVFPAASTMVDIARSQDAEV----GDGTTSVVVLAAEILKQ 107
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAKTndlaGDGTTTSVVLAQGLIAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 108 MKPFIEDGVHPQLLIRAIgkacEKTLKNLADLEIKINGETELREMLVKCAATTLSSKLVsqerlffANMIVDAVNTLDAH 187
Cdd:PLN03167 158 GVKVVAAGANPVQITRGI----EKTAKALVKELKKMSKEVEDSELADVAAVSAGNNYEV-------GNMIAEAMSKVGRK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 188 lplnmiGIKKVNGGNLHESRL--IKGVAFQKAFSYAGFEMQPKK----YSNVKVALLnielelkaekenaEMRLTNVSDF 261
Cdd:PLN03167 227 ------GVVTLEEGKSAENNLyvVEGMQFDRGYISPYFVTDSEKmsveYDNCKLLLV-------------DKKITNARDL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 262 QAVVD----AEWNILYDKLQKIHDSGANVVLSKLP------------IGDVATQWFADRDMFCAGRIPQDDLDRLMSACG 325
Cdd:PLN03167 288 IGILEdairGGYPLLIIAEDIEQEALATLVVNKLRgslkiaalkapgFGERKSQYLDDIAILTGGTVIREEVGLSLDKVG 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 326 GSVLTTVSQIddsVLGK-----CGKFYEQQVGSERY----NFFEDCSKAQACTLL------LRGGAE--QFIAETERSLH 388
Cdd:PLN03167 368 KEVLGTAAKV---VLTKdtttiVGDGSTQEAVNKRVaqikNLIEAAEQDYEKEKLneriakLSGGVAviQVGAQTETELK 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564182 389 DAIMIVR------RAKKNDSIVAGGGAIEMELSRLIREHSKGIEGKDQAFwmaygqAFEIIPRQLC-------QNAGLDA 455
Cdd:PLN03167 445 EKKLRVEdalnatKAAVEEGIVVGGGCTLLRLASKVDAIKDTLENDEQKV------GADIVKRALSyplkliaKNAGVNG 518
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17564182 456 LDVLNKLRhrhAQGEKWAGIDIHREAVGDNLVACVWEPSIVKRNAITAATEAACLVLSIDQTVKNVRTPSG 526
Cdd:PLN03167 519 SVVSEKVL---SNDNPKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPEP 586
|
|
| |
