|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
4-524 |
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: 1105.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 4 PVILLKEGTDTSQGIPQLVSNINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDIAK 83
Cdd:cd03340 1 PIILLKEGTDTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 84 SQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVKKEDKDEQRSLLEKCAATALS 163
Cdd:cd03340 81 SQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKEEQRELLEKCAATALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 164 SKLISQSKEFFSKMVVDAVMMLDDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFEMQPKKYQSPKIALLNVEL 243
Cdd:cd03340 161 SKLIASEKEFFAKMVVDAVLSLDDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAGFEQQPKKFKNPKILLLNVEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 244 ELKAEKDNAEVRVNTVEDYQAIVDAEWNILYDKLDKIHKSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMM 323
Cdd:cd03340 241 ELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 324 ACGGSIQTSVNALSDDVLGRCELFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDS 403
Cdd:cd03340 321 ATGGSIQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 404 VVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQG-GMWYGVDVNNED 482
Cdd:cd03340 401 VVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGgGKWYGVDINNEG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1110997893 483 IADNFEACVWEPAIVRINALTAASEAACLIVSVDETIKNPRS 524
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 ... |
2-524 |
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: 957.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 2 PTPVILLKEGTDTSQGIPQLVSNINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDI 81
Cdd:TIGR02345 1 RPTIVLLKEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 82 AKSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVkKEDKDEQRSLLEKCAATA 161
Cdd:TIGR02345 81 AKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTI-DEEKGEQRELLEKCAATA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 162 LSSKLISQSKEFFSKMVVDAVMMLD-DLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFEMQPKKYQSPKIALLN 240
Cdd:TIGR02345 160 LSSKLISHNKEFFSKMIVDAVLSLDrDDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAGFEQQPKKFANPKILLLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 241 VELELKAEKDNAEVRVNTVEDYQAIVDAEWNILYDKLDKIHKSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKR 320
Cdd:TIGR02345 240 VELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 321 TMMACGGSIQTSVNALSDDVLGRCELFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIK 400
Cdd:TIGR02345 320 VIKACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 401 NDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQGGMWYGVDVNN 480
Cdd:TIGR02345 400 NKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINT 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1110997893 481 EDIADNFEACVWEPAIVRINALTAASEAACLIVSVDETIKNPRS 524
Cdd:TIGR02345 480 EDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITNPKS 523
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
12-520 |
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 1110997893 12 TDTSQGIPQLVSNINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGD 91
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 92 GTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVKKEDKDEqrslLEKCAATALSSKLISQSK 171
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREE----LLKVATTSLNSKLVSGGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 172 EFFSKMVVDAVMMLDDLLQ---LKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFemqPKKYQSPKIALLNVELELkae 248
Cdd:cd00309 157 DFLGELVVDAVLKVGKENGdvdLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYM---PKRLENAKILLLDCKLEY--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 249 kdnaevrvntvedyqaivdaewnilydkldkihksgakVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGS 328
Cdd:cd00309 231 --------------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGAT 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 329 IQTSVNALSDDVLGRCELFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGG 408
Cdd:cd00309 273 IVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 409 GAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQGGMWYGVDVNNEDIADNFE 488
Cdd:cd00309 353 GAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKE 432
|
490 500 510
....*....|....*....|....*....|..
gi 1110997893 489 ACVWEPAIVRINALTAASEAACLIVSVDETIK 520
Cdd:cd00309 433 AGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
31-520 |
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: 561.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 31 IAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLKQVKPY 110
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 111 VEEGLHPQIIIRAFRTATQLAVNKIKDIavaVKKEDKDEQRSLLEKCAATALSSKLISQSKEFFSKMVVDAVMMLDDL-- 188
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSI---ISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 189 -LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYagfEMQPKKYQSPKIALLNVELELKAEKDNAEVRVNTVEDYQAIVD 267
Cdd:pfam00118 158 sFDLGNIGVVKILGGSLEDSELVDGVVLDKGPLH---PDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 268 AEWNILYDKLDKIHKSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALSDDVLGRCELF 347
Cdd:pfam00118 235 AEEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 348 EETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIP 427
Cdd:pfam00118 315 EEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 428 GKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQGGMWYGVDVNNEDIADNFEACVWEPAIVRINALTAASE 507
Cdd:pfam00118 395 GKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATE 474
|
490
....*....|...
gi 1110997893 508 AACLIVSVDETIK 520
Cdd:pfam00118 475 AASTILRIDDIIK 487
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
3-519 |
4.31e-172 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 496.78 E-value: 4.31e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 3 TPVILLKEGTDTSQGIPQLVSNINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDIA 82
Cdd:NF041083 1 QPVLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 83 KSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVKKEDKDeqrsLLEKCAATAL 162
Cdd:NF041083 81 KTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRE----TLKKIAETSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 163 SSKLISQSKEFFSKMVVDAVMMLDDL------LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFemqPKKYQSPKI 236
Cdd:NF041083 157 TSKGVEEARDYLAEIAVKAVKQVAEKrdgkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGM---PKRVENAKI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 237 ALLNVELELKAEKDNAEVRVNTVEDYQAIVDAEWNILYDKLDKIHKSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEE 316
Cdd:NF041083 234 ALLDAPLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 317 DLKRTMMACGGSIQTSVNALSDDVLGRCELFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVR 396
Cdd:NF041083 314 DMEKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 397 RAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQGGMWYGV 476
Cdd:NF041083 394 DAVEDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGI 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1110997893 477 DVNNEDIADNFEACVWEPAIVRINALTAASEAACLIVSVDETI 519
Cdd:NF041083 474 NVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVI 516
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
3-519 |
1.89e-169 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 490.17 E-value: 1.89e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 3 TPVILLKEGTDTSQGIPQLVSNINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDIA 82
Cdd:NF041082 1 QPILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 83 KSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVKKEDKDeqrsLLEKCAATAL 162
Cdd:NF041082 81 KTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKE----TLKKIAATAM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 163 SSKLISQSKEFFSKMVVDAVMMLDD-----LLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGfeMqPKKYQSPKIA 237
Cdd:NF041082 157 TGKGAEAAKDKLADLVVDAVKAVAEkdggyNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPG--M-PKRVENAKIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 238 LLNVELELKAEKDNAEVRVNTVEDYQAIVDAEWNILYDKLDKIHKSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEED 317
Cdd:NF041082 234 LLDAPLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 318 LKRTMMACGGSIQTSVNALSDDVLGRCELFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRR 397
Cdd:NF041082 314 MEKLAKATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 398 AIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQGGMWYGVD 477
Cdd:NF041082 394 VLEDGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLD 473
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1110997893 478 VNNEDIADNFEACVWEPAIVRINALTAASEAACLIVSVDETI 519
Cdd:NF041082 474 VYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVI 515
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
5-520 |
4.84e-168 |
|
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: 486.39 E-value: 4.84e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 5 VILLKEGTDTSQGIPQLVSNINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDIAKS 84
Cdd:cd03343 1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 85 QDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVKKEDKDeqrsLLEKCAATALSS 164
Cdd:cd03343 81 QDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKD----TLRKIAKTSLTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 165 KLISQSKEFFSKMVVDAVMMLDDL------LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFemqPKKYQSPKIAL 238
Cdd:cd03343 157 KGAEAAKDKLADLVVDAVLQVAEKrdgkyvVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGM---PKRVENAKIAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 239 LNVELELKAEKDNAEVRVNTVEDYQAIVDAEWNILYDKLDKIHKSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDL 318
Cdd:cd03343 234 LDAPLEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 319 KRTMMACGGSIQTSVNALSDDVLGRCELFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRA 398
Cdd:cd03343 314 EKLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 399 IKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQGGMWYGVDV 478
Cdd:cd03343 394 LEDGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDV 473
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1110997893 479 NNEDIADNFEACVWEPAIVRINALTAASEAACLIVSVDETIK 520
Cdd:cd03343 474 YTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIA 515
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
4-519 |
1.94e-163 |
|
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: 474.94 E-value: 1.94e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 4 PVILLKEGTDTSQGIPQLVSNINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDIAK 83
Cdd:TIGR02339 1 PVFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 84 SQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVKKEDKDeqrsLLEKCAATALS 163
Cdd:TIGR02339 81 TQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRD----LLKKIAYTSLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 164 SKLISQS-KEFFSKMVVDAVMMLDDL-------LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFemqPKKYQSPK 235
Cdd:TIGR02339 157 SKASAEVaKDKLADLVVEAVKQVAELrgdgkyyVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGM---PKRVENAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 236 IALLNVELELKAEKDNAEVRVNTVEDYQAIVDAEWNILYDKLDKIHKSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPE 315
Cdd:TIGR02339 234 IALLDAPLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 316 EDLKRTMMACGGSIQTSVNALSDDVLGRCELFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIV 395
Cdd:TIGR02339 314 SDIEKLARATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 396 RRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQGGMWYG 475
Cdd:TIGR02339 394 ANALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAG 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1110997893 476 VDVNNEDIADNFEACVWEPAIVRINALTAASEAACLIVSVDETI 519
Cdd:TIGR02339 474 INVFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVI 517
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
24-522 |
1.89e-143 |
|
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: 424.00 E-value: 1.89e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 24 NINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAEF 103
Cdd:cd03335 13 NVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 104 LKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKD-IAVAVKKEDKDeqrsLLEKCAATALSSKLISQSKEFFSKMVVDAV 182
Cdd:cd03335 93 LKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDNLGKE----SLINVAKTSMSSKIIGADSDFFANMVVDAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 183 M---MLDDLLQ----LKMIGIKKVQGGALEDSQLVAGVAFKKTFsyAGFEMqPKKYQSPKIALLNVELELKAEKDNAEVR 255
Cdd:cd03335 169 LavkTTNEKGKtkypIKAVNILKAHGKSAKESYLVNGYALNCTR--ASQGM-PTRVKNAKIACLDFNLQKTKMKLGVQVV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 256 VNTVEDYQAIVDAEWNILYDKLDKIHKSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNA 335
Cdd:cd03335 246 VTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVSTLAN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 336 L------SDDVLGRCELFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGGG 409
Cdd:cd03335 326 LegeetfDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 410 AIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHA--------QGGMWYGVDVNNE 481
Cdd:cd03335 406 AVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAaaqvkpdkKHLKWYGLDLING 485
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1110997893 482 DIADNFEACVWEPAIVRINALTAASEAACLIVSVDETIK-NP 522
Cdd:cd03335 486 KVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIKlNP 527
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
11-520 |
3.72e-139 |
|
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: 413.35 E-value: 3.72e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 11 GTDTSQGIPQLVSNINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVG 90
Cdd:TIGR02340 4 GGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 91 DGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKD-IAVAVKKEDKDEqrslLEKCAATALSSKLISQ 169
Cdd:TIGR02340 84 DGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDELGREA----LINVAKTSMSSKIIGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 170 SKEFFSKMVVDAVM-------MLDDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFsyAGFEMqPKKYQSPKIALLNVE 242
Cdd:TIGR02340 160 DSDFFSNIVVDAVLavkttneNGETKYPIKAINILKAHGKSARESMLVKGYALNCTV--ASQQM-PKRIKNAKIACLDFN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 243 LELKAEKDNAEVRVNTVEDYQAIVDAEWNILYDKLDKIHKSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTM 322
Cdd:TIGR02340 237 LQKAKMALGVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 323 MACGGSIQTSVNALSDD------VLGRCELFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVR 396
Cdd:TIGR02340 317 KATGATLVSTLADLEGEetfeasYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 397 RAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHA-------- 468
Cdd:TIGR02340 397 RTLESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAaaqlkpek 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1110997893 469 QGGMWYGVDVNNEDIADNFEACVWEPAIVRINALTAASEAACLIVSVDETIK 520
Cdd:TIGR02340 477 KHLKWYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIK 528
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
3-523 |
3.23e-134 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 400.56 E-value: 3.23e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 3 TPVILLKEGTDTSQGIPQLVSNINACQVIAEAVRTTLGPRGMDKLIV-----DDRGKATISNDGATILKLLDVVHPAAKT 77
Cdd:PTZ00212 6 VPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 78 LVDIAKSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVKKeDKDEQRSLLEKC 157
Cdd:PTZ00212 86 LVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGS-DEEKFKEDLLNI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 158 AATALSSKLISQSKEFFSKMVVDAVMMLDDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAgfemQPKKYQSPKIA 237
Cdd:PTZ00212 165 ARTTLSSKLLTVEKDHFAKLAVDAVLRLKGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVG----QPKRLENCKIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 238 LLNVELEL-KAEKDNAEVRVNTVEDYQAIVDAEWNILYDKLDKIHKSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEE 316
Cdd:PTZ00212 241 VANTPMDTdKIKIYGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 317 DLKRTMMACGGSIQTSVNALSDDVLGRCELFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVR 396
Cdd:PTZ00212 321 GMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 397 RAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQGGMWYGV 476
Cdd:PTZ00212 401 QTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGI 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1110997893 477 DVNNEDIADNFEACVWEPAIVRINALTAASEAACLIVSVDETIKN-PR 523
Cdd:PTZ00212 481 DMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRCaPR 528
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
8-523 |
7.74e-129 |
|
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: 386.30 E-value: 7.74e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 8 LKEGTDTSQGIPQLVSNINACQVIAEAVRTTLGPRGMDKLI--VDDRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQ 85
Cdd:cd03336 2 LKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 86 DAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVKkEDKDEQRSLLEKCAATALSSK 165
Cdd:cd03336 82 DDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHS-SDEEAFREDLLNIARTTLSSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 166 LISQSKEFFSKMVVDAVMMLDDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAgfemQPKKYQSPKIALLNVELEL 245
Cdd:cd03336 161 ILTQDKEHFAELAVDAVLRLKGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVN----QPKRIENAKILIANTPMDT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 246 -KAEKDNAEVRVNTVEDYQAIVDAEWNILYDKLDKIHKSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMA 324
Cdd:cd03336 237 dKIKIFGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 325 CGGSIQTSVNALSDDVLGRCELFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSV 404
Cdd:cd03336 317 TGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 405 VAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQGGMWYGVDVNNEDIA 484
Cdd:cd03336 397 VLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTVG 476
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1110997893 485 DNFEACVWEPAIVRINALTAASEAACLIVSVDETIK-NPR 523
Cdd:cd03336 477 DMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKcAPR 516
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
22-519 |
2.04e-123 |
|
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: 372.39 E-value: 2.04e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 22 VSNINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAA 101
Cdd:cd03338 11 LSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 102 EFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVKKEDkdeqRSLLEKCAATALSSKLISQSKEFFSKMVVDA 181
Cdd:cd03338 91 ALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLND----RESLIKSATTSLNSKVVSQYSSLLAPIAVDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 182 VMMLDDL-----LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGfeMQPKKYQSPKIALlnVELELKAEKDNAEVRV 256
Cdd:cd03338 167 VLKVIDPatatnVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKA--GGPTRIEKAKIGL--IQFCLSPPKTDMDNNI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 257 nTVEDYQA---IVDAEWNILYDKLDKIHKSGAKVVL---SKL--PIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGS 328
Cdd:cd03338 243 -VVNDYAQmdrILREERKYILNMCKKIKKSGCNVLLiqkSILrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 329 IQTSVNALSDDVLGRCELFEETQIGGERYNFFTGCPKA-KTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAG 407
Cdd:cd03338 322 PVASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 408 GGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQGGMWYGVDVNNEDIADNF 487
Cdd:cd03338 402 GGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITNIL 481
|
490 500 510
....*....|....*....|....*....|..
gi 1110997893 488 EACVWEPAIVRINALTAASEAACLIVSVDETI 519
Cdd:cd03338 482 EENVVQPLLVSTSAITLATETVRMILKIDDIV 513
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
4-519 |
4.17e-122 |
|
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: 367.78 E-value: 4.17e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 4 PVILLKEGTDTSQGIPQLVSNINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDIAK 83
Cdd:cd03337 1 PVLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 84 SQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVKKEDKDEQRSLLEKCaataLS 163
Cdd:cd03337 81 TQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSC----IG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 164 SKLISQSKEFFSKMVVDAVMM--LDDLLQLKMIGIK------KVQGGALEDSQLVAGVAFKKTFSYAGfeMQpKKYQSPK 235
Cdd:cd03337 157 TKFVSRWSDLMCNLALDAVKTvaVEENGRKKEIDIKryakveKIPGGEIEDSRVLDGVMLNKDVTHPK--MR-RRIENPR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 236 IALLNVELElkaekdnaevrvntvedYqaivdaewnilydkldkihksgakVVLSKLPIGDVATQYFADRDMFCAGRVPE 315
Cdd:cd03337 234 IVLLDCPLE-----------------Y------------------------LVITEKGVSDLAQHYLVKAGITALRRVRK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 316 EDLKRTMMACGGSIQTSVNALSDDVLG-RCELFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMI 394
Cdd:cd03337 273 TDNNRIARACGATIVNRPEELTESDVGtGAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 395 VRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQ-GGMW 473
Cdd:cd03337 353 ARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQgENST 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1110997893 474 YGVDVNNEDIADNFEACVWEPAIVRINALTAASEAACLIVSVDETI 519
Cdd:cd03337 433 WGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
4-519 |
4.01e-117 |
|
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: 356.36 E-value: 4.01e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 4 PVILLKEGTDTSQGIPQLVSNINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDIAK 83
Cdd:TIGR02344 1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 84 SQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVKKEDKDEQRSLLEKCaataLS 163
Cdd:TIGR02344 81 TQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSC----IG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 164 SKLISQSKEFFSKMVVDAVMMLDDLLQLKM-IGIK------KVQGGALEDSQLVAGVAFKKTFSYAgfEMQpKKYQSPKI 236
Cdd:TIGR02344 157 TKFVSRWSDLMCDLALDAVRTVQRDENGRKeIDIKryakveKIPGGDIEDSCVLKGVMINKDVTHP--KMR-RYIENPRI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 237 ALLNVELELKAEKDNAEVRVNTVEDYQAIVDAEWNILYDKLDKIHKSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEE 316
Cdd:TIGR02344 234 VLLDCPLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 317 DLKRTMMACGGSIQTSVNALSD-DVLGRCELFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIV 395
Cdd:TIGR02344 314 DNNRIARACGATIVNRPEELREsDVGTGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 396 RRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQGGM-WY 474
Cdd:TIGR02344 394 RNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNcTW 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1110997893 475 GVDVNNEDIADNFEACVWEPAIVRINALTAASEAACLIVSVDETI 519
Cdd:TIGR02344 474 GIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
23-517 |
5.58e-116 |
|
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: 353.32 E-value: 5.58e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 23 SNINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAE 102
Cdd:TIGR02342 13 SNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 103 FLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVKKEDkdeqRSLLEKCAATALSSKLISQSKEFFSKMVVDAV 182
Cdd:TIGR02342 93 LLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSD----REQLLKSATTSLSSKVVSQYSSLLAPLAVDAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 183 MMLDDL-----LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAgfEMQPKKYQSPKIALlnVELELKAEKDNAEVRVn 257
Cdd:TIGR02342 169 LKVIDPenaknVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKS--AGGPTRIEKAKIGL--IQFQISPPKTDMENQI- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 258 TVEDYQA---IVDAEWNILYDKLDKIHKSGAKVVLSKLPI-----GDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSI 329
Cdd:TIGR02342 244 IVNDYAQmdrVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 330 QTSVNALSDDVLGRCELFEETQIGGERYNFFTGCPKA-KTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGG 408
Cdd:TIGR02342 324 IASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 409 GAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQGGMWYGVDVNNEDIADNFE 488
Cdd:TIGR02342 404 GAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITNMLE 483
|
490 500
....*....|....*....|....*....
gi 1110997893 489 ACVWEPAIVRINALTAASEAACLIVSVDE 517
Cdd:TIGR02342 484 EHVLQPLLVTTSAITLASETVRSILKIDD 512
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
4-520 |
1.10e-109 |
|
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: 337.35 E-value: 1.10e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 4 PVILLKEGTDTS--QGIPQLVSNINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDI 81
Cdd:cd03339 6 PFIIVREQEKKKrlKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 82 AKSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIavAVKKEDKDEQRSLLEKCAATA 161
Cdd:cd03339 86 SKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEI--ADKIEFSPDNKEPLIQTAMTS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 162 LSSKLISQSKEFFSKMVVDAVMMLDDL----LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAgfEMqPKKYQSPKIA 237
Cdd:cd03339 164 LGSKIVSRCHRQFAEIAVDAVLSVADLerkdVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHP--QM-PKEVKDAKIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 238 LLNVELELKAEKDNAEVRVNTVEDYQAIVDAEWNILYDKLDKIHKSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEED 317
Cdd:cd03339 241 ILTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 318 LKRTMMACGGSIQTSVNALSDDVLGRCELFEETQIGG--ERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIV 395
Cdd:cd03339 321 IELIAIATGGRIVPRFEDLSPEKLGKAGLVREISFGTtkDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 396 RRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKH-AQGGMWY 474
Cdd:cd03339 401 RNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPHL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1110997893 475 GVDVNNEDIADNFEACVWEPAIVRINALTAASEAACLIVSVDETIK 520
Cdd:cd03339 481 GIDCLGRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
7-524 |
1.07e-104 |
|
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: 324.51 E-value: 1.07e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 7 LLKEGTDTSQGIPQLVSNINACQVIAEAVRTTLGPRGMDKLIVDDRGKATI--SNDGATILKLLDVVHPAAKTLVDIAKS 84
Cdd:TIGR02341 2 IFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSSSDASImvTNDGATILKSIGVDNPAAKVLVDMSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 85 QDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAvKKEDKDEQRSLLEKCAATALSS 164
Cdd:TIGR02341 82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVD-NGSDEVKFRQDLMNIARTTLSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 165 KLISQSKEFFSKMVVDAVMMLDDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYagfeMQPKKYQSPKIALLNVELE 244
Cdd:TIGR02341 161 KILSQHKDHFAQLAVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGV----NQPKRIENAKILIANTGMD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 245 L-KAEKDNAEVRVNTVEDYQAIVDAEWNILYDKLDKIHKSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMM 323
Cdd:TIGR02341 237 TdKVKIFGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 324 ACGGSIQTSVNALSDDVLGRCELFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDS 403
Cdd:TIGR02341 317 VTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 404 VVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQGGMWYGVDVNNEDI 483
Cdd:TIGR02341 397 TVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGTI 476
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1110997893 484 ADNFEACVWEPAIVRINALTAASEAACLIVSVDETIK-NPRS 524
Cdd:TIGR02341 477 ADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKaAPRK 518
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
19-519 |
3.03e-99 |
|
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: 308.77 E-value: 3.03e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 19 PQLVSNINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTL 98
Cdd:cd03341 8 EAVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 99 LAAEFLKQVKPYVEEGLHPQIIIRAFRTAT--------QLAVNKIKDiavavkKEDKDEqrslLEKCAATALSSKLISQS 170
Cdd:cd03341 88 LAGELLEKAEELLRMGLHPSEIIEGYEKALkkaleileELVVYKIED------LRNKEE----VSKALKTAIASKQYGNE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 171 kEFFSKMVVDAVMML----DDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKtfsyaGFEMQPKKYQSPKIALLNVELELk 246
Cdd:cd03341 158 -DFLSPLVAEACISVlpenIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKR-----EPEGSVKRVKKAKVAVFSCPFDI- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 247 aekdnaevrvntvedyqaivdaewnilydkldkihksGAKVVLSKLPIGDVAtQYFADRDMFCAGRVPEE-DLKRTMMAC 325
Cdd:cd03341 231 -------------------------------------GVNVIVAGGSVGDLA-LHYCNKYGIMVIKINSKfELRRLCRTV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 326 GGSIQTSVNALSDDVLGRCELFEETQIGGERYNFFTGCPKA-KTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSV 404
Cdd:cd03341 273 GATPLPRLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDsKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 405 VAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQGGMWYGVDVNNEDIA 484
Cdd:cd03341 353 VPGAGATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDEG 432
|
490 500 510
....*....|....*....|....*....|....*..
gi 1110997893 485 --DNFEACVWEPAIVRINALTAASEAACLIVSVDETI 519
Cdd:cd03341 433 tkDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
4-521 |
5.18e-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: 310.20 E-value: 5.18e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 4 PVILLKEGTDTSQ--GIPQLVSNINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDI 81
Cdd:TIGR02343 10 PFIIIKDQDNKKRlkGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 82 AKSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVkkEDKDEQRSLLEKCAATA 161
Cdd:TIGR02343 90 SKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEI--SADNNNREPLIQAAKTS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 162 LSSKLISQSKEFFSKMVVDAVMMLDDL----LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAgfEMqPKKYQSPKIA 237
Cdd:TIGR02343 168 LGSKIVSKCHRRFAEIAVDAVLNVADMerrdVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHP--QM-PKEVEDAKIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 238 LLNVELELKAEKDNAEVRVNTVEDYQAIVDAEWNILYDKLDKIHKSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEED 317
Cdd:TIGR02343 245 ILTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 318 LKRTMMACGGSIQTSVNALSDDVLGRCELFEETQIG--GERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIV 395
Cdd:TIGR02343 325 LELIAIATGGRIVPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 396 RRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKH-AQGGMWY 474
Cdd:TIGR02343 405 RNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQlKEKNPNL 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1110997893 475 GVDVNNEDIADNFEACVWEPAIVRINALTAASEAACLIVSVDETIKN 521
Cdd:TIGR02343 485 GVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVISP 531
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
23-519 |
7.46e-98 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 305.85 E-value: 7.46e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 23 SNINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHP----AAKTLVDIAKSQDAEVGDGTTSVTL 98
Cdd:COG0459 14 ANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTTTATV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 99 LAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVkkEDKDEqrslLEKCAATALSSKlisqskEFFSKMV 178
Cdd:COG0459 94 LAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPV--DDKEE----LAQVATISANGD------EEIGELI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 179 VDAVMMLDdllqlKMIGIKKVQGGALE-DSQLVAGVAFKKTFSYAGF----EMQPKKYQSPKIALLNVELELKAEkdnae 253
Cdd:COG0459 162 AEAMEKVG-----KDGVITVEEGKGLEtELEVVEGMQFDKGYLSPYFvtdpEKMPAELENAYILLTDKKISSIQD----- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 254 vrvntvedyqaivdaewniLYDKLDKIHKSGAKVVLSKLPIGDVATQYFADRDMFCAGRVP-----------EEDLKRTM 322
Cdd:COG0459 232 -------------------LLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVavkapgfgdrrKAMLEDIA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 323 MACGGSIQT-----SVNALSDDVLGRCELFEETqigGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRR 397
Cdd:COG0459 293 ILTGGRVISedlglKLEDVTLDDLGRAKRVEVD---KDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALHATRA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 398 AIKnDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRakhAQGGMWYGVD 477
Cdd:COG0459 370 AVE-EGIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVR---AAKDKGFGFD 445
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1110997893 478 VNNEDIADNFEACVWEPAIVRINALTAASEAACLIVSVDETI 519
Cdd:COG0459 446 AATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVI 487
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
7-519 |
9.60e-95 |
|
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: 298.94 E-value: 9.60e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 7 LLKEGTDTSQGIP-QLVSNINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQ 85
Cdd:TIGR02346 5 LLKEGYRHFSGLEeAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 86 DAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAV--AVKKEDKDEqrslLEKCAATALS 163
Cdd:TIGR02346 85 ENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVweVKDLRDKDE----LIKALKASIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 164 SKLISQsKEFFSKMVVDAVMML----DDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFsyagfEMQPKKYQSPKIALL 239
Cdd:TIGR02346 161 SKQYGN-EDFLAQLVAQACSTVlpknPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNREA-----EGSVKSVKNAKVAVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 240 NVELELKAEKDNAEVRVNTVEDYQAIVDAEWNILYDKLDKIHKSGAKVVLSKLPIGDVAtQYFADRDMFCAGRVPEE-DL 318
Cdd:TIGR02346 235 SCPLDTATTETKGTVLIHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMA-LHYLNKYNIMVLKIPSKfEL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 319 KRTMMACGGSIQTSVNALSDDVLGRCELFEETQIGGERYNFFTGCPK-AKTCTIILRGGAEQFMEETERSLHDAIMIVRR 397
Cdd:TIGR02346 314 RRLCKTVGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGdSKISTIILRGSTDNLLDDIERAIDDGVNTVKA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 398 AIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQGGMWYGVD 477
Cdd:TIGR02346 394 LVKDGRLLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGID 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1110997893 478 VNNEDIA--DNFEACVWEPAIVRINALTAASEAACLIVSVDETI 519
Cdd:TIGR02346 474 IEAESDGvkDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQII 517
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
21-525 |
8.22e-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: 265.06 E-value: 8.22e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 21 LVSNINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLA 100
Cdd:TIGR02347 18 LMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 101 AEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDiaVAVKKEDKDEqRSLLEKCAATALSSKLISQSKEFFSKMVVD 180
Cdd:TIGR02347 98 GELLKQAERYILEGVHPRIITEGFEIARKEALQFLDK--FKVKKEDEVD-REFLLNVARTSLRTKLPADLADQLTEIVVD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 181 AVMML---DDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFemqPKKYQSPKIALLNVELELKAEKDNAEVRVN 257
Cdd:TIGR02347 175 AVLAIkkdGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDM---PRRVKNAYILTCNVSLEYEKTEVNSGFFYS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 258 TVEDYQAIVDAEWNILYDKLDKI--------HKSGAK--VVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGG 327
Cdd:TIGR02347 252 SAEQREKLVKAERKFVDDRVKKIielkkkvcGKSPDKgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 328 SIQTSVNALSDDVLGRCELFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAG 407
Cdd:TIGR02347 332 EALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPG 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 408 GGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQGGMWYGVDVNNEDIADNF 487
Cdd:TIGR02347 412 AGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGVDLNTGEPIDPE 491
|
490 500 510
....*....|....*....|....*....|....*...
gi 1110997893 488 EACVWEPAIVRINALTAASEAACLIVSVDETIKNPRST 525
Cdd:TIGR02347 492 IKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSM 529
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
24-520 |
5.83e-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: 258.73 E-value: 5.83e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 24 NINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAEF 103
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 104 LKQVKPYVEEGLHPQIIIRAFrtatQLAVNKIKDIAVAVKKE-DKDEQRSLLEKCAATALSSKLISQSKEFFSKMVVDAV 182
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGF----ELAKNKALKFLESFKVPvEIDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 183 MML---DDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAgfEMqPKKYQSPKIALLNVELEL-KAEkdnaevrVNT 258
Cdd:cd03342 173 LAIykpDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHP--DM-PKRVENAYILTCNVSLEYeKTE-------VNS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 259 vedyqaivdaewNILYdkldkihksgaKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALSD 338
Cdd:cd03342 243 ------------GFFY-----------SVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 339 DVLGRCELFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKY 418
Cdd:cd03342 300 ECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAH 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 419 LRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQGGMWYGVDVNNEDIADNFEACVWEPAIVR 498
Cdd:cd03342 380 LKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVK 459
|
490 500
....*....|....*....|..
gi 1110997893 499 INALTAASEAACLIVSVDETIK 520
Cdd:cd03342 460 RQILHSATVIASQLLLVDEIIR 481
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
151-401 |
2.39e-69 |
|
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: 221.96 E-value: 2.39e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 151 RSLLEKCAATALSSKlISQSKEFFSKMVVDAVMMLDDLLQ---LKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFemq 227
Cdd:cd03333 1 RELLLQVATTSLNSK-LSSWDDFLGKLVVDAVLKVGPDNRmddLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYM--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 228 PKKYQSPKIALLNVELELkaekdnaevrvntvedyqaivdaewnilydkldkihksgakVVLSKLPIGDVATQYFADRDM 307
Cdd:cd03333 77 PKRLENAKILLLDCPLEY-----------------------------------------VVIAEKGIDDLALHYLAKAGI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 308 FCAGRVPEEDLKRTMMACGGSIQTSVNALSDDVLGRCELFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERS 387
Cdd:cd03333 116 MAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRS 195
|
250
....*....|....
gi 1110997893 388 LHDAIMIVRRAIKN 401
Cdd:cd03333 196 LHDALCAVRAAVEE 209
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
25-512 |
1.11e-19 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 92.28 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 25 INACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILK-------LLDVvhpAAKTLVDIAKSQDAEVGDGTTSVT 97
Cdd:PTZ00114 28 LKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKaiefsdrFENV---GAQLIRQVASKTNDKAGDGTTTAT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 98 LLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVKkeDKDEqrslLEKCAATALS-----SKLISQSke 172
Cdd:PTZ00114 105 ILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVK--TKED----ILNVATISANgdveiGSLIADA-- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 173 fFSKMVVDAVMMLDDllqlkmigikkvqGGALEDS-QLVAGVAFkktfsyagfemqPKKYQSPkiALLNVELELKAEKDN 251
Cdd:PTZ00114 177 -MDKVGKDGTITVED-------------GKTLEDElEVVEGMSF------------DRGYISP--YFVTNEKTQKVELEN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 252 AEVRV--NTVEDYQAIV----------------------DAEWNILYDKLdkihKSGAKVVLSKLP-IGDVATQYFADRD 306
Cdd:PTZ00114 229 PLILVtdKKISSIQSILpilehavknkrplliiaedvegEALQTLIINKL----RGGLKVCAVKAPgFGDNRKDILQDIA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 307 MFCAGRVPEED---------LKRTMMACGGSIQTSVNAL-------SDDVLGRCELF----------EETQIGGERYNFF 360
Cdd:PTZ00114 305 VLTGATVVSEDnvglklddfDPSMLGSAKKVTVTKDETViltgggdKAEIKERVELLrsqierttseYDKEKLKERLAKL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 361 TGcpkaKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNdSVVAGGGAIEMELSKYLrDY---SRTIPGKQQLLIGAY 437
Cdd:PTZ00114 385 SG----GVAVIKVGGASEVEVNEKKDRIEDALNATRAAVEE-GIVPGGGVALLRASKLL-DKleeDNELTPDQRTGVKIV 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1110997893 438 AKALEIIPRQLCDNAGFDATNILNKLRAKHAQGgmwYGVDVNNEDIADNFEACVWEPAIVRINALTAASEAACLI 512
Cdd:PTZ00114 459 RNALRLPTKQIAENAGVEGAVVVEKILEKKDPS---FGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLM 530
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
29-518 |
3.28e-19 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 90.93 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 29 QVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKT---LVDIAKSQDAEV-GDGTTSVTLLAAEFL 104
Cdd:CHL00093 20 DILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTgvaLIRQAASKTNDVaGDGTTTATVLAYAIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 105 KQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVkkedkdeqrsllEKCAATALSSKLISQSKEFFSKMVVDAvmm 184
Cdd:CHL00093 100 KQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPV------------EDIQAITQVASISAGNDEEVGSMIADA--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 185 LDDLLQLKMIGIKKVQGGALEdSQLVAGVAFKKTFSYAGFEMQPKK----YQSP-------KIALLNVELELKAEKDNAE 253
Cdd:CHL00093 165 IEKVGREGVISLEEGKSTVTE-LEITEGMRFEKGFISPYFVTDTERmevvQENPyilltdkKITLVQQDLLPILEQVTKT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 254 VR--VNTVEDYQAivDAEWNILYDKLDKIhksgAKVVLSKLP-IGDVATQYFADRDMFCAGRVPEED----LKR-TMMAC 325
Cdd:CHL00093 244 KRplLIIAEDVEK--EALATLVLNKLRGI----VNVVAVRAPgFGDRRKAMLEDIAILTGGQVITEDaglsLETiQLDLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 326 GGSIQTSVN---------ALSDDVLGRCE----LFEETQIGGERYNFFTGCPKAKTCTIILRGGA--EQFMEETERSLHD 390
Cdd:CHL00093 318 GQARRIIVTkdsttiiadGNEEQVKARCEqlrkQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAatETEMKDKKLRLED 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 391 AIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYSRTiPGKQQLLIGAY--AKALEIIPRQLCDNAGFDATNILNKLRAKHA 468
Cdd:CHL00093 398 AINATKAAVE-EGIVPGGGATLVHLSENLKTWAKN-NLKEDELIGALivARAILAPLKRIAENAGKNGSVIIEKVQEQDF 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1110997893 469 QggmwYGVDVNNEDIADNFEACVWEPAIVRINAL-TAASEAA------CLIVSVDET 518
Cdd:CHL00093 476 E----IGYNAANNKFVNMYEAGIIDPAKVTRSALqNAASIASmiltteCIIVDKKES 528
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
28-512 |
1.59e-17 |
|
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: 85.59 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 28 CQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILK---LLD-VVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAEF 103
Cdd:cd03344 17 VNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKeieLEDpFENMGAQLVKEVASKTNDVAGDGTTTATVLARAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 104 LKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVKKEDKDEQrsllekCAATALSS-----KLISQSkefFSKMV 178
Cdd:cd03344 97 IKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQ------VATISANGdeeigELIAEA---MEKVG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 179 VDAVMMLDDllqlkmigikkvqGGALEDS-QLVAGVAFKKTfsyagfemqpkkYQSPKIAlLNVElELKAEKDNAEV--- 254
Cdd:cd03344 168 KDGVITVEE-------------GKTLETElEVVEGMQFDRG------------YLSPYFV-TDPE-KMEVELENPYIllt 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 255 --RVNTVEDYQAIvdaewnilydkLDKIHKSGA--------------------------KVVLSKLP---------IGDV 297
Cdd:cd03344 221 dkKISSIQELLPI-----------LELVAKAGRplliiaedvegealatlvvnklrgglKVCAVKAPgfgdrrkamLEDI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 298 AT----QYFADRDMFCAGRVPEEDLKR-----------TMMACGGSiqtsvnalSDDVLGRCE----LFEETQIGGERYN 358
Cdd:cd03344 290 AIltggTVISEELGLKLEDVTLEDLGRakkvvvtkddtTIIGGAGD--------KAAIKARIAqirkQIEETTSDYDKEK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 359 F------FTGcpkaKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKnDSVVAGGGAIEMELSKYLrDYSRTIPGKQQL 432
Cdd:cd03344 362 LqerlakLSG----GVAVIKVGGATEVELKEKKDRVEDALNATRAAVE-EGIVPGGGVALLRASPAL-DKLKALNGDEKL 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 433 LIGAYAKALEIIPRQLCDNAGFDATNILNKLRaKHAQGgmwYGVDVNNEDIADNFEACVWEPAIVRINALTAASEAACLI 512
Cdd:cd03344 436 GIEIVRRALEAPLRQIAENAGVDGSVVVEKVL-ESPDG---FGYDAATGEYVDMIEAGIIDPTKVVRSALQNAASVASLL 511
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
30-531 |
1.32e-16 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 82.97 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 30 VIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVV----HPAAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLK 105
Cdd:PRK12852 22 ILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 106 QVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVKKEDKDEQRSLLEKCAATALsSKLISQSKEffsKMVVDAVMML 185
Cdd:PRK12852 102 EGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAI-GKMIAQAMQ---KVGNEGVITV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 186 DDLLQLKMigikkvqggaleDSQLVAGVAFKKTFSYAGFEMQPKK----YQSPKIALLNVELE--------LKAEKDNAE 253
Cdd:PRK12852 178 EENKSLET------------EVDIVEGMKFDRGYLSPYFVTNAEKmtveLDDAYILLHEKKLSglqamlpvLEAVVQSGK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 254 VRVNTVEDYQAivDAEWNILYDKLdkihKSGAKVVLSKLP-IGDVATQYFADRDMFCAGRVPEEDL-------------- 318
Cdd:PRK12852 246 PLLIIAEDVEG--EALATLVVNRL----RGGLKVAAVKAPgFGDRRKAMLEDIAILTGGQLISEDLgiklenvtlkmlgr 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 319 -KR-------TMMACGGSIQTSVNALSDDVLGRcelFEETQIGGERYNFFTGCPK-AKTCTIILRGGA-EQFMEETERSL 388
Cdd:PRK12852 320 aKKvvidkenTTIVNGAGKKADIEARVGQIKAQ---IEETTSDYDREKLQERLAKlAGGVAVIRVGGAtEVEVKEKKDRV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 389 HDAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYSRTIPgKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHA 468
Cdd:PRK12852 397 EDALNATRAAVQ-EGIVPGGGVALLRAKKAVGRINNDNA-DVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKS 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1110997893 469 QGgmwYGVDVNNEDIADNFEACVWEPAIVRINALTAASEAACLIVSVDETIKN-PRStvDAAPS 531
Cdd:PRK12852 475 ET---FGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAElPKK--DAAPA 533
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
196-376 |
5.77e-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: 74.95 E-value: 5.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 196 IKKVQGGALEDSQLVAGVAFKKTFSYAGfeMqPKKYQSPKIALLNVELELkaekdnaEVRVNTVEDYQAIVDAEWNILYD 275
Cdd:cd03334 52 IKKIPGGSPSDSEVVDGVVFTKNVAHKR--M-PSKIKNPRILLLQGPLEY-------QRVENKLLSLDPVILQEKEYLKN 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 276 KLDKIHKSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALSDD-VLGRCELFEETQIGG 354
Cdd:cd03334 122 LVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDLLTSpKLGTCESFRVRTYVE 201
|
170 180
....*....|....*....|....*..
gi 1110997893 355 ER-----YNFFTGCPKAKTCTIILRGG 376
Cdd:cd03334 202 EHgrsktLMFFEGCPKELGCTILLRGG 228
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
30-521 |
2.90e-14 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 75.55 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 30 VIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHP----AAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLK 105
Cdd:PRK12851 22 ILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 106 QVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVKKEDKDEQRSLLEKCAATALsSKLISQSKEffsKMVVDAVMML 185
Cdd:PRK12851 102 EGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEI-GRLVAEAME---KVGNEGVITV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 186 DDllqlkmigiKKVQGGALEdsqLVAGVAFKKTFSYAGFEMQPKK----YQSPKIALlnVELELKAEKDNAEVRVNTVED 261
Cdd:PRK12851 178 EE---------SKTAETELE---VVEGMQFDRGYLSPYFVTDADKmeaeLEDPYILI--HEKKISNLQDLLPVLEAVVQS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 262 YQAIV----DAEWNILYD-KLDKIHkSGAKVVLSKLP-IGDVATQYFADRDMFCAGRVPEEDLKR--------------- 320
Cdd:PRK12851 244 GKPLLiiaeDVEGEALATlVVNKLR-GGLKVAAVKAPgFGDRRKAMLEDIAILTGGTVISEDLGIklenvtleqlgrakk 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 321 -------TMMACGGSIQTSVNALSDDVlgRCELfEETQIGGERYNFFTGCPKAKTCTIILRGGA--EQFMEETERSLHDA 391
Cdd:PRK12851 323 vvvekenTTIIDGAGSKTEIEGRVAQI--RAQI-EETTSDYDREKLQERLAKLAGGVAVIRVGAstEVEVKEKKDRVDDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 392 IMIVRRAIKnDSVVAGGGAIEMELSKYLrDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKhaQGG 471
Cdd:PRK12851 400 LHATRAAVE-EGIVPGGGVALLRAVKAL-DKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREK--PGG 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1110997893 472 mwYGVDVNNEDIADNFEACVWEPAIVRINALTAASEAACLIVSVDETIKN 521
Cdd:PRK12851 476 --YGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAE 523
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
29-530 |
2.44e-13 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 72.37 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 29 QVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDV----VHPAAKTLVDIA-KSQDAeVGDGTTSVTLLAAEF 103
Cdd:PRK14104 21 DILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVAsKSADA-AGDGTTTATVLAQAI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 104 LKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVKKEDKDEQrsllekcaATALSSKLISQSKEFFSkmvvdavm 183
Cdd:PRK14104 100 VREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQ--------VGTISANGDAEIGKFLA-------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 184 mlDDLLQLKMIGIKKVQGGALEDSQL--VAGVAFKKTFSYAGFEMQPKKYQ-----------SPKIALLNVELE-LKAEK 249
Cdd:PRK14104 164 --DAMKKVGNEGVITVEEAKSLETELdvVEGMQFDRGYISPYFVTNADKMRvemddayilinEKKLSSLNELLPlLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 250 DNAEVRVNTVEDYQAivDAEWNILYDKLdkihKSGAKVVLSKLP-IGDVATQYFADRDMFCAGRVPEEDL---------- 318
Cdd:PRK14104 242 QTGKPLVIVAEDVEG--EALATLVVNRL----RGGLKVAAVKAPgFGDRRKAMLQDIAILTGGQAISEDLgiklenvtlq 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 319 -----KRTMMACGGSIQTSVNALSDDVLGRCE----LFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERS-- 387
Cdd:PRK14104 316 mlgraKKVMIDKENTTIVNGAGKKADIEARVAqikaQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKdr 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 388 LHDAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYsRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKH 467
Cdd:PRK14104 396 VDDAMHATRAAVE-EGIVPGGGVALLRASEQLKGI-KTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKE 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1110997893 468 AQGgmwYGVDVNNEDIADNFEACVWEPA-IVRINALTAASEAACLIVSVDETIKNPRSTVDAAP 530
Cdd:PRK14104 474 QYS---YGFDSQTGEYGNLVSKGIIDPTkVVRTAIQNAASVAALLITTEAMVAELPKKGGAGPA 534
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
31-530 |
2.96e-13 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 72.06 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 31 IAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHP----AAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLKQ 106
Cdd:PRK12850 23 LANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 107 VKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVKKEDKDEQRSLLEKCAATALSSkLISQSKEFFSKmvvDAVMMLD 186
Cdd:PRK12850 103 GAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGE-MIAEAMDKVGK---EGVITVE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 187 DllqlkmigiKKVQGGALEdsqLVAGVAFKKTFSYAGFEMQPKK----YQSPKIALLNVELE--------LKAEKDNAEV 254
Cdd:PRK12850 179 E---------AKTLGTELD---VVEGMQFDRGYLSPYFVTNPEKmraeLEDPYILLHEKKISnlqdllpiLEAVVQSGRP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 255 RVNTVEDyqaiVDAEWNILYdKLDKIHKsGAKVVLSKLP-IGDVATQYFADRDMFCAGRVPEEDLkrtmmacggSIQTSV 333
Cdd:PRK12850 247 LLIIAED----VEGEALATL-VVNKLRG-GLKSVAVKAPgFGDRRKAMLEDIAVLTGGQVISEDL---------GIKLEN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 334 NALsdDVLGRCELF-----EETQIGG-------------------------------ERYNFFTGcpkakTCTIILRGGA 377
Cdd:PRK12850 312 VTL--DMLGRAKRVlitkeNTTIIDGagdkkniearvkqiraqieettsdydreklqERLAKLAG-----GVAVIRVGGA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 378 -EQFMEETERSLHDAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYsRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDA 456
Cdd:PRK12850 385 tEVEVKEKKDRVDDALHATRAAVE-EGIVPGGGVALLRARSALRGL-KGANADETAGIDIVRRALEEPLRQIATNAGFEG 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1110997893 457 TNILNKLRAKhaQGGmwYGVDVNNEDIADNFEACVWEPAIVRINAL-TAASEAACLIVS----VDETIKNPRSTVDAAP 530
Cdd:PRK12850 463 SVVVGKVAEL--PGN--FGFNAQTGEYGDMVEAGIIDPAKVTRTALqDAASIAALLITTeamvAEAPKKAAAAAAGPGP 537
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
30-512 |
1.83e-11 |
|
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: 66.55 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 30 VIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHP----AAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLK 105
Cdd:TIGR02348 20 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVASKTNDVAGDGTTTATVLAQAIVK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 106 QVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVKKEDKDEQrsllekcaATALSS-------KLISQSKEFFSKmv 178
Cdd:TIGR02348 100 EGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQ--------VATISAnndeeigSLIAEAMEKVGK-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 179 vDAVMMLDDllqlkmigikkvqGGALEDSQ-LVAGVAFKKTFSYAGFEMQPKK----YQSPKIalLNVELELKAEKDNAE 253
Cdd:TIGR02348 170 -DGVITVEE-------------SKSLETELeVVEGMQFDRGYISPYFVTDAEKmeveLENPYI--LITDKKISNIKDLLP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 254 VRVNTVEDYQAIV----DAEWNILYDKLDKIHKSGAKVVLSKLP-IGDVATQYFADRDMFCAGRVPEEDLKRTMmacggs 328
Cdd:TIGR02348 234 LLEKVAQSGKPLLiiaeDVEGEALATLVVNKLRGTLNVCAVKAPgFGDRRKAMLEDIAILTGGQVISEELGLKL------ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 329 iqtsvNALSDDVLGRCELF----EETQI---GGERYNFFTGCPKAKT------------------------CTIILRGGA 377
Cdd:TIGR02348 308 -----EEVTLDDLGKAKKVtvdkDNTTIvegAGDKAAIKARVAQIKAqieettsdydreklqerlaklaggVAVIKVGAA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 378 -EQFMEETERSLHDAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYsRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDA 456
Cdd:TIGR02348 383 tETEMKEKKLRIEDALNATRAAVE-EGIVPGGGVALLRAAAALEGL-KGDGEDEAIGIDIVKRALEAPLRQIAENAGLDG 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1110997893 457 TNILNKLRAKHAQggmwYGVDVNNEDIADNFEACVWEPAIVRINALT-AASEAACLI 512
Cdd:TIGR02348 461 AVVAEKVKELKGN----FGFNAATGEYEDLVEAGIIDPTKVTRSALQnAASIAGLLL 513
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
32-519 |
1.19e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 64.06 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 32 AEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHP----AAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLKQV 107
Cdd:PRK12849 23 ADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQALVQEG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 108 KPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVkkEDKDEqrslLEKCAATAlsskliSQSKEFFSKMVVDAvmmldd 187
Cdd:PRK12849 103 LKNVAAGANPMDLKRGIDKAVEAVVEELKALARPV--SGSEE----IAQVATIS------ANGDEEIGELIAEA------ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 188 llqLKMIGIKKV----QGGALEDS-QLVAGVAFKKTFSYAGFEMQPKKYQspkiallnvelelkAEKDNAEV-----RVN 257
Cdd:PRK12849 165 ---MEKVGKDGVitveESKTLETElEVTEGMQFDRGYLSPYFVTDPERME--------------AVLEDPLIlltdkKIS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 258 TVEDYQAIvdaewnilydkLDKIHKSG---------------AKVVLSK----LPIGDVATQYFADR------DM--FCA 310
Cdd:PRK12849 228 SLQDLLPL-----------LEKVAQSGkplliiaedvegealATLVVNKlrggLKVAAVKAPGFGDRrkamleDIaiLTG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 311 GRVPEEDLkrtmmacGGSIQTSvnalSDDVLGRCELF----EETQI--GG------------------------------ 354
Cdd:PRK12849 297 GTVISEDL-------GLKLEEV----TLDDLGRAKRVtitkDNTTIvdGAgdkeaiearvaqirrqieettsdydreklq 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 355 ERYNFFTGcpkakTCTIILRGGA-EQFMEETERSLHDAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYsRTIPGKQQLL 433
Cdd:PRK12849 366 ERLAKLAG-----GVAVIKVGAAtEVELKERKDRVEDALNATRAAVE-EGIVPGGGVALLRAAKALDEL-AGLNGDQAAG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 434 IGAYAKALEIIPRQLCDNAGFDATNILNKLRaKHAQGgmwYGVDVNNEDIADNFEACVWEPAIVRINALTAASEAACLIV 513
Cdd:PRK12849 439 VEIVRRALEAPLRQIAENAGLDGSVVVAKVL-ELEDG---FGFNAATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLL 514
|
....*.
gi 1110997893 514 SVDETI 519
Cdd:PRK12849 515 TTEALV 520
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
30-150 |
3.36e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 59.37 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 30 VIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHP----AAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLK 105
Cdd:PRK00013 21 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLAQAIVR 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1110997893 106 QVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVAVKKEDKDEQ 150
Cdd:PRK00013 101 EGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQ 145
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
31-530 |
7.89e-07 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 51.85 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 31 IAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHP----AAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLKQ 106
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 107 VKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAvavkKEDKDEQrsLLEKCAATALSSKLISQskeffskMVVDAvmmld 186
Cdd:PLN03167 158 GVKVVAAGANPVQITRGIEKTAKALVKELKKMS----KEVEDSE--LADVAAVSAGNNYEVGN-------MIAEA----- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 187 dllqLKMIGIKKV----QGGALEDS-QLVAGVAFKKTFSYAGFEMQPKK----YQSPKIALLNVELElkaekdNAEVRVN 257
Cdd:PLN03167 220 ----MSKVGRKGVvtleEGKSAENNlYVVEGMQFDRGYISPYFVTDSEKmsveYDNCKLLLVDKKIT------NARDLIG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 258 TVED-----YQAIVDAE-------WNILYDKLdkihKSGAKVVLSKLP-IGDVATQYFADRDMFCAGRVPEEDLKRTMMA 324
Cdd:PLN03167 290 ILEDairggYPLLIIAEdieqealATLVVNKL----RGSLKIAALKAPgFGERKSQYLDDIAILTGGTVIREEVGLSLDK 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 325 CG----------------------GSIQTSVNALSDDVLGRCELFEETQiggERYNFFTGCPKAKTCTIILRGGAEQFME 382
Cdd:PLN03167 366 VGkevlgtaakvvltkdtttivgdGSTQEAVNKRVAQIKNLIEAAEQDY---EKEKLNERIAKLSGGVAVIQVGAQTETE 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 383 ETERSL--HDAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYSRTIPGKQQlLIGAyakalEIIPRQLC-------DNAG 453
Cdd:PLN03167 443 LKEKKLrvEDALNATKAAVE-EGIVVGGGCTLLRLASKVDAIKDTLENDEQ-KVGA-----DIVKRALSyplkliaKNAG 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 454 FDATNILNKLRAKHaqgGMWYGVDVNNEDIADNFEACVWEPA-IVRINALTAASEAACLIVS--VDETIKNPRSTVDAAP 530
Cdd:PLN03167 516 VNGSVVSEKVLSND---NPKFGYNAATGKYEDLMAAGIIDPTkVVRCCLEHAASVAKTFLTSdcVVVEIKEPEPVPAGNP 592
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
404-512 |
6.01e-04 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 42.42 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110997893 404 VVAGGGAIEMELSKYLrDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQGgmwYGVDVNNEDI 483
Cdd:PRK00013 410 IVPGGGVALLRAAPAL-EALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKG---YGYNAATGEY 485
|
90 100 110
....*....|....*....|....*....|
gi 1110997893 484 ADNFEACVWEPAIVRINAL-TAASEAACLI 512
Cdd:PRK00013 486 VDMIEAGIIDPTKVTRSALqNAASVAGLLL 515
|
|
| |
