|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
3-438 |
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: 903.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQRKLLEKCAMTALSSKLIS 82
Cdd:cd03340 86 VGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKEEQRELLEKCAATALNSKLIA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 83 QQKAFFAKMVVDAVMMLDDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFEMQPKKYHNPKIALLNVELELKAE 162
Cdd:cd03340 166 SEKEFFAKMVVDAVLSLDDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAGFEQQPKKFKNPKILLLNVELELKAE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 163 KDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGS 242
Cdd:cd03340 246 KDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGS 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 243 IQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGG 322
Cdd:cd03340 326 IQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGG 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 323 GAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQG-GTWYGVDINNEDIADNF 401
Cdd:cd03340 406 GAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGgGKWYGVDINNEGIADNF 485
|
410 420 430
....*....|....*....|....*....|....*..
gi 221042112 402 EAFVWEPAMVRINALTAASEAACLIVSVDETIKNPRS 438
Cdd:cd03340 486 EAFVWEPSLVKINALTAATEAACLILSVDETIKNPKS 522
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
3-438 |
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: 812.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKaDKVEQRKLLEKCAMTALSSKLIS 82
Cdd:TIGR02345 88 VGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDE-EKGEQRELLEKCAATALSSKLIS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 83 QQKAFFAKMVVDAVMMLD-DLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFEMQPKKYHNPKIALLNVELELKA 161
Cdd:TIGR02345 167 HNKEFFSKMIVDAVLSLDrDDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAGFEQQPKKFANPKILLLNVELELKA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 162 EKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGG 241
Cdd:TIGR02345 247 EKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGG 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 242 SIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAG 321
Cdd:TIGR02345 327 SIQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAG 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 322 GGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNEDIADNF 401
Cdd:TIGR02345 407 GGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNF 486
|
410 420 430
....*....|....*....|....*....|....*..
gi 221042112 402 EAFVWEPAMVRINALTAASEAACLIVSVDETIKNPRS 438
Cdd:TIGR02345 487 EAFVWEPALVKINALKAAFEAACTILSVDETITNPKS 523
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
3-434 |
1.00e-163 |
|
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: 469.60 E-value: 1.00e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADkveqRKLLEKCAMTALSSKLIS 82
Cdd:cd00309 78 VGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVED----REELLKVATTSLNSKLVS 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 83 QQKAFFAKMVVDAVMMLDDLLQ---LKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFemqPKKYHNPKIALLNVELEL 159
Cdd:cd00309 154 GGDDFLGELVVDAVLKVGKENGdvdLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYM---PKRLENAKILLLDCKLEY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 160 kaekdnaeirvhtvedyqaivdaewnilydklekihhsgakVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMAC 239
Cdd:cd00309 231 -----------------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKAT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 240 GGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVV 319
Cdd:cd00309 270 GATIVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 320 AGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNEDIAD 399
Cdd:cd00309 350 PGGGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVD 429
|
410 420 430
....*....|....*....|....*....|....*
gi 221042112 400 NFEAFVWEPAMVRINALTAASEAACLIVSVDETIK 434
Cdd:cd00309 430 MKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
3-434 |
2.77e-159 |
|
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: 459.36 E-value: 2.77e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEI-AVTVKKADkveqRKLLEKCAMTALSSKLI 81
Cdd:pfam00118 59 VGDGTTTVVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVD----REDLLKVARTSLSSKII 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 82 SQQKAFFAKMVVDAVMMLDDL---LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYagfEMQPKKYHNPKIALLNVELE 158
Cdd:pfam00118 135 SRESDFLAKLVVDAVLAIPKNdgsFDLGNIGVVKILGGSLEDSELVDGVVLDKGPLH---PDMPKRLENAKVLLLNCSLE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 159 LKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMA 238
Cdd:pfam00118 212 YEKTETKATVVLSDAEQLERFLKAEEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 239 CGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNDSV 318
Cdd:pfam00118 292 TGARAVSSLDDLTPDDLGTAGKVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRV 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 319 VAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNEDIA 398
Cdd:pfam00118 372 VPGGGAVEMELARALREYAKSVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEII 451
|
410 420 430
....*....|....*....|....*....|....*.
gi 221042112 399 DNFEAFVWEPAMVRINALTAASEAACLIVSVDETIK 434
Cdd:pfam00118 452 DMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIK 487
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
3-433 |
3.32e-124 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 370.82 E-value: 3.32e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADkveqRKLLEKCAMTALSSKLIS 82
Cdd:NF041083 87 VGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDD----RETLKKIAETSLTSKGVE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 83 QQKAFFAKMVVDAVMMLDDL------LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFemqPKKYHNPKIALLNVE 156
Cdd:NF041083 163 EARDYLAEIAVKAVKQVAEKrdgkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGM---PKRVENAKIALLDAP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 157 LELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTM 236
Cdd:NF041083 240 LEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLA 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 237 MACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKND 316
Cdd:NF041083 320 KATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDG 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 317 SVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNED 396
Cdd:NF041083 400 KIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGE 479
|
410 420 430
....*....|....*....|....*....|....*..
gi 221042112 397 IADNFEAFVWEPAMVRINALTAASEAACLIVSVDETI 433
Cdd:NF041083 480 VVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVI 516
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
3-434 |
4.87e-122 |
|
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: 365.43 E-value: 4.87e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADkveqRKLLEKCAMTALSSKLIS 82
Cdd:cd03343 85 VGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDD----KDTLRKIAKTSLTGKGAE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 83 QQKAFFAKMVVDAVMMLDDL------LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFemqPKKYHNPKIALLNVE 156
Cdd:cd03343 161 AAKDKLADLVVDAVLQVAEKrdgkyvVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGM---PKRVENAKIALLDAP 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 157 LELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTM 236
Cdd:cd03343 238 LEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 237 MACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKND 316
Cdd:cd03343 318 RATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDG 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 317 SVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNED 396
Cdd:cd03343 398 KVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGE 477
|
410 420 430
....*....|....*....|....*....|....*...
gi 221042112 397 IADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIK 434
Cdd:cd03343 478 VVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIA 515
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
3-433 |
5.76e-121 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 362.67 E-value: 5.76e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKveqrKLLEKCAMTALSSKLIS 82
Cdd:NF041082 87 VGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDK----ETLKKIAATAMTGKGAE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 83 QQKAFFAKMVVDAVMMLDD-----LLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGfeMqPKKYHNPKIALLNVEL 157
Cdd:NF041082 163 AAKDKLADLVVDAVKAVAEkdggyNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPG--M-PKRVENAKIALLDAPL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 158 ELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMM 237
Cdd:NF041082 240 EVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAK 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 238 ACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNDS 317
Cdd:NF041082 320 ATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGK 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 318 VVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNEDI 397
Cdd:NF041082 400 VVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKV 479
|
410 420 430
....*....|....*....|....*....|....*.
gi 221042112 398 ADNFEAFVWEPAMVRINALTAASEAACLIVSVDETI 433
Cdd:NF041082 480 VDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVI 515
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
3-436 |
7.69e-107 |
|
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: 326.55 E-value: 7.69e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKE-IAVTVKKADkveqRKLLEKCAMTALSSKLI 81
Cdd:cd03335 78 VGDGTTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDNLG----KESLINVAKTSMSSKII 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 82 SQQKAFFAKMVVDAVM---MLDDLLQ----LKMIGIKKVQGGALEDSQLVAGVAFKKTFsyAGFEMqPKKYHNPKIALLN 154
Cdd:cd03335 154 GADSDFFANMVVDAILavkTTNEKGKtkypIKAVNILKAHGKSAKESYLVNGYALNCTR--ASQGM-PTRVKNAKIACLD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 155 VELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKR 234
Cdd:cd03335 231 FNLQKTKMKLGVQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 235 TMMACGGSIQTSVNAL------SADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMI 308
Cdd:cd03335 311 IAKATGATLVSTLANLegeetfDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCV 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 309 VRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHA------ 382
Cdd:cd03335 391 VKRTLESNSVVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAaaqvkp 470
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 221042112 383 --QGGTWYGVDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIK-NP 436
Cdd:cd03335 471 dkKHLKWYGLDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIKlNP 527
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
3-437 |
2.38e-104 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 320.44 E-value: 2.38e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKkADKVEQRKLLEKCAMTALSSKLIS 82
Cdd:PTZ00212 97 VGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHG-SDEEKFKEDLLNIARTTLSSKLLT 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 83 QQKAFFAKMVVDAVMMLDDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAgfemQPKKYHNPKIALLNVELEL-KA 161
Cdd:PTZ00212 176 VEKDHFAKLAVDAVLRLKGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVG----QPKRLENCKILVANTPMDTdKI 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 162 EKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGG 241
Cdd:PTZ00212 252 KIYGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGA 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 242 SIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAG 321
Cdd:PTZ00212 332 EIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKDTRVVLG 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 322 GGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNEDIADNF 401
Cdd:PTZ00212 412 GGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGIDMEKGTVGDMK 491
|
410 420 430
....*....|....*....|....*....|....*..
gi 221042112 402 EAFVWEPAMVRINALTAASEAACLIVSVDETIKN-PR 437
Cdd:PTZ00212 492 ELGITESYKVKLSQLCSATEAAEMILRVDDIIRCaPR 528
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
3-434 |
1.08e-102 |
|
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: 316.28 E-value: 1.08e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEiaVTVKKADKVeQRKLLEKCAMTALSSKLIS 82
Cdd:TIGR02340 82 VGDGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKE--NLSVSVDEL-GREALINVAKTSMSSKIIG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 83 QQKAFFAKMVVDAVM-------MLDDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFsyAGFEMqPKKYHNPKIALLNV 155
Cdd:TIGR02340 159 LDSDFFSNIVVDAVLavkttneNGETKYPIKAINILKAHGKSARESMLVKGYALNCTV--ASQQM-PKRIKNAKIACLDF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 156 ELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRT 235
Cdd:TIGR02340 236 NLQKAKMALGVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRI 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 236 MMACGGSIQTSV------NALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIV 309
Cdd:TIGR02340 316 AKATGATLVSTLadlegeETFEASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVV 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 310 RRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHA------- 382
Cdd:TIGR02340 396 KRTLESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAaaqlkpe 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 221042112 383 -QGGTWYGVDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIK 434
Cdd:TIGR02340 476 kKHLKWYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIK 528
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
3-437 |
5.68e-102 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239452 [Multi-domain] Cd Length: 517 Bit Score: 313.88 E-value: 5.68e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKkADKVEQRKLLEKCAMTALSSKLIS 82
Cdd:cd03336 85 VGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHS-SDEEAFREDLLNIARTTLSSKILT 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 83 QQKAFFAKMVVDAVMMLDDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAgfemQPKKYHNPKIALLNVELEL-KA 161
Cdd:cd03336 164 QDKEHFAELAVDAVLRLKGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVN----QPKRIENAKILIANTPMDTdKI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 162 EKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGG 241
Cdd:cd03336 240 KIFGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTGG 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 242 SIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAG 321
Cdd:cd03336 320 EIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRVVLG 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 322 GGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNEDIADNF 401
Cdd:cd03336 400 GGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTVGDMK 479
|
410 420 430
....*....|....*....|....*....|....*..
gi 221042112 402 EAFVWEPAMVRINALTAASEAACLIVSVDETIK-NPR 437
Cdd:cd03336 480 ELGITESFKVKRQVLLSASEAAEMILRVDDIIKcAPR 516
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
3-433 |
1.27e-88 |
|
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: 278.02 E-value: 1.27e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKkadkVEQRKLLEKCAMTALSSKLIS 82
Cdd:cd03337 86 VGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVD----VNDRAQMLKIIKSCIGTKFVS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 83 QQKAFFAKMVVDAVMM--LDDLLQLKMIGIK------KVQGGALEDSQLVAGVAFKKTFSYAGfeMQpKKYHNPKIALLN 154
Cdd:cd03337 162 RWSDLMCNLALDAVKTvaVEENGRKKEIDIKryakveKIPGGEIEDSRVLDGVMLNKDVTHPK--MR-RRIENPRIVLLD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 155 VELElkaekdnaeirvhtvedyqaivdaewnilYdklekihhsgakVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKR 234
Cdd:cd03337 239 CPLE-----------------------------Y------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 235 TMMACGGSIQTSVNALSADVLG-RCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAI 313
Cdd:cd03337 278 IARACGATIVNRPEELTESDVGtGAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNII 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 314 KNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQ-GGTWYGVDI 392
Cdd:cd03337 358 LNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQgENSTWGIDG 437
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 221042112 393 NNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETI 433
Cdd:cd03337 438 ETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
3-433 |
1.24e-84 |
|
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: 269.30 E-value: 1.24e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQRKLLEKCamtaLSSKLIS 82
Cdd:TIGR02344 86 VGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSC----IGTKFVS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 83 QQKAFFAKMVVDAVMMLDDLLQLKM-IGIK------KVQGGALEDSQLVAGVAFKKTFSYAgfEMQpKKYHNPKIALLNV 155
Cdd:TIGR02344 162 RWSDLMCDLALDAVRTVQRDENGRKeIDIKryakveKIPGGDIEDSCVLKGVMINKDVTHP--KMR-RYIENPRIVLLDC 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 156 ELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRT 235
Cdd:TIGR02344 239 PLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRI 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 236 MMACGGSIQTSVNAL-SADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIK 314
Cdd:TIGR02344 319 ARACGATIVNRPEELrESDVGTGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLL 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 315 NDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGT-WYGVDIN 393
Cdd:TIGR02344 399 DPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNcTWGIDGE 478
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 221042112 394 NEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETI 433
Cdd:TIGR02344 479 TGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
4-433 |
5.32e-83 |
|
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: 264.53 E-value: 5.32e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 4 GDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADkveqRKLLEKCAMTALSSKLISQ 83
Cdd:cd03338 79 GDGTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLND----RESLIKSATTSLNSKVVSQ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 84 QKAFFAKMVVDAVMMLDDL-----LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGfeMQPKKYHNPKIALlnVELE 158
Cdd:cd03338 155 YSSLLAPIAVDAVLKVIDPatatnVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKA--GGPTRIEKAKIGL--IQFC 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 159 LKAEKDNAEIRVhTVEDYQA---IVDAEWNILYDKLEKIHHSGAKVVL---SKL--PIGDVATQYFADRDMFCAGRVPEE 230
Cdd:cd03338 231 LSPPKTDMDNNI-VVNDYAQmdrILREERKYILNMCKKIKKSGCNVLLiqkSILrdAVSDLALHFLAKLKIMVVKDIERE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 231 DLKRTMMACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKA-KTCTFILRGGAEQFMEETERSLHDAIMIV 309
Cdd:cd03338 310 EIEFICKTIGCKPVASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVI 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 310 RRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYG 389
Cdd:cd03338 390 RCLVKKRALIPGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAG 469
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 221042112 390 VDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETI 433
Cdd:cd03338 470 INVRKGAITNILEENVVQPLLVSTSAITLATETVRMILKIDDIV 513
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
3-438 |
1.84e-82 |
|
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: 263.64 E-value: 1.84e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTvKKADKVEQRKLLEKCAMTALSSKLIS 82
Cdd:TIGR02341 86 VGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVD-NGSDEVKFRQDLMNIARTTLSSKILS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 83 QQKAFFAKMVVDAVMMLDDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYagfeMQPKKYHNPKIALLNVELEL-KA 161
Cdd:TIGR02341 165 QHKDHFAQLAVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGV----NQPKRIENAKILIANTGMDTdKV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 162 EKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGG 241
Cdd:TIGR02341 241 KIFGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 242 SIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAG 321
Cdd:TIGR02341 321 EIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLG 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 322 GGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNEDIADNF 401
Cdd:TIGR02341 401 GGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGTIADMR 480
|
410 420 430
....*....|....*....|....*....|....*...
gi 221042112 402 EAFVWEPAMVRINALTAASEAACLIVSVDETIK-NPRS 438
Cdd:TIGR02341 481 QLGITESYKVKRAVVSSAAEAAEVILRVDNIIKaAPRK 518
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
4-431 |
7.28e-81 |
|
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: 259.33 E-value: 7.28e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 4 GDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADkveqRKLLEKCAMTALSSKLISQ 83
Cdd:TIGR02342 80 GDGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSD----REQLLKSATTSLSSKVVSQ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 84 QKAFFAKMVVDAVMMLDDL-----LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAgfEMQPKKYHNPKIALlnVELE 158
Cdd:TIGR02342 156 YSSLLAPLAVDAVLKVIDPenaknVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKS--AGGPTRIEKAKIGL--IQFQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 159 LKAEKDNAEIRVhTVEDYQA---IVDAEWNILYDKLEKIHHSGAKVVLSKLPI-----GDVATQYFADRDMFCAGRVPEE 230
Cdd:TIGR02342 232 ISPPKTDMENQI-IVNDYAQmdrVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIERE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 231 DLKRTMMACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKA-KTCTFILRGGAEQFMEETERSLHDAIMIV 309
Cdd:TIGR02342 311 EIEFICKTIGCKPIASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVI 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 310 RRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYG 389
Cdd:TIGR02342 391 RCLVKKRGLIAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAG 470
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 221042112 390 VDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDE 431
Cdd:TIGR02342 471 ISVRKGGITNMLEEHVLQPLLVTTSAITLASETVRSILKIDD 512
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
3-434 |
3.23e-76 |
|
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: 247.21 E-value: 3.23e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADkvEQRKLLEKCAMTALSSKLIS 82
Cdd:cd03339 93 IGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSP--DNKEPLIQTAMTSLGSKIVS 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 83 QQKAFFAKMVVDAVMMLDDL----LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAgfEMqPKKYHNPKIALLNVELE 158
Cdd:cd03339 171 RCHRQFAEIAVDAVLSVADLerkdVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHP--QM-PKEVKDAKIAILTCPFE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 159 LKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMA 238
Cdd:cd03339 248 PPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 239 CGGSIQTSVNALSADVLGRCQVFEETQIGG--ERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKND 316
Cdd:cd03339 328 TGGRIVPRFEDLSPEKLGKAGLVREISFGTtkDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDN 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 317 SVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGT-WYGVDINNE 395
Cdd:cd03339 408 RIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNpHLGIDCLGR 487
|
410 420 430
....*....|....*....|....*....|....*....
gi 221042112 396 DIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIK 434
Cdd:cd03339 488 GTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
65-315 |
4.37e-70 |
|
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. This superfamily also contains related domains from Fab1-like phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinases that only contain the intermediate and apical domains.
Pssm-ID: 239449 [Multi-domain] Cd Length: 209 Bit Score: 221.19 E-value: 4.37e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 65 RKLLEKCAMTALSSKlISQQKAFFAKMVVDAVMMLDDLLQ---LKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFemq 141
Cdd:cd03333 1 RELLLQVATTSLNSK-LSSWDDFLGKLVVDAVLKVGPDNRmddLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYM--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 142 PKKYHNPKIALLNVELELkaekdnaeirvhtvedyqaivdaewnilydklekihhsgakVVLSKLPIGDVATQYFADRDM 221
Cdd:cd03333 77 PKRLENAKILLLDCPLEY-----------------------------------------VVIAEKGIDDLALHYLAKAGI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 222 FCAGRVPEEDLKRTMMACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERS 301
Cdd:cd03333 116 MAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRS 195
|
250
....*....|....
gi 221042112 302 LHDAIMIVRRAIKN 315
Cdd:cd03333 196 LHDALCAVRAAVEE 209
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
3-435 |
2.14e-69 |
|
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: 229.69 E-value: 2.14e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVkkADKVEQRKLLEKCAMTALSSKLIS 82
Cdd:TIGR02343 97 IGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEI--SADNNNREPLIQAAKTSLGSKIVS 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 83 QQKAFFAKMVVDAVMMLDDL----LQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAgfEMqPKKYHNPKIALLNVELE 158
Cdd:TIGR02343 175 KCHRRFAEIAVDAVLNVADMerrdVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHP--QM-PKEVEDAKIAILTCPFE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 159 LKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMA 238
Cdd:TIGR02343 252 PPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIA 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 239 CGGSIQTSVNALSADVLGRCQVFEETQIG--GERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKND 316
Cdd:TIGR02343 332 TGGRIVPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDS 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 317 SVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARH-AQGGTWYGVDINNE 395
Cdd:TIGR02343 412 RIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQlKEKNPNLGVDCLGY 491
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 221042112 396 DIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIKN 435
Cdd:TIGR02343 492 GTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVISP 531
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
3-433 |
1.07e-67 |
|
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: 223.64 E-value: 1.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAV-TVKKADKVEQrklLEKCAMTALSSKLI 81
Cdd:cd03341 78 IGDGTNLVVVLAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVyKIEDLRNKEE---VSKALKTAIASKQY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 82 SQQkAFFAKMVVDAVMML----DDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKtfsyaGFEMQPKKYHNPKIALLNVEL 157
Cdd:cd03341 155 GNE-DFLSPLVAEACISVlpenIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKR-----EPEGSVKRVKKAKVAVFSCPF 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 158 ELkaekdnaeirvhtvedyqaivdaewnilydklekihhsGAKVVLSKLPIGDVAtQYFADRDMFCAGRVPEE-DLKRTM 236
Cdd:cd03341 229 DI--------------------------------------GVNVIVAGGSVGDLA-LHYCNKYGIMVIKINSKfELRRLC 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 237 MACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKA-KTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKN 315
Cdd:cd03341 270 RTVGATPLPRLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDsKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 316 DSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNE 395
Cdd:cd03341 350 GRFVPGAGATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESG 429
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 221042112 396 DIA--DNFEAFVWEPAMVRINALTAASEAACLIVSVDETI 433
Cdd:cd03341 430 DEGtkDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
3-433 |
3.05e-66 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 220.33 E-value: 3.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVtvkkadKVEQRKLLEKCAMTALSSKlis 82
Cdd:COG0459 84 AGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAK------PVDDKEELAQVATISANGD--- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 83 qqkAFFAKMVVDAVMMLDdllqlKMIGIKKVQGGALE-DSQLVAGVAFKKTFSYAGF----EMQPKKYHNPKIALLNVEL 157
Cdd:COG0459 155 ---EEIGELIAEAMEKVG-----KDGVITVEEGKGLEtELEVVEGMQFDKGYLSPYFvtdpEKMPAELENAYILLTDKKI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 158 ELKAEkdnaeirvhtvedyqaivdaewniLYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVP--------- 228
Cdd:COG0459 227 SSIQD------------------------LLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVavkapgfgd 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 229 --EEDLKRTMMACGGSIQT-----SVNALSADVLGRCqvfEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERS 301
Cdd:COG0459 283 rrKAMLEDIAILTGGRVISedlglKLEDVTLDDLGRA---KRVEVDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRR 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 302 LHDAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRarh 381
Cdd:COG0459 360 VEDALHATRAAVE-EGIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVR--- 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 221042112 382 AQGGTWYGVDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETI 433
Cdd:COG0459 436 AAKDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVI 487
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
3-433 |
9.64e-66 |
|
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: 219.97 E-value: 9.64e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTvkKADKVEQRKLLEKCAMTALSSKLIS 82
Cdd:TIGR02346 88 IGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVW--EVKDLRDKDELIKALKASISSKQYG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 83 QQKaFFAKMVVDAVMML----DDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFsyagfEMQPKKYHNPKIALLNVELE 158
Cdd:TIGR02346 166 NED-FLAQLVAQACSTVlpknPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNREA-----EGSVKSVKNAKVAVFSCPLD 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 159 LKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVAtQYFADRDMFCAGRVPEE-DLKRTMM 237
Cdd:TIGR02346 240 TATTETKGTVLIHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMA-LHYLNKYNIMVLKIPSKfELRRLCK 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 238 ACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPK-AKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKND 316
Cdd:TIGR02346 319 TVGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGdSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDG 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 317 SVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNED 396
Cdd:TIGR02346 399 RLLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAES 478
|
410 420 430
....*....|....*....|....*....|....*....
gi 221042112 397 IA--DNFEAFVWEPAMVRINALTAASEAACLIVSVDETI 433
Cdd:TIGR02346 479 DGvkDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQII 517
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
3-434 |
4.68e-65 |
|
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: 216.74 E-value: 4.68e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFrtatQLAVNKIKEIAVTVKKADKVEQ-RKLLEKCAMTALSSKLI 81
Cdd:cd03342 82 TGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGF----ELAKNKALKFLESFKVPVEIDTdRELLLSVARTSLRTKLH 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 82 SQQKAFFAKMVVDAVMML---DDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAgfEMqPKKYHNPKIALLNVELE 158
Cdd:cd03342 158 ADLADQLTEIVVDAVLAIykpDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHP--DM-PKRVENAYILTCNVSLE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 159 lkaekdnaeirvhtvedyqaivdaewnilYDKLEKihHSG--AKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTM 236
Cdd:cd03342 235 -----------------------------YEKTEV--NSGffYSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLT 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 237 MACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKND 316
Cdd:cd03342 284 LACGGVAMNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDK 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 317 SVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNED 396
Cdd:cd03342 364 CVVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGE 443
|
410 420 430
....*....|....*....|....*....|....*...
gi 221042112 397 IADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIK 434
Cdd:cd03342 444 PMDPESEGIWDNYSVKRQILHSATVIASQLLLVDEIIR 481
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
3-439 |
8.80e-65 |
|
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: 217.29 E-value: 8.80e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 3 VGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEiaVTVKKADKVEqRKLLEKCAMTALSSKLIS 82
Cdd:TIGR02347 86 TGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDK--FKVKKEDEVD-REFLLNVARTSLRTKLPA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 83 QQKAFFAKMVVDAVMML---DDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFemqPKKYHNPKIALLNVELEL 159
Cdd:TIGR02347 163 DLADQLTEIVVDAVLAIkkdGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDM---PRRVKNAYILTCNVSLEY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 160 KAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIG-DVATQ---------YFADRDMFCAGRVPE 229
Cdd:TIGR02347 240 EKTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCGKSPDKGfVVINQkgidppsldLLAKEGIMALRRAKR 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 230 EDLKRTMMACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIV 309
Cdd:TIGR02347 320 RNMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAV 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 310 RRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYG 389
Cdd:TIGR02347 400 KNAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVG 479
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 221042112 390 VDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIKNPRST 439
Cdd:TIGR02347 480 VDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSM 529
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
110-290 |
2.32e-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: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 110 IKKVQGGALEDSQLVAGVAFKKTFSYAGfeMqPKKYHNPKIALLNVELElkaekdnaeirVHTVE----DYQAIVDAEWN 185
Cdd:cd03334 52 IKKIPGGSPSDSEVVDGVVFTKNVAHKR--M-PSKIKNPRILLLQGPLE-----------YQRVEnkllSLDPVILQEKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 186 ILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALSAD-VLGRCQVFEET 264
Cdd:cd03334 118 YLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDLLTSpKLGTCESFRVR 197
|
170 180 190
....*....|....*....|....*....|.
gi 221042112 265 QIGGER-----YNFFTGCPKAKTCTFILRGG 290
Cdd:cd03334 198 TYVEEHgrsktLMFFEGCPKELGCTILLRGG 228
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
4-432 |
2.00e-10 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 62.81 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 4 GDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQrkllekcaMTALSSKlisq 83
Cdd:CHL00093 85 GDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQ--------VASISAG---- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 84 QKAFFAKMVVDAvmmLDDLLQLKMIGIKKVQGGALEdSQLVAGVAFKKTFSYAGFEMQPKK----YHNP-------KIAL 152
Cdd:CHL00093 153 NDEEVGSMIADA---IEKVGREGVISLEEGKSTVTE-LEITEGMRFEKGFISPYFVTDTERmevvQENPyilltdkKITL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 153 LNVELELKAEKDNAEIR--VHTVEDYQAivDAEWNILYDKLEKIhhsgAKVVLSKLP-IGDVATQYFADRDMFCAGRVPE 229
Cdd:CHL00093 229 VQQDLLPILEQVTKTKRplLIIAEDVEK--EALATLVLNKLRGI----VNVVAVRAPgFGDRRKAMLEDIAILTGGQVIT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 230 ED----LKR-TMMACGGSIQTSVN---------ALSADVLGRC----QVFEETQIGGERYNFFTGCPKAKTCTFILRGGA 291
Cdd:CHL00093 303 EDaglsLETiQLDLLGQARRIIVTkdsttiiadGNEEQVKARCeqlrKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGA 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 292 --EQFMEETERSLHDAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYSRTiPGKQQLLIGAY--AKALEIIPRQLCDNAG 367
Cdd:CHL00093 383 atETEMKDKKLRLEDAINATKAAVE-EGIVPGGGATLVHLSENLKTWAKN-NLKEDELIGALivARAILAPLKRIAENAG 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221042112 368 FDATNILNKLRARHAQggtwYGVDINNEDIADNFEAFVWEPAMVRINAL-TAASEAA------CLIVSVDET 432
Cdd:CHL00093 461 KNGSVIIEKVQEQDFE----IGYNAANNKFVNMYEAGIIDPAKVTRSALqNAASIASmiltteCIIVDKKES 528
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
4-426 |
9.89e-10 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 60.70 E-value: 9.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 4 GDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADkveqrkLLEKCAMTALS-----S 78
Cdd:PTZ00114 97 GDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKE------DILNVATISANgdveiG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 79 KLISQQkafFAKMVVDAVMMLDDllqlkmigikkvqGGALEDS-QLVAGVAFkktfsyagfemqPKKYHNPkiALLNVEL 157
Cdd:PTZ00114 171 SLIADA---MDKVGKDGTITVED-------------GKTLEDElEVVEGMSF------------DRGYISP--YFVTNEK 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 158 ELKAEKDNAEIRVHT--VEDYQAIV----------------------DAEWNILYDKLekihHSGAKVVLSKLP-IGDVA 212
Cdd:PTZ00114 221 TQKVELENPLILVTDkkISSIQSILpilehavknkrplliiaedvegEALQTLIINKL----RGGLKVCAVKAPgFGDNR 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 213 TQYFADRDMFCAGRVPEEDL-----------------------KRTMMACGG----SIQTSVNALSaDVLGRCQVFEETQ 265
Cdd:PTZ00114 297 KDILQDIAVLTGATVVSEDNvglklddfdpsmlgsakkvtvtkDETVILTGGgdkaEIKERVELLR-SQIERTTSEYDKE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 266 IGGERYNFFTGcpkaKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNdSVVAGGGAIEMELSKYLrDY---SRTIPG 342
Cdd:PTZ00114 376 KLKERLAKLSG----GVAVIKVGGASEVEVNEKKDRIEDALNATRAAVEE-GIVPGGGVALLRASKLL-DKleeDNELTP 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 343 KQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARhaqGGTWYGVDINNEDIADNFEAFVWEPAMVRINALTAASEA 422
Cdd:PTZ00114 450 DQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEK---KDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASV 526
|
....
gi 221042112 423 ACLI 426
Cdd:PTZ00114 527 ASLM 530
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
2-443 |
1.76e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 59.86 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 2 MVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQRKLLEKCAMTALSsKLI 81
Cdd:PRK12852 84 LAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIG-KMI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 82 SQQkafFAKMVVDAVMMLDDllqlkmigikkvqGGALE-DSQLVAGVAFKKTFSYAGFEMQPKKY-----------HNPK 149
Cdd:PRK12852 163 AQA---MQKVGNEGVITVEE-------------NKSLEtEVDIVEGMKFDRGYLSPYFVTNAEKMtvelddayillHEKK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 150 IALLNVELE-LKAEKDNAEIRVHTVEDYQAivDAEWNILYDKLEkihhSGAKVVLSKLP-IGDVATQYFADRDMFCAGRV 227
Cdd:PRK12852 227 LSGLQAMLPvLEAVVQSGKPLLIIAEDVEG--EALATLVVNRLR----GGLKVAAVKAPgFGDRRKAMLEDIAILTGGQL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 228 PEEDL---------------KR-------TMMACGGSIQTSVNALSADVlgRCQVfEETQIGGERYNFFTGCPKAKTCTF 285
Cdd:PRK12852 301 ISEDLgiklenvtlkmlgraKKvvidkenTTIVNGAGKKADIEARVGQI--KAQI-EETTSDYDREKLQERLAKLAGGVA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 286 ILR-GGA-EQFMEETERSLHDAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYSRTIPgKQQLLIGAYAKALEIIPRQLC 363
Cdd:PRK12852 378 VIRvGGAtEVEVKEKKDRVEDALNATRAAVQ-EGIVPGGGVALLRAKKAVGRINNDNA-DVQAGINIVLKALEAPIRQIA 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 364 DNAGFDATNILNKLRARHAQGgtwYGVDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIKNPRSTVDAP 443
Cdd:PRK12852 456 ENAGVEGSIVVGKILENKSET---FGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDAAP 532
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
2-443 |
4.12e-08 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 55.42 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 2 MVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQrkllekcaMTALSSKLI 81
Cdd:PRK14104 84 AAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQ--------VGTISANGD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 82 SQQKAFFAkmvvdavmmlDDLLQLKMIGIKKVQGGALEDSQL--VAGVAFKKTFSYAGFEMQPKKY-----------HNP 148
Cdd:PRK14104 156 AEIGKFLA----------DAMKKVGNEGVITVEEAKSLETELdvVEGMQFDRGYISPYFVTNADKMrvemddayiliNEK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 149 KIALLNVELEL-KAEKDNAEIRVHTVEDYQAivDAEWNILYDKLEkihhSGAKVVLSKLP-IGDVATQYFADRDMFCAGR 226
Cdd:PRK14104 226 KLSSLNELLPLlEAVVQTGKPLVIVAEDVEG--EALATLVVNRLR----GGLKVAAVKAPgFGDRRKAMLQDIAILTGGQ 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 227 VPEEDL---------------KRTMMACGGSIQTSVNALSADVLGR-CQV---FEETQIGGERYNFFTGCPKAKTCTFIL 287
Cdd:PRK14104 300 AISEDLgiklenvtlqmlgraKKVMIDKENTTIVNGAGKKADIEARvAQIkaqIEETTSDYDREKLQERLAKLAGGVAVI 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 288 RGGAEQFMEETERS--LHDAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYsRTIPGKQQLLIGAYAKALEIIPRQLCDN 365
Cdd:PRK14104 380 RVGGATEVEVKERKdrVDDAMHATRAAVE-EGIVPGGGVALLRASEQLKGI-KTKNDDQKTGVEIVRKALSAPARQIAIN 457
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221042112 366 AGFDATNILNKLRARHAQGgtwYGVDINNEDIADNFEAFVWEPA-MVRINALTAASEAACLIVSVDETIKNPRSTVDAP 443
Cdd:PRK14104 458 AGEDGSVIVGKILEKEQYS---YGFDSQTGEYGNLVSKGIIDPTkVVRTAIQNAASVAALLITTEAMVAELPKKGGAGP 533
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
2-426 |
3.06e-07 |
|
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: 52.46 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 2 MVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQrkllekCAMTALSS--- 78
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQ------VATISANGdee 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 79 --KLISQQkafFAKMVVDAVMMLDDllqlkmigikkvqGGALEDS-QLVAGVAFKKTFSYAGFEMQPKK----YHNPKIa 151
Cdd:cd03344 155 igELIAEA---MEKVGKDGVITVEE-------------GKTLETElEVVEGMQFDRGYLSPYFVTDPEKmeveLENPYI- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 152 lLNVELELKAEKDNAEIRVHTV----------EDyqaiVDAEW--NILYDKLEKihhsGAKVVLSKLP---------IGD 210
Cdd:cd03344 218 -LLTDKKISSIQELLPILELVAkagrplliiaED----VEGEAlaTLVVNKLRG----GLKVCAVKAPgfgdrrkamLED 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 211 VAT----QYFADRDMFCAGRVPEEDLKR-----------TMMACGGSiqtsvnalSADVLGRCQV----FEETQIGGERY 271
Cdd:cd03344 289 IAIltggTVISEELGLKLEDVTLEDLGRakkvvvtkddtTIIGGAGD--------KAAIKARIAQirkqIEETTSDYDKE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 272 NF------FTGcpkaKTCTfILRGGA-EQFMEETERSLHDAIMIVRRAIKnDSVVAGGGAIEMELSKYLrDYSRTIPGKQ 344
Cdd:cd03344 361 KLqerlakLSG----GVAV-IKVGGAtEVELKEKKDRVEDALNATRAAVE-EGIVPGGGVALLRASPAL-DKLKALNGDE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 345 QLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRArHAQGgtwYGVDINNEDIADNFEAFVWEPAMVRINALTAASEAAC 424
Cdd:cd03344 434 KLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLE-SPDG---FGYDAATGEYVDMIEAGIIDPTKVVRSALQNAASVAS 509
|
..
gi 221042112 425 LI 426
Cdd:cd03344 510 LL 511
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
2-446 |
5.84e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 51.64 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 2 MVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQrklleKCAMTALSSKLI 81
Cdd:PRK12850 84 LAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQ-----VATISANGDESI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 82 SQqkaffakMVVDAVmmlDDLLQLKMIGIKKVQGGALEdSQLVAGVAFKKTFSYAGFEMQPKKY-----------HNPKI 150
Cdd:PRK12850 159 GE-------MIAEAM---DKVGKEGVITVEEAKTLGTE-LDVVEGMQFDRGYLSPYFVTNPEKMraeledpyillHEKKI 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 151 ALLNVELE-LKAEKDNAEIRVHTVEDyqaiVDAE--WNILYDKLekihHSGAKVVLSKLP-IGDVATQYFADRDMFCAGR 226
Cdd:PRK12850 228 SNLQDLLPiLEAVVQSGRPLLIIAED----VEGEalATLVVNKL----RGGLKSVAVKAPgFGDRRKAMLEDIAVLTGGQ 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 227 VPEEDL---------------------KRTMMACGGS-----IQTSVNALSADVlgrcqvfEETQIGGERYNFFTGCPKA 280
Cdd:PRK12850 300 VISEDLgiklenvtldmlgrakrvlitKENTTIIDGAgdkknIEARVKQIRAQI-------EETTSDYDREKLQERLAKL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 281 KTCTFILRGGAEQFMEETERSLH--DAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYsRTIPGKQQLLIGAYAKALEII 358
Cdd:PRK12850 373 AGGVAVIRVGGATEVEVKEKKDRvdDALHATRAAVE-EGIVPGGGVALLRARSALRGL-KGANADETAGIDIVRRALEEP 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 359 PRQLCDNAGFDATNILNKLrarhAQGGTWYGVDINNEDIADNFEAFVWEPAMVRINAL-TAASEAACLIVS----VDETI 433
Cdd:PRK12850 451 LRQIATNAGFEGSVVVGKV----AELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALqDAASIAALLITTeamvAEAPK 526
|
490
....*....|...
gi 221042112 434 KNPRSTVDAPTAA 446
Cdd:PRK12850 527 KAAAAAAGPGPGM 539
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
318-426 |
3.38e-04 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 42.80 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042112 318 VVAGGGAIEMELSKYLrDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGgtwYGVDINNEDI 397
Cdd:PRK00013 410 IVPGGGVALLRAAPAL-EALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKG---YGYNAATGEY 485
|
90 100 110
....*....|....*....|....*....|
gi 221042112 398 ADNFEAFVWEPAMVRINAL-TAASEAACLI 426
Cdd:PRK00013 486 VDMIEAGIIDPTKVTRSALqNAASVAGLLL 515
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
4-64 |
6.58e-03 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 38.95 E-value: 6.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221042112 4 GDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQ 64
Cdd:PRK00013 85 GDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQ 145
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