|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
5-525 |
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: 1084.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 5 PVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAK 84
Cdd:cd03340 1 PIILLKEGTDTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 85 SQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQRKLLEKCAMTALS 164
Cdd:cd03340 81 SQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKEEQRELLEKCAATALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 165 SKLISQQKAFFAKMVVDAVMMLDDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFEMQPKKYHNPKIALLNVEL 244
Cdd:cd03340 161 SKLIASEKEFFAKMVVDAVLSLDDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAGFEQQPKKFKNPKILLLNVEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 245 ELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMM 324
Cdd:cd03340 241 ELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 325 ACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNDS 404
Cdd:cd03340 321 ATGGSIQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 405 VVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQG-GTWYGVDINNED 483
Cdd:cd03340 401 VVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGgGKWYGVDINNEG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 5453607 484 IADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIKNPRS 525
Cdd:cd03340 481 IADNFEAFVWEPSLVKINALTAATEAACLILSVDETIKNPKS 522
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
3-525 |
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: 974.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 3 PTPVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDI 82
Cdd:TIGR02345 1 RPTIVLLKEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 83 AKSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKaDKVEQRKLLEKCAMTA 162
Cdd:TIGR02345 81 AKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDE-EKGEQRELLEKCAATA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 163 LSSKLISQQKAFFAKMVVDAVMMLD-DLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFEMQPKKYHNPKIALLN 241
Cdd:TIGR02345 160 LSSKLISHNKEFFSKMIVDAVLSLDrDDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAGFEQQPKKFANPKILLLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 242 VELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKR 321
Cdd:TIGR02345 240 VELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 322 TMMACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIK 401
Cdd:TIGR02345 320 VIKACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 402 NDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINN 481
Cdd:TIGR02345 400 NKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINT 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 5453607 482 EDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIKNPRS 525
Cdd:TIGR02345 480 EDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITNPKS 523
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
13-521 |
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: 588.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 13 TDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGD 92
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 93 GTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADkveqRKLLEKCAMTALSSKLISQQK 172
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVED----REELLKVATTSLNSKLVSGGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 173 AFFAKMVVDAVMMLDDLLQ---LKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFemqPKKYHNPKIALLNVELELkae 249
Cdd:cd00309 157 DFLGELVVDAVLKVGKENGdvdLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYM---PKRLENAKILLLDCKLEY--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 250 kdnaeirvhtvedyqaivdaewnilydklekihhsgakVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGS 329
Cdd:cd00309 231 --------------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGAT 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 330 IQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGG 409
Cdd:cd00309 273 IVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 410 GAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNEDIADNFE 489
Cdd:cd00309 353 GAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKE 432
|
490 500 510
....*....|....*....|....*....|..
gi 5453607 490 AFVWEPAMVRINALTAASEAACLIVSVDETIK 521
Cdd:cd00309 433 AGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
32-521 |
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: 552.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 32 IAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLKQVKPY 111
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 112 VEEGLHPQIIIRAFRTATQLAVNKIKEI-AVTVKKADkveqRKLLEKCAMTALSSKLISQQKAFFAKMVVDAVMMLDDL- 189
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVD----REDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 190 --LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYagfEMQPKKYHNPKIALLNVELELKAEKDNAEIRVHTVEDYQAIV 267
Cdd:pfam00118 157 gsFDLGNIGVVKILGGSLEDSELVDGVVLDKGPLH---PDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 268 DAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALSADVLGRCQV 347
Cdd:pfam00118 234 KAEEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 348 FEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTI 427
Cdd:pfam00118 314 VEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 428 PGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNEDIADNFEAFVWEPAMVRINALTAAS 507
Cdd:pfam00118 394 SGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSAT 473
|
490
....*....|....
gi 5453607 508 EAACLIVSVDETIK 521
Cdd:pfam00118 474 EAASTILRIDDIIK 487
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
4-520 |
3.04e-169 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 489.46 E-value: 3.04e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 4 TPVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIA 83
Cdd:NF041083 1 QPVLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 84 KSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADkveqRKLLEKCAMTAL 163
Cdd:NF041083 81 KTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDD----RETLKKIAETSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 164 SSKLISQQKAFFAKMVVDAVMMLDDL------LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFemqPKKYHNPKI 237
Cdd:NF041083 157 TSKGVEEARDYLAEIAVKAVKQVAEKrdgkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGM---PKRVENAKI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 238 ALLNVELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEE 317
Cdd:NF041083 234 ALLDAPLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 318 DLKRTMMACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVR 397
Cdd:NF041083 314 DMEKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 398 RAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGV 477
Cdd:NF041083 394 DAVEDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGI 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 5453607 478 DINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETI 520
Cdd:NF041083 474 NVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVI 516
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
4-520 |
3.86e-166 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 481.31 E-value: 3.86e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 4 TPVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIA 83
Cdd:NF041082 1 QPILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 84 KSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKveqrKLLEKCAMTAL 163
Cdd:NF041082 81 KTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDK----ETLKKIAATAM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 164 SSKLISQQKAFFAKMVVDAVMMLDD-----LLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGfeMqPKKYHNPKIA 238
Cdd:NF041082 157 TGKGAEAAKDKLADLVVDAVKAVAEkdggyNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPG--M-PKRVENAKIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 239 LLNVELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEED 318
Cdd:NF041082 234 LLDAPLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 319 LKRTMMACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRR 398
Cdd:NF041082 314 MEKLAKATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 399 AIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVD 478
Cdd:NF041082 394 VLEDGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLD 473
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 5453607 479 INNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETI 520
Cdd:NF041082 474 VYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVI 515
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
6-521 |
1.37e-165 |
|
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: 479.84 E-value: 1.37e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 6 VILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKS 85
Cdd:cd03343 1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 86 QDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADkveqRKLLEKCAMTALSS 165
Cdd:cd03343 81 QDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDD----KDTLRKIAKTSLTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 166 KLISQQKAFFAKMVVDAVMMLDDL------LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFemqPKKYHNPKIAL 239
Cdd:cd03343 157 KGAEAAKDKLADLVVDAVLQVAEKrdgkyvVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGM---PKRVENAKIAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 240 LNVELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDL 319
Cdd:cd03343 234 LDAPLEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 320 KRTMMACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRA 399
Cdd:cd03343 314 EKLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 400 IKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDI 479
Cdd:cd03343 394 LEDGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDV 473
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 5453607 480 NNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIK 521
Cdd:cd03343 474 YTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIA 515
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
5-520 |
3.04e-162 |
|
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: 471.48 E-value: 3.04e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 5 PVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAK 84
Cdd:TIGR02339 1 PVFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 85 SQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVkkadKVEQRKLLEKCAMTALS 164
Cdd:TIGR02339 81 TQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKI----SPEDRDLLKKIAYTSLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 165 SKLISQQ-KAFFAKMVVDAVMMLDDL-------LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFemqPKKYHNPK 236
Cdd:TIGR02339 157 SKASAEVaKDKLADLVVEAVKQVAELrgdgkyyVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGM---PKRVENAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 237 IALLNVELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPE 316
Cdd:TIGR02339 234 IALLDAPLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 317 EDLKRTMMACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIV 396
Cdd:TIGR02339 314 SDIEKLARATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 397 RRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYG 476
Cdd:TIGR02339 394 ANALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAG 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 5453607 477 VDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETI 520
Cdd:TIGR02339 474 INVFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVI 517
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
14-523 |
1.11e-141 |
|
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: 419.38 E-value: 1.11e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 14 DSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDG 93
Cdd:cd03335 2 ERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 94 TTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKE-IAVTVKKADkveqRKLLEKCAMTALSSKLISQQK 172
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDNLG----KESLINVAKTSMSSKIIGADS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 173 AFFAKMVVDAVM---MLDDLLQ----LKMIGIKKVQGGALEDSQLVAGVAFKKTFsyAGFEMqPKKYHNPKIALLNVELE 245
Cdd:cd03335 158 DFFANMVVDAILavkTTNEKGKtkypIKAVNILKAHGKSAKESYLVNGYALNCTR--ASQGM-PTRVKNAKIACLDFNLQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 246 LKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMA 325
Cdd:cd03335 235 KTKMKLGVQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 326 CGGSIQTSVNAL------SADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRA 399
Cdd:cd03335 315 TGATLVSTLANLegeetfDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 400 IKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGT------ 473
Cdd:cd03335 395 LESNSVVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVkpdkkh 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 5453607 474 --WYGVDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIK-NP 523
Cdd:cd03335 475 lkWYGLDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIKlNP 527
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
12-521 |
1.53e-137 |
|
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: 409.11 E-value: 1.53e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 12 GTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVG 91
Cdd:TIGR02340 4 GGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 92 DGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEiaVTVKKADKVeQRKLLEKCAMTALSSKLISQQ 171
Cdd:TIGR02340 84 DGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKE--NLSVSVDEL-GREALINVAKTSMSSKIIGLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 172 KAFFAKMVVDAVM-------MLDDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFsyAGFEMqPKKYHNPKIALLNVEL 244
Cdd:TIGR02340 161 SDFFSNIVVDAVLavkttneNGETKYPIKAINILKAHGKSARESMLVKGYALNCTV--ASQQM-PKRIKNAKIACLDFNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 245 ELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMM 324
Cdd:TIGR02340 238 QKAKMALGVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 325 ACGGSIQTSV------NALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRR 398
Cdd:TIGR02340 318 ATGATLVSTLadlegeETFEASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 399 AIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHA--------Q 470
Cdd:TIGR02340 398 TLESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAaaqlkpekK 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 5453607 471 GGTWYGVDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIK 521
Cdd:TIGR02340 478 HLKWYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIK 528
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-524 |
6.29e-133 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 397.09 E-value: 6.29e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 1 MMPTPVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIV-----DGRGKATISNDGATILKLLDVVHPA 75
Cdd:PTZ00212 3 MANVPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 76 AKTLVDIAKSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKkADKVEQRKLL 155
Cdd:PTZ00212 83 AKILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHG-SDEEKFKEDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 156 EKCAMTALSSKLISQQKAFFAKMVVDAVMMLDDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAgfemQPKKYHNP 235
Cdd:PTZ00212 162 LNIARTTLSSKLLTVEKDHFAKLAVDAVLRLKGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVG----QPKRLENC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 236 KIALLNVELEL-KAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRV 314
Cdd:PTZ00212 238 KILVANTPMDTdKIKIYGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 315 PEEDLKRTMMACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIM 394
Cdd:PTZ00212 318 DFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALC 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 395 IVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTW 474
Cdd:PTZ00212 398 VLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKT 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 5453607 475 YGVDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIKN-PR 524
Cdd:PTZ00212 478 AGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRCaPR 528
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
9-524 |
7.02e-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: 7.02e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 9 LKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLI--VDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQ 86
Cdd:cd03336 2 LKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 87 DAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKkADKVEQRKLLEKCAMTALSSK 166
Cdd:cd03336 82 DDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHS-SDEEAFREDLLNIARTTLSSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 167 LISQQKAFFAKMVVDAVMMLDDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAgfemQPKKYHNPKIALLNVELEL 246
Cdd:cd03336 161 ILTQDKEHFAELAVDAVLRLKGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVN----QPKRIENAKILIANTPMDT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 247 -KAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMA 325
Cdd:cd03336 237 dKIKIFGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 326 CGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNDSV 405
Cdd:cd03336 317 TGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 406 VAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNEDIA 485
Cdd:cd03336 397 VLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTVG 476
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 5453607 486 DNFEAFVWEPAMVRINALTAASEAACLIVSVDETIK-NPR 524
Cdd:cd03336 477 DMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKcAPR 516
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
23-520 |
4.74e-122 |
|
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: 368.54 E-value: 4.74e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 23 VSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAA 102
Cdd:cd03338 11 LSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 103 EFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADkveqRKLLEKCAMTALSSKLISQQKAFFAKMVVDA 182
Cdd:cd03338 91 ALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLND----RESLIKSATTSLNSKVVSQYSSLLAPIAVDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 183 VMMLDDL-----LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGfeMQPKKYHNPKIALlnVELELKAEKDNAEIRV 257
Cdd:cd03338 167 VLKVIDPatatnVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKA--GGPTRIEKAKIGL--IQFCLSPPKTDMDNNI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 258 hTVEDYQA---IVDAEWNILYDKLEKIHHSGAKVVL---SKL--PIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGS 329
Cdd:cd03338 243 -VVNDYAQmdrILREERKYILNMCKKIKKSGCNVLLiqkSILrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 330 IQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKA-KTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAG 408
Cdd:cd03338 322 PVASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 409 GGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNEDIADNF 488
Cdd:cd03338 402 GGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITNIL 481
|
490 500 510
....*....|....*....|....*....|..
gi 5453607 489 EAFVWEPAMVRINALTAASEAACLIVSVDETI 520
Cdd:cd03338 482 EENVVQPLLVSTSAITLATETVRMILKIDDIV 513
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
5-520 |
1.13e-120 |
|
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: 363.92 E-value: 1.13e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 5 PVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAK 84
Cdd:cd03337 1 PVLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 85 SQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVkkadKVEQRKLLEKCAMTALS 164
Cdd:cd03337 81 TQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPV----DVNDRAQMLKIIKSCIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 165 SKLISQQKAFFAKMVVDAVMM--LDDLLQLKMIGIK------KVQGGALEDSQLVAGVAFKKTFSYAGfeMQpKKYHNPK 236
Cdd:cd03337 157 TKFVSRWSDLMCNLALDAVKTvaVEENGRKKEIDIKryakveKIPGGEIEDSRVLDGVMLNKDVTHPK--MR-RRIENPR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 237 IALLNVELElkaekdnaeirvhtvedYqaivdaewnilydklekihhsgakVVLSKLPIGDVATQYFADRDMFCAGRVPE 316
Cdd:cd03337 234 IVLLDCPLE-----------------Y------------------------LVITEKGVSDLAQHYLVKAGITALRRVRK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 317 EDLKRTMMACGGSIQTSVNALSADVLG-RCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMI 395
Cdd:cd03337 273 TDNNRIARACGATIVNRPEELTESDVGtGAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 396 VRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQ-GGTW 474
Cdd:cd03337 353 ARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQgENST 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 5453607 475 YGVDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETI 520
Cdd:cd03337 433 WGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
24-518 |
6.20e-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: 352.93 E-value: 6.20e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 24 SNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAE 103
Cdd:TIGR02342 13 SNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 104 FLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADkveqRKLLEKCAMTALSSKLISQQKAFFAKMVVDAV 183
Cdd:TIGR02342 93 LLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSD----REQLLKSATTSLSSKVVSQYSSLLAPLAVDAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 184 MMLDDL-----LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAgfEMQPKKYHNPKIALlnVELELKAEKDNAEIRVh 258
Cdd:TIGR02342 169 LKVIDPenaknVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKS--AGGPTRIEKAKIGL--IQFQISPPKTDMENQI- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 259 TVEDYQA---IVDAEWNILYDKLEKIHHSGAKVVLSKLPI-----GDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSI 330
Cdd:TIGR02342 244 IVNDYAQmdrVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 331 QTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKA-KTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGG 409
Cdd:TIGR02342 324 IASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 410 GAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNEDIADNFE 489
Cdd:TIGR02342 404 GAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITNMLE 483
|
490 500
....*....|....*....|....*....
gi 5453607 490 AFVWEPAMVRINALTAASEAACLIVSVDE 518
Cdd:TIGR02342 484 EHVLQPLLVTTSAITLASETVRSILKIDD 512
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
5-520 |
7.75e-115 |
|
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: 350.19 E-value: 7.75e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 5 PVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAK 84
Cdd:TIGR02344 1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 85 SQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQRKLLEKCamtaLS 164
Cdd:TIGR02344 81 TQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSC----IG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 165 SKLISQQKAFFAKMVVDAVMMLDDLLQLKM-IGIK------KVQGGALEDSQLVAGVAFKKTFSYAgfEMQpKKYHNPKI 237
Cdd:TIGR02344 157 TKFVSRWSDLMCDLALDAVRTVQRDENGRKeIDIKryakveKIPGGDIEDSCVLKGVMINKDVTHP--KMR-RYIENPRI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 238 ALLNVELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEE 317
Cdd:TIGR02344 234 VLLDCPLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 318 DLKRTMMACGGSIQTSVNAL-SADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIV 396
Cdd:TIGR02344 314 DNNRIARACGATIVNRPEELrESDVGTGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 397 RRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGT-WY 475
Cdd:TIGR02344 394 RNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNcTW 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 5453607 476 GVDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETI 520
Cdd:TIGR02344 474 GIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
5-521 |
7.34e-112 |
|
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: 342.74 E-value: 7.34e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 5 PVILLKEGTDSS--QGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDI 82
Cdd:cd03339 6 PFIIVREQEKKKrlKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 83 AKSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADkvEQRKLLEKCAMTA 162
Cdd:cd03339 86 SKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSP--DNKEPLIQTAMTS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 163 LSSKLISQQKAFFAKMVVDAVMMLDDL----LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAgfEMqPKKYHNPKIA 238
Cdd:cd03339 164 LGSKIVSRCHRQFAEIAVDAVLSVADLerkdVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHP--QM-PKEVKDAKIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 239 LLNVELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEED 318
Cdd:cd03339 241 ILTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 319 LKRTMMACGGSIQTSVNALSADVLGRCQVFEETQIGG--ERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIV 396
Cdd:cd03339 321 IELIAIATGGRIVPRFEDLSPEKLGKAGLVREISFGTtkDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 397 RRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGT-WY 475
Cdd:cd03339 401 RNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNpHL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 5453607 476 GVDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIK 521
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 ... |
8-525 |
1.96e-105 |
|
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: 326.05 E-value: 1.96e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 8 LLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATI--SNDGATILKLLDVVHPAAKTLVDIAKS 85
Cdd:TIGR02341 2 IFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSSSDASImvTNDGATILKSIGVDNPAAKVLVDMSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 86 QDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTvKKADKVEQRKLLEKCAMTALSS 165
Cdd:TIGR02341 82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVD-NGSDEVKFRQDLMNIARTTLSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 166 KLISQQKAFFAKMVVDAVMMLDDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYagfeMQPKKYHNPKIALLNVELE 245
Cdd:TIGR02341 161 KILSQHKDHFAQLAVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGV----NQPKRIENAKILIANTGMD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 246 L-KAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMM 324
Cdd:TIGR02341 237 TdKVKIFGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 325 ACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNDS 404
Cdd:TIGR02341 317 VTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 405 VVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNEDI 484
Cdd:TIGR02341 397 TVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGTI 476
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 5453607 485 ADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIK-NPRS 525
Cdd:TIGR02341 477 ADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKaAPRK 518
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
5-522 |
1.09e-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: 311.35 E-value: 1.09e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 5 PVILLKEGTDSSQ--GIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDI 82
Cdd:TIGR02343 10 PFIIIKDQDNKKRlkGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 83 AKSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVkkADKVEQRKLLEKCAMTA 162
Cdd:TIGR02343 90 SKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEI--SADNNNREPLIQAAKTS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 163 LSSKLISQQKAFFAKMVVDAVMMLDDL----LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAgfEMqPKKYHNPKIA 238
Cdd:TIGR02343 168 LGSKIVSKCHRRFAEIAVDAVLNVADMerrdVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHP--QM-PKEVEDAKIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 239 LLNVELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEED 318
Cdd:TIGR02343 245 ILTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 319 LKRTMMACGGSIQTSVNALSADVLGRCQVFEETQIG--GERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIV 396
Cdd:TIGR02343 325 LELIAIATGGRIVPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 397 RRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARH-AQGGTWY 475
Cdd:TIGR02343 405 RNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQlKEKNPNL 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 5453607 476 GVDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIKN 522
Cdd:TIGR02343 485 GVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVISP 531
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
20-520 |
3.74e-98 |
|
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: 305.68 E-value: 3.74e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 20 PQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTL 99
Cdd:cd03341 8 EAVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 100 LAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAV-TVKKADKVEQrklLEKCAMTALSSKLISQQkAFFAKM 178
Cdd:cd03341 88 LAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVyKIEDLRNKEE---VSKALKTAIASKQYGNE-DFLSPL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 179 VVDAVMML----DDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKtfsyaGFEMQPKKYHNPKIALLNVELELkaekdnae 254
Cdd:cd03341 164 VAEACISVlpenIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKR-----EPEGSVKRVKKAKVAVFSCPFDI-------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 255 irvhtvedyqaivdaewnilydklekihhsGAKVVLSKLPIGDVAtQYFADRDMFCAGRVPEE-DLKRTMMACGGSIQTS 333
Cdd:cd03341 231 ------------------------------GVNVIVAGGSVGDLA-LHYCNKYGIMVIKINSKfELRRLCRTVGATPLPR 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 334 VNALSADVLGRCQVFEETQIGGERYNFFTGCPKA-KTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGGGAI 412
Cdd:cd03341 280 LGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDsKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGAT 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 413 EMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNEDIA--DNFEA 490
Cdd:cd03341 360 EIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDEGtkDAKEA 439
|
490 500 510
....*....|....*....|....*....|
gi 5453607 491 FVWEPAMVRINALTAASEAACLIVSVDETI 520
Cdd:cd03341 440 GIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
24-520 |
2.38e-97 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 304.31 E-value: 2.38e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 24 SNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHP----AAKTLVDIAKSQDAEVGDGTTSVTL 99
Cdd:COG0459 14 ANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTTTATV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 100 LAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVtvkkadKVEQRKLLEKCAMTALSSKlisqqkAFFAKMV 179
Cdd:COG0459 94 LAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAK------PVDDKEELAQVATISANGD------EEIGELI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 180 VDAVMMLDdllqlKMIGIKKVQGGALE-DSQLVAGVAFKKTFSYAGF----EMQPKKYHNPKIALLNVELELKAEkdnae 254
Cdd:COG0459 162 AEAMEKVG-----KDGVITVEEGKGLEtELEVVEGMQFDKGYLSPYFvtdpEKMPAELENAYILLTDKKISSIQD----- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 255 irvhtvedyqaivdaewniLYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVP-----------EEDLKRTM 323
Cdd:COG0459 232 -------------------LLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVavkapgfgdrrKAMLEDIA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 324 MACGGSIQT-----SVNALSADVLGRCqvfEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRR 398
Cdd:COG0459 293 ILTGGRVISedlglKLEDVTLDDLGRA---KRVEVDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALHATRA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 399 AIKnDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRarhAQGGTWYGVD 478
Cdd:COG0459 370 AVE-EGIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVR---AAKDKGFGFD 445
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 5453607 479 INNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETI 520
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 ... |
8-520 |
1.63e-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: 300.48 E-value: 1.63e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 8 LLKEGTDSSQGIP-QLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQ 86
Cdd:TIGR02346 5 LLKEGYRHFSGLEeAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 87 DAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTvkKADKVEQRKLLEKCAMTALSSK 166
Cdd:TIGR02346 85 ENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVW--EVKDLRDKDELIKALKASISSK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 167 LISQQKaFFAKMVVDAVMML----DDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFsyagfEMQPKKYHNPKIALLNV 242
Cdd:TIGR02346 163 QYGNED-FLAQLVAQACSTVlpknPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNREA-----EGSVKSVKNAKVAVFSC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 243 ELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVAtQYFADRDMFCAGRVPEE-DLKR 321
Cdd:TIGR02346 237 PLDTATTETKGTVLIHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMA-LHYLNKYNIMVLKIPSKfELRR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 322 TMMACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPK-AKTCTFILRGGAEQFMEETERSLHDAIMIVRRAI 400
Cdd:TIGR02346 316 LCKTVGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGdSKISTIILRGSTDNLLDDIERAIDDGVNTVKALV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 401 KNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDIN 480
Cdd:TIGR02346 396 KDGRLLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIE 475
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 5453607 481 NEDIA--DNFEAFVWEPAMVRINALTAASEAACLIVSVDETI 520
Cdd:TIGR02346 476 AESDGvkDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQII 517
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
8-526 |
1.67e-81 |
|
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: 263.90 E-value: 1.67e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 8 LLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQD 87
Cdd:TIGR02347 4 LLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 88 AEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEiaVTVKKADKVEqRKLLEKCAMTALSSKL 167
Cdd:TIGR02347 84 DITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDK--FKVKKEDEVD-REFLLNVARTSLRTKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 168 ISQQKAFFAKMVVDAVMML---DDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFemqPKKYHNPKIALLNVEL 244
Cdd:TIGR02347 161 PADLADQLTEIVVDAVLAIkkdGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDM---PRRVKNAYILTCNVSL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 245 ELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIG-DVATQ---------YFADRDMFCAGRV 314
Cdd:TIGR02347 238 EYEKTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCGKSPDKGfVVINQkgidppsldLLAKEGIMALRRA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 315 PEEDLKRTMMACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIM 394
Cdd:TIGR02347 318 KRRNMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 395 IVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTW 474
Cdd:TIGR02347 398 AVKNAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEV 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 5453607 475 YGVDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIKNPRST 526
Cdd:TIGR02347 478 VGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSM 529
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
25-521 |
1.07e-79 |
|
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: 257.96 E-value: 1.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 25 NISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAEF 104
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 105 LKQVKPYVEEGLHPQIIIRAFrtatQLAVNKIKEIAVTVKKADKVEQ-RKLLEKCAMTALSSKLISQQKAFFAKMVVDAV 183
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGF----ELAKNKALKFLESFKVPVEIDTdRELLLSVARTSLRTKLHADLADQLTEIVVDAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 184 MML---DDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAgfEMqPKKYHNPKIALLNVELElkaekdnaeirvhtv 260
Cdd:cd03342 173 LAIykpDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHP--DM-PKRVENAYILTCNVSLE--------------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 261 edyqaivdaewnilYDKLEKihHSG--AKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALS 338
Cdd:cd03342 235 --------------YEKTEV--NSGffYSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 339 ADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSK 418
Cdd:cd03342 299 PECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 419 YLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNEDIADNFEAFVWEPAMV 498
Cdd:cd03342 379 HLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSV 458
|
490 500
....*....|....*....|...
gi 5453607 499 RINALTAASEAACLIVSVDETIK 521
Cdd:cd03342 459 KRQILHSATVIASQLLLVDEIIR 481
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
152-402 |
1.06e-68 |
|
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: 220.03 E-value: 1.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 152 RKLLEKCAMTALSSKlISQQKAFFAKMVVDAVMMLDDLLQ---LKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFemq 228
Cdd:cd03333 1 RELLLQVATTSLNSK-LSSWDDFLGKLVVDAVLKVGPDNRmddLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYM--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 229 PKKYHNPKIALLNVELELkaekdnaeirvhtvedyqaivdaewnilydklekihhsgakVVLSKLPIGDVATQYFADRDM 308
Cdd:cd03333 77 PKRLENAKILLLDCPLEY-----------------------------------------VVIAEKGIDDLALHYLAKAGI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 309 FCAGRVPEEDLKRTMMACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERS 388
Cdd:cd03333 116 MAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRS 195
|
250
....*....|....
gi 5453607 389 LHDAIMIVRRAIKN 402
Cdd:cd03333 196 LHDALCAVRAAVEE 209
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
30-519 |
3.72e-19 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 90.55 E-value: 3.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 30 QVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKT---LVDIAKSQDAEV-GDGTTSVTLLAAEFL 105
Cdd:CHL00093 20 DILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTgvaLIRQAASKTNDVaGDGTTTATVLAYAIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 106 KQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQrkllekcaMTALSSKlisqQKAFFAKMVVDAvmm 185
Cdd:CHL00093 100 KQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQ--------VASISAG----NDEEVGSMIADA--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 186 LDDLLQLKMIGIKKVQGGALEdSQLVAGVAFKKTFSYAGFEMQPKK----YHNP-------KIALLNVELELKAEKDNAE 254
Cdd:CHL00093 165 IEKVGREGVISLEEGKSTVTE-LEITEGMRFEKGFISPYFVTDTERmevvQENPyilltdkKITLVQQDLLPILEQVTKT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 255 IR--VHTVEDYQAivDAEWNILYDKLEKIhhsgAKVVLSKLP-IGDVATQYFADRDMFCAGRVPEED----LKR-TMMAC 326
Cdd:CHL00093 244 KRplLIIAEDVEK--EALATLVLNKLRGI----VNVVAVRAPgFGDRRKAMLEDIAILTGGQVITEDaglsLETiQLDLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 327 GGSIQTSVN---------ALSADVLGRC----QVFEETQIGGERYNFFTGCPKAKTCTFILRGGA--EQFMEETERSLHD 391
Cdd:CHL00093 318 GQARRIIVTkdsttiiadGNEEQVKARCeqlrKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAatETEMKDKKLRLED 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 392 AIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYSRTiPGKQQLLIGAY--AKALEIIPRQLCDNAGFDATNILNKLRARHA 469
Cdd:CHL00093 398 AINATKAAVE-EGIVPGGGATLVHLSENLKTWAKN-NLKEDELIGALivARAILAPLKRIAENAGKNGSVIIEKVQEQDF 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 5453607 470 QggtwYGVDINNEDIADNFEAFVWEPAMVRINAL-TAASEAA------CLIVSVDET 519
Cdd:CHL00093 476 E----IGYNAANNKFVNMYEAGIIDPAKVTRSALqNAASIASmiltteCIIVDKKES 528
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
26-513 |
2.74e-18 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 88.05 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 26 ISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILK-------LLDVvhpAAKTLVDIAKSQDAEVGDGTTSVT 98
Cdd:PTZ00114 28 LKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKaiefsdrFENV---GAQLIRQVASKTNDKAGDGTTTAT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 99 LLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADkveqrkLLEKCAMTALS-----SKLISQQka 173
Cdd:PTZ00114 105 ILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKE------DILNVATISANgdveiGSLIADA-- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 174 fFAKMVVDAVMMLDDllqlkmigikkvqGGALEDS-QLVAGVAFkktfsyagfemqPKKYHNPkiALLNVELELKAEKDN 252
Cdd:PTZ00114 177 -MDKVGKDGTITVED-------------GKTLEDElEVVEGMSF------------DRGYISP--YFVTNEKTQKVELEN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 253 AEIRVHT--VEDYQAIV----------------------DAEWNILYDKLekihHSGAKVVLSKLP-IGDVATQYFADRD 307
Cdd:PTZ00114 229 PLILVTDkkISSIQSILpilehavknkrplliiaedvegEALQTLIINKL----RGGLKVCAVKAPgFGDNRKDILQDIA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 308 MFCAGRVPEEDL-----------------------KRTMMACGG----SIQTSVNALSaDVLGRCQVFEETQIGGERYNF 360
Cdd:PTZ00114 305 VLTGATVVSEDNvglklddfdpsmlgsakkvtvtkDETVILTGGgdkaEIKERVELLR-SQIERTTSEYDKEKLKERLAK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 361 FTGcpkaKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNdSVVAGGGAIEMELSKYLrDY---SRTIPGKQQLLIGA 437
Cdd:PTZ00114 384 LSG----GVAVIKVGGASEVEVNEKKDRIEDALNATRAAVEE-GIVPGGGVALLRASKLL-DKleeDNELTPDQRTGVKI 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5453607 438 YAKALEIIPRQLCDNAGFDATNILNKLRARhaqGGTWYGVDINNEDIADNFEAFVWEPAMVRINALTAASEAACLI 513
Cdd:PTZ00114 458 VRNALRLPTKQIAENAGVEGAVVVEKILEK---KDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLM 530
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
29-513 |
1.58e-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: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 29 CQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILK---LLDVVHPA-AKTLVDIAKSQDAEVGDGTTSVTLLAAEF 104
Cdd:cd03344 17 VNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKeieLEDPFENMgAQLVKEVASKTNDVAGDGTTTATVLARAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 105 LKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQrkllekCAMTALSS-----KLISQQkafFAKMV 179
Cdd:cd03344 97 IKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQ------VATISANGdeeigELIAEA---MEKVG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 180 VDAVMMLDDllqlkmigikkvqGGALEDS-QLVAGVAFKKTFSYAGFEMQPKK----YHNPKIalLNVELELKAEKDNAE 254
Cdd:cd03344 168 KDGVITVEE-------------GKTLETElEVVEGMQFDRGYLSPYFVTDPEKmeveLENPYI--LLTDKKISSIQELLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 255 IRVHTVEDYQAIV--------DAEWNILYDKLEKihhsGAKVVLSKLP---------IGDVAT----QYFADRDMFCAGR 313
Cdd:cd03344 233 ILELVAKAGRPLLiiaedvegEALATLVVNKLRG----GLKVCAVKAPgfgdrrkamLEDIAIltggTVISEELGLKLED 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 314 VPEEDLKR-----------TMMACGGSiqtsvnalSADVLGRCQV----FEETQIGGERYNF------FTGcpkaKTCTf 372
Cdd:cd03344 309 VTLEDLGRakkvvvtkddtTIIGGAGD--------KAAIKARIAQirkqIEETTSDYDKEKLqerlakLSG----GVAV- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 373 ILRGGA-EQFMEETERSLHDAIMIVRRAIKnDSVVAGGGAIEMELSKYLrDYSRTIPGKQQLLIGAYAKALEIIPRQLCD 451
Cdd:cd03344 376 IKVGGAtEVELKEKKDRVEDALNATRAAVE-EGIVPGGGVALLRASPAL-DKLKALNGDEKLGIEIVRRALEAPLRQIAE 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5453607 452 NAGFDATNILNKLRArHAQGgtwYGVDINNEDIADNFEAFVWEPAMVRINALTAASEAACLI 513
Cdd:cd03344 454 NAGVDGSVVVEKVLE-SPDG---FGYDAATGEYVDMIEAGIIDPTKVVRSALQNAASVASLL 511
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
31-532 |
3.81e-17 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 84.51 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 31 VIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVV----HPAAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLK 106
Cdd:PRK12852 22 ILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 107 QVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQRKLLEKCAMTALsSKLISQQkafFAKMVVDAVMML 186
Cdd:PRK12852 102 EGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAI-GKMIAQA---MQKVGNEGVITV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 187 DDLLQLKMigikkvqggaleDSQLVAGVAFKKTFSYAGFEMQPKKY-----------HNPKIALLNVELE-LKAEKDNAE 254
Cdd:PRK12852 178 EENKSLET------------EVDIVEGMKFDRGYLSPYFVTNAEKMtvelddayillHEKKLSGLQAMLPvLEAVVQSGK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 255 IRVHTVEDYQAivDAEWNILYDKLEkihhSGAKVVLSKLP-IGDVATQYFADRDMFCAGRVPEEDL-------------- 319
Cdd:PRK12852 246 PLLIIAEDVEG--EALATLVVNRLR----GGLKVAAVKAPgFGDRRKAMLEDIAILTGGQLISEDLgiklenvtlkmlgr 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 320 -KR-------TMMACGGSIQTSVNALSADVlgRCQVfEETQIGGERYNFFTGCPKAKTCTFILR-GGA-EQFMEETERSL 389
Cdd:PRK12852 320 aKKvvidkenTTIVNGAGKKADIEARVGQI--KAQI-EETTSDYDREKLQERLAKLAGGVAVIRvGGAtEVEVKEKKDRV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 390 HDAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYSRTIPgKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHA 469
Cdd:PRK12852 397 EDALNATRAAVQ-EGIVPGGGVALLRAKKAVGRINNDNA-DVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKS 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5453607 470 QGgtwYGVDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIKNPRSTVDAPTA 532
Cdd:PRK12852 475 ET---FGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDAAPAM 534
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
30-530 |
1.44e-14 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 76.22 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 30 QVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDV----VHPAAKTLVDIA-KSQDAeVGDGTTSVTLLAAEF 104
Cdd:PRK14104 21 DILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVAsKSADA-AGDGTTTATVLAQAI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 105 LKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQrkllekcaMTALSSKLISQQKAFFAkmvvdavm 184
Cdd:PRK14104 100 VREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQ--------VGTISANGDAEIGKFLA-------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 185 mlDDLLQLKMIGIKKVQGGALEDSQL--VAGVAFKKTFSYAGFEMQPKKY-----------HNPKIALLNVELE-LKAEK 250
Cdd:PRK14104 164 --DAMKKVGNEGVITVEEAKSLETELdvVEGMQFDRGYISPYFVTNADKMrvemddayiliNEKKLSSLNELLPlLEAVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 251 DNAEIRVHTVEDYQAivDAEWNILYDKLEkihhSGAKVVLSKLP-IGDVATQYFADRDMFCAGRVPEEDL---------- 319
Cdd:PRK14104 242 QTGKPLVIVAEDVEG--EALATLVVNRLR----GGLKVAAVKAPgFGDRRKAMLQDIAILTGGQAISEDLgiklenvtlq 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 320 -----KRTMMACGGSIQTSVNALSADVLGR-CQV---FEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERS-- 388
Cdd:PRK14104 316 mlgraKKVMIDKENTTIVNGAGKKADIEARvAQIkaqIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKdr 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 389 LHDAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYsRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARH 468
Cdd:PRK14104 396 VDDAMHATRAAVE-EGIVPGGGVALLRASEQLKGI-KTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKE 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5453607 469 AQGgtwYGVDINNEDIADNFEAFVWEPA-MVRINALTAASEAACLIVSVDETIKNPRSTVDAP 530
Cdd:PRK14104 474 QYS---YGFDSQTGEYGNLVSKGIIDPTkVVRTAIQNAASVAALLITTEAMVAELPKKGGAGP 533
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
32-533 |
1.75e-14 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 75.91 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 32 IAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHP----AAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLKQ 107
Cdd:PRK12850 23 LANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 108 VKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQrklleKCAMTALSSKLISQqkaffakMVVDAVmmlD 187
Cdd:PRK12850 103 GAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQ-----VATISANGDESIGE-------MIAEAM---D 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 188 DLLQLKMIGIKKVQGGALEdSQLVAGVAFKKTFSYAGFEMQPKKY-----------HNPKIALLNVELE-LKAEKDNAEI 255
Cdd:PRK12850 168 KVGKEGVITVEEAKTLGTE-LDVVEGMQFDRGYLSPYFVTNPEKMraeledpyillHEKKISNLQDLLPiLEAVVQSGRP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 256 RVHTVEDyqaiVDAE--WNILYDKLekihHSGAKVVLSKLP-IGDVATQYFADRDMFCAGRVPEEDL------------- 319
Cdd:PRK12850 247 LLIIAED----VEGEalATLVVNKL----RGGLKSVAVKAPgFGDRRKAMLEDIAVLTGGQVISEDLgiklenvtldmlg 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 320 --------KRTMMACGGS-----IQTSVNALSADVlgrcqvfEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETE 386
Cdd:PRK12850 319 rakrvlitKENTTIIDGAgdkknIEARVKQIRAQI-------EETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 387 RSLH--DAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYsRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKL 464
Cdd:PRK12850 392 KKDRvdDALHATRAAVE-EGIVPGGGVALLRARSALRGL-KGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKV 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5453607 465 rarhAQGGTWYGVDINNEDIADNFEAFVWEPAMVRINAL-TAASEAACLIVS----VDETIKNPRSTVDAPTAA 533
Cdd:PRK12850 470 ----AELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALqDAASIAALLITTeamvAEAPKKAAAAAAGPGPGM 539
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
31-522 |
7.31e-14 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 74.01 E-value: 7.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 31 VIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHP----AAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLK 106
Cdd:PRK12851 22 ILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 107 QVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQRKLLEKCAMTALsSKLISQQkafFAKMVVDAVMML 186
Cdd:PRK12851 102 EGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEI-GRLVAEA---MEKVGNEGVITV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 187 DDllqlkmigiKKVQGGALEdsqLVAGVAFKKTFSYAGFEMQPKKY-----------HNPKIALLN-----VELELKAEK 250
Cdd:PRK12851 178 EE---------SKTAETELE---VVEGMQFDRGYLSPYFVTDADKMeaeledpyiliHEKKISNLQdllpvLEAVVQSGK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 251 DNAEIrvhtVEDYQAivDAEWNILYDKLekihHSGAKVVLSKLP-IGDVATQYFADRDMFCAGRVPEEDLKR-------- 321
Cdd:PRK12851 246 PLLII----AEDVEG--EALATLVVNKL----RGGLKVAAVKAPgFGDRRKAMLEDIAILTGGTVISEDLGIklenvtle 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 322 --------------TMMACGGSIQTSVNALSADVlgRCQVfEETQIGGERYNFFTGCPKAKTCTFILRGGA--EQFMEET 385
Cdd:PRK12851 316 qlgrakkvvvekenTTIIDGAGSKTEIEGRVAQI--RAQI-EETTSDYDREKLQERLAKLAGGVAVIRVGAstEVEVKEK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 386 ERSLHDAIMIVRRAIKnDSVVAGGGAIEMELSKYLrDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLR 465
Cdd:PRK12851 393 KDRVDDALHATRAAVE-EGIVPGGGVALLRAVKAL-DKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLR 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 5453607 466 arhaQGGTWYGVDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIKN 522
Cdd:PRK12851 471 ----EKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAE 523
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
197-377 |
3.06e-12 |
|
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: 66.86 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 197 IKKVQGGALEDSQLVAGVAFKKTFSYAGfeMqPKKYHNPKIALLNVELElkaekdnaeirVHTVE----DYQAIVDAEWN 272
Cdd:cd03334 52 IKKIPGGSPSDSEVVDGVVFTKNVAHKR--M-PSKIKNPRILLLQGPLE-----------YQRVEnkllSLDPVILQEKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 273 ILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALSAD-VLGRCQVFEET 351
Cdd:cd03334 118 YLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDLLTSpKLGTCESFRVR 197
|
170 180 190
....*....|....*....|....*....|.
gi 5453607 352 QIGGER-----YNFFTGCPKAKTCTFILRGG 377
Cdd:cd03334 198 TYVEEHgrsktLMFFEGCPKELGCTILLRGG 228
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
31-151 |
6.61e-12 |
|
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES cytosolic chaperonin. It is found in bacteria, organelles derived from bacteria, and occasionally in the Archaea. The bacterial GroEL/GroES group I chaperonin is replaced a group II chaperonin, usually called the thermosome in the Archaeota and CCT (chaperone-containing TCP) in the Eukaryota. GroEL, thermosome subunits, and CCT subunits all fall under the scope of pfam00118. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274089 Cd Length: 524 Bit Score: 67.70 E-value: 6.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 31 VIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHP----AAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLK 106
Cdd:TIGR02348 20 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVASKTNDVAGDGTTTATVLAQAIVK 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 5453607 107 QVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQ 151
Cdd:TIGR02348 100 EGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQ 144
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
33-530 |
2.35e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 65.98 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 33 AEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHP----AAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLKQV 108
Cdd:PRK12849 23 ADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQALVQEG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 109 KPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQrkllekCAMTAlsskliSQQKAFFAKMVVDAvmmldd 188
Cdd:PRK12849 103 LKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQ------VATIS------ANGDEEIGELIAEA------ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 189 llqLKMIGIKKV----QGGALEDS-QLVAGVAFKKTFSYAGFEMQPKKyhnpkiallnveleLKAEKDNAEIRVH----- 258
Cdd:PRK12849 165 ---MEKVGKDGVitveESKTLETElEVTEGMQFDRGYLSPYFVTDPER--------------MEAVLEDPLILLTdkkis 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 259 TVEDYQAIvdaewnilydkLEKIHHSG---------------AKVVLSK----LPIGDVATQYFADR------DM--FCA 311
Cdd:PRK12849 228 SLQDLLPL-----------LEKVAQSGkplliiaedvegealATLVVNKlrggLKVAAVKAPGFGDRrkamleDIaiLTG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 312 GRVPEEDLkrtmmacGGSIQTSvnalSADVLGRC-QVF---EETQI--GG------------------------------ 355
Cdd:PRK12849 297 GTVISEDL-------GLKLEEV----TLDDLGRAkRVTitkDNTTIvdGAgdkeaiearvaqirrqieettsdydreklq 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 356 ERYNFFTGcpkakTCTFILRGGA-EQFMEETERSLHDAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYsRTIPGKQQLL 434
Cdd:PRK12849 366 ERLAKLAG-----GVAVIKVGAAtEVELKERKDRVEDALNATRAAVE-EGIVPGGGVALLRAAKALDEL-AGLNGDQAAG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 435 IGAYAKALEIIPRQLCDNAGFDATNILNKLRaRHAQGgtwYGVDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIV 514
Cdd:PRK12849 439 VEIVRRALEAPLRQIAENAGLDGSVVVAKVL-ELEDG---FGFNAATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLL 514
|
570
....*....|....*.
gi 5453607 515 SVDETIknprstVDAP 530
Cdd:PRK12849 515 TTEALV------ADKP 524
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
31-151 |
3.79e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 62.45 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 31 VIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHP----AAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLK 106
Cdd:PRK00013 21 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLAQAIVR 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 5453607 107 QVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQ 151
Cdd:PRK00013 101 EGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQ 145
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
32-466 |
3.27e-07 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 53.00 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 32 IAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILK---LLDVVHPAAKTLVDIAKSQDAEV-GDGTTSVTLLAAEFLKQ 107
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKeveLEDPVENIGAKLVRQAAAKTNDLaGDGTTTSVVLAQGLIAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 108 VKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIavtvkkADKVEQRKLLEKCAMTALSSKLISQqkaffakMVVDAvmmld 187
Cdd:PLN03167 158 GVKVVAAGANPVQITRGIEKTAKALVKELKKM------SKEVEDSELADVAAVSAGNNYEVGN-------MIAEA----- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 188 dllqLKMIGIKKV----QGGALEDS-QLVAGVAFKKTFSYAGFEMQPKK----YHNPKIALLNVELElkaekdNAEIRVH 258
Cdd:PLN03167 220 ----MSKVGRKGVvtleEGKSAENNlYVVEGMQFDRGYISPYFVTDSEKmsveYDNCKLLLVDKKIT------NARDLIG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 259 TVED-----YQAIVDAEwNILYDKLEKI----HHSGAKVVLSKLP-IGDVATQYFADRDMFCAGRVPEEDLKRTMMACG- 327
Cdd:PLN03167 290 ILEDairggYPLLIIAE-DIEQEALATLvvnkLRGSLKIAALKAPgFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGk 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 328 ---------------------GSIQTSVNALSADVLGRCQVFEETQiggERYNFFTGCPKAKTCTFILRGGAEQFMEETE 386
Cdd:PLN03167 369 evlgtaakvvltkdtttivgdGSTQEAVNKRVAQIKNLIEAAEQDY---EKEKLNERIAKLSGGVAVIQVGAQTETELKE 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 387 RSL--HDAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYSRTIPGKQQlLIGAyakalEIIPRQLC-------DNAGFDA 457
Cdd:PLN03167 446 KKLrvEDALNATKAAVE-EGIVVGGGCTLLRLASKVDAIKDTLENDEQ-KVGA-----DIVKRALSyplkliaKNAGVNG 518
|
....*....
gi 5453607 458 TNILNKLRA 466
Cdd:PLN03167 519 SVVSEKVLS 527
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
405-513 |
4.85e-04 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 42.80 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453607 405 VVAGGGAIEMELSKYLrDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGgtwYGVDINNEDI 484
Cdd:PRK00013 410 IVPGGGVALLRAAPAL-EALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKG---YGYNAATGEY 485
|
90 100 110
....*....|....*....|....*....|
gi 5453607 485 ADNFEAFVWEPAMVRINAL-TAASEAACLI 513
Cdd:PRK00013 486 VDMIEAGIIDPTKVTRSALqNAASVAGLLL 515
|
|
| |
