|
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: 1085.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 5 PVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAK 84
Cdd:cd03340 1 PIILLKEGTDTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 85 SQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKQDKVEQRKMLEKCAMTALS 164
Cdd:cd03340 81 SQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKEEQRELLEKCAATALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 165 SKLISQQKVFFAKMVVDAVMMLDELLQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAGFEMQPKKYKNPKIALLNVEL 244
Cdd:cd03340 161 SKLIASEKEFFAKMVVDAVLSLDDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAGFEQQPKKFKNPKILLLNVEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 245 ELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHQSGAKVILSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMM 324
Cdd:cd03340 241 ELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 325 ACGGSIQTSVNALVPDVLGHCQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDS 404
Cdd:cd03340 321 ATGGSIQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 405 VVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQG-GMWYGVDINNEN 483
Cdd:cd03340 401 VVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGgGKWYGVDINNEG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 238814391 484 IADNFQAFVWEPAMVRINALTAASEAACLIVSVDETIKNPRS 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: 965.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 3 PTPVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDI 82
Cdd:TIGR02345 1 RPTIVLLKEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 83 AKSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVkKQDKVEQRKMLEKCAMTA 162
Cdd:TIGR02345 81 AKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTI-DEEKGEQRELLEKCAATA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 163 LSSKLISQQKVFFAKMVVDAVMMLD-ELLQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAGFEMQPKKYKNPKIALLN 241
Cdd:TIGR02345 160 LSSKLISHNKEFFSKMIVDAVLSLDrDDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAGFEQQPKKFANPKILLLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 242 VELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHQSGAKVILSKLPIGDVATQYFADRDMFCAGRVPEEDLKR 321
Cdd:TIGR02345 240 VELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 322 TMMACGGSIQTSVNALVPDVLGHCQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIK 401
Cdd:TIGR02345 320 VIKACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 402 NDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMWYGVDINN 481
Cdd:TIGR02345 400 NKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINT 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 238814391 482 ENIADNFQAFVWEPAMVRINALTAASEAACLIVSVDETIKNPRS 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: 594.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 13 TDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGD 92
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 93 GTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKQDkveqRKMLEKCAMTALSSKLISQQK 172
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVED----REELLKVATTSLNSKLVSGGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 173 VFFAKMVVDAVMML---DELLQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAGFemqPKKYKNPKIALLNVELELkae 249
Cdd:cd00309 157 DFLGELVVDAVLKVgkeNGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYM---PKRLENAKILLLDCKLEY--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 250 kdnaeirvhtvedyqaivdaewnilydklekihqsgakVILSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGS 329
Cdd:cd00309 231 --------------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGAT 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 330 IQTSVNALVPDVLGHCQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGG 409
Cdd:cd00309 273 IVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 410 GAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMWYGVDINNENIADNFQ 489
Cdd:cd00309 353 GAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKE 432
|
490 500 510
....*....|....*....|....*....|..
gi 238814391 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: 561.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 32 IAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLKQVKPY 111
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 112 VEEGLHPQIIIRAFRTATQLAVNKIKEIavtVKKQDKVEQRKMLEKCAMTALSSKLISQQKVFFAKMVVDAVMML---DE 188
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSI---ISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIpknDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 189 LLQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYagfEMQPKKYKNPKIALLNVELELKAEKDNAEIRVHTVEDYQAIVD 268
Cdd:pfam00118 158 SFDLGNIGVVKILGGSLEDSELVDGVVLDKGPLH---PDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 269 AEWNILYDKLEKIHQSGAKVILSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALVPDVLGHCQVF 348
Cdd:pfam00118 235 AEEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 349 EETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIP 428
Cdd:pfam00118 315 EEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 429 GKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMWYGVDINNENIADNFQAFVWEPAMVRINALTAASE 508
Cdd:pfam00118 395 GKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATE 474
|
490
....*....|...
gi 238814391 509 AACLIVSVDETIK 521
Cdd:pfam00118 475 AASTILRIDDIIK 487
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
4-520 |
4.02e-171 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 494.08 E-value: 4.02e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 4 TPVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIA 83
Cdd:NF041083 1 QPVLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 84 KSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKQDkveqRKMLEKCAMTAL 163
Cdd:NF041083 81 KTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDD----RETLKKIAETSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 164 SSKLISQQKVFFAKMVVDAVMMLDEL------LQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAGFemqPKKYKNPKI 237
Cdd:NF041083 157 TSKGVEEARDYLAEIAVKAVKQVAEKrdgkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGM---PKRVENAKI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 238 ALLNVELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHQSGAKVILSKLPIGDVATQYFADRDMFCAGRVPEE 317
Cdd:NF041083 234 ALLDAPLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 318 DLKRTMMACGGSIQTSVNALVPDVLGHCQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVR 397
Cdd:NF041083 314 DMEKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 398 RAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMWYGV 477
Cdd:NF041083 394 DAVEDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGI 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 238814391 478 DINNENIADNFQAFVWEPAMVRINALTAASEAACLIVSVDETI 520
Cdd:NF041083 474 NVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVI 516
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
6-521 |
5.55e-167 |
|
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: 483.69 E-value: 5.55e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 6 VILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKS 85
Cdd:cd03343 1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 86 QDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKQDkveqRKMLEKCAMTALSS 165
Cdd:cd03343 81 QDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDD----KDTLRKIAKTSLTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 166 KLISQQKVFFAKMVVDAVMMLDEL------LQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAGFemqPKKYKNPKIAL 239
Cdd:cd03343 157 KGAEAAKDKLADLVVDAVLQVAEKrdgkyvVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGM---PKRVENAKIAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 240 LNVELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHQSGAKVILSKLPIGDVATQYFADRDMFCAGRVPEEDL 319
Cdd:cd03343 234 LDAPLEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 320 KRTMMACGGSIQTSVNALVPDVLGHCQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRA 399
Cdd:cd03343 314 EKLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 400 IKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMWYGVDI 479
Cdd:cd03343 394 LEDGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDV 473
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 238814391 480 NNENIADNFQAFVWEPAMVRINALTAASEAACLIVSVDETIK 521
Cdd:cd03343 474 YTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIA 515
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
4-520 |
3.66e-166 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 481.31 E-value: 3.66e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 4 TPVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIA 83
Cdd:NF041082 1 QPILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 84 KSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKQDKveqrKMLEKCAMTAL 163
Cdd:NF041082 81 KTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDK----ETLKKIAATAM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 164 SSKLISQQKVFFAKMVVDAVMMLDE-----LLQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAGfeMqPKKYKNPKIA 238
Cdd:NF041082 157 TGKGAEAAKDKLADLVVDAVKAVAEkdggyNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPG--M-PKRVENAKIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 239 LLNVELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHQSGAKVILSKLPIGDVATQYFADRDMFCAGRVPEED 318
Cdd:NF041082 234 LLDAPLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 319 LKRTMMACGGSIQTSVNALVPDVLGHCQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRR 398
Cdd:NF041082 314 MEKLAKATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 399 AIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMWYGVD 478
Cdd:NF041082 394 VLEDGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLD 473
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 238814391 479 INNENIADNFQAFVWEPAMVRINALTAASEAACLIVSVDETI 520
Cdd:NF041082 474 VYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVI 515
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
5-520 |
6.30e-163 |
|
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather than eukaryotic form of the group II chaperonin (counterpart to the group I chaperonin, GroEL/GroES, in bacterial), a torroidal, ATP-dependent molecular chaperone that assists in the folding or refolding of nascent or denatured proteins. Various homologous subunits, one to five per archaeal genome, may be designated alpha, beta, etc., but phylogenetic analysis does not show distinct alpha subunit and beta subunit lineages traceable to ancient paralogs. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274080 Cd Length: 519 Bit Score: 473.40 E-value: 6.30e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 5 PVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAK 84
Cdd:TIGR02339 1 PVFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 85 SQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVkkqdKVEQRKMLEKCAMTALS 164
Cdd:TIGR02339 81 TQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKI----SPEDRDLLKKIAYTSLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 165 SKLISQQ-KVFFAKMVVDAVMMLDEL-------LQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAGFemqPKKYKNPK 236
Cdd:TIGR02339 157 SKASAEVaKDKLADLVVEAVKQVAELrgdgkyyVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGM---PKRVENAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 237 IALLNVELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHQSGAKVILSKLPIGDVATQYFADRDMFCAGRVPE 316
Cdd:TIGR02339 234 IALLDAPLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 317 EDLKRTMMACGGSIQTSVNALVPDVLGHCQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIV 396
Cdd:TIGR02339 314 SDIEKLARATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 397 RRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMWYG 476
Cdd:TIGR02339 394 ANALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAG 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 238814391 477 VDINNENIADNFQAFVWEPAMVRINALTAASEAACLIVSVDETI 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 |
1.59e-145 |
|
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: 429.01 E-value: 1.59e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 14 DSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDG 93
Cdd:cd03335 2 ERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 94 TTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKE-IAVTVKKQDkveqRKMLEKCAMTALSSKLISQQK 172
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDNLG----KESLINVAKTSMSSKIIGADS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 173 VFFAKMVVDAVM---MLDELLQ----LKMIGIKKVQGGALEESQLVAGVAFKKTFsyAGFEMqPKKYKNPKIALLNVELE 245
Cdd:cd03335 158 DFFANMVVDAILavkTTNEKGKtkypIKAVNILKAHGKSAKESYLVNGYALNCTR--ASQGM-PTRVKNAKIACLDFNLQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 246 LKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHQSGAKVILSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMA 325
Cdd:cd03335 235 KTKMKLGVQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 326 CGGSIQTSVNALV------PDVLGHCQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRA 399
Cdd:cd03335 315 TGATLVSTLANLEgeetfdPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 400 IKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHA--------QG 471
Cdd:cd03335 395 LESNSVVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAaaqvkpdkKH 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 238814391 472 GMWYGVDINNENIADNFQAFVWEPAMVRINALTAASEAACLIVSVDETIK-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 |
1.35e-140 |
|
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: 416.81 E-value: 1.35e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 12 GTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVG 91
Cdd:TIGR02340 4 GGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 92 DGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKE-IAVTVKKQDkveqRKMLEKCAMTALSSKLISQ 170
Cdd:TIGR02340 84 DGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDELG----REALINVAKTSMSSKIIGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 171 QKVFFAKMVVDAVM---MLDELLQ----LKMIGIKKVQGGALEESQLVAGVAFKKTFsyAGFEMqPKKYKNPKIALLNVE 243
Cdd:TIGR02340 160 DSDFFSNIVVDAVLavkTTNENGEtkypIKAINILKAHGKSARESMLVKGYALNCTV--ASQQM-PKRIKNAKIACLDFN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 244 LELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHQSGAKVILSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTM 323
Cdd:TIGR02340 237 LQKAKMALGVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 324 MACGGSIQTSV------NALVPDVLGHCQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVR 397
Cdd:TIGR02340 317 KATGATLVSTLadlegeETFEASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 398 RAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHA-------- 469
Cdd:TIGR02340 397 RTLESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAaaqlkpek 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 238814391 470 QGGMWYGVDINNENIADNFQAFVWEPAMVRINALTAASEAACLIVSVDETIK 521
Cdd:TIGR02340 477 KHLKWYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIK 528
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-524 |
1.28e-132 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 396.32 E-value: 1.28e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 1 MMPTPVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIV-----DGRGKATISNDGATILKLLDVVHPA 75
Cdd:PTZ00212 3 MANVPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 76 AKTLVDIAKSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKqDKVEQRKML 155
Cdd:PTZ00212 83 AKILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGS-DEEKFKEDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 156 EKCAMTALSSKLISQQKVFFAKMVVDAVMMLDELLQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAgfemQPKKYKNP 235
Cdd:PTZ00212 162 LNIARTTLSSKLLTVEKDHFAKLAVDAVLRLKGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVG----QPKRLENC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 236 KIALLNVELEL-KAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHQSGAKVILSKLPIGDVATQYFADRDMFCAGRV 314
Cdd:PTZ00212 238 KILVANTPMDTdKIKIYGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 315 PEEDLKRTMMACGGSIQTSVNALVPDVLGHCQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIM 394
Cdd:PTZ00212 318 DFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALC 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 395 IVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMW 474
Cdd:PTZ00212 398 VLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKT 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 238814391 475 YGVDINNENIADNFQAFVWEPAMVRINALTAASEAACLIVSVDETIKN-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 |
8.81e-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: 385.91 E-value: 8.81e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 9 LKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLI--VDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQ 86
Cdd:cd03336 2 LKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 87 DAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKkQDKVEQRKMLEKCAMTALSSK 166
Cdd:cd03336 82 DDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHS-SDEEAFREDLLNIARTTLSSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 167 LISQQKVFFAKMVVDAVMMLDELLQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAgfemQPKKYKNPKIALLNVELEL 246
Cdd:cd03336 161 ILTQDKEHFAELAVDAVLRLKGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVN----QPKRIENAKILIANTPMDT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 247 -KAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHQSGAKVILSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMA 325
Cdd:cd03336 237 dKIKIFGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 326 CGGSIQTSVNALVPDVLGHCQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSV 405
Cdd:cd03336 317 TGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 406 VAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMWYGVDINNENIA 485
Cdd:cd03336 397 VLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTVG 476
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 238814391 486 DNFQAFVWEPAMVRINALTAASEAACLIVSVDETIK-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 |
7.67e-124 |
|
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: 373.16 E-value: 7.67e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 23 VSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAA 102
Cdd:cd03338 11 LSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 103 EFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKQDkveqRKMLEKCAMTALSSKLISQQKVFFAKMVVDA 182
Cdd:cd03338 91 ALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLND----RESLIKSATTSLNSKVVSQYSSLLAPIAVDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 183 VMML-----DELLQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAGfeMQPKKYKNPKIALlnVELELKAEKDNAEIRV 257
Cdd:cd03338 167 VLKVidpatATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKA--GGPTRIEKAKIGL--IQFCLSPPKTDMDNNI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 258 hTVEDYQA---IVDAEWNILYDKLEKIHQSGAKVIL---SKL--PIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGS 329
Cdd:cd03338 243 -VVNDYAQmdrILREERKYILNMCKKIKKSGCNVLLiqkSILrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 330 IQTSVNALVPDVLGHCQVFEETQIGGERYNFFTGCPKA-KTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAG 408
Cdd:cd03338 322 PVASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 409 GGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMWYGVDINNENIADNF 488
Cdd:cd03338 402 GGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITNIL 481
|
490 500 510
....*....|....*....|....*....|..
gi 238814391 489 QAFVWEPAMVRINALTAASEAACLIVSVDETI 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 |
3.49e-122 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239453 [Multi-domain] Cd Length: 480 Bit Score: 367.78 E-value: 3.49e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 5 PVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAK 84
Cdd:cd03337 1 PVLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 85 SQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVkkqdKVEQRKMLEKCAMTALS 164
Cdd:cd03337 81 TQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPV----DVNDRAQMLKIIKSCIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 165 SKLISQQKVFFAKMVVDAVMM--LDELLQLKMIGIK------KVQGGALEESQLVAGVAFKKTFSYAGfeMQpKKYKNPK 236
Cdd:cd03337 157 TKFVSRWSDLMCNLALDAVKTvaVEENGRKKEIDIKryakveKIPGGEIEDSRVLDGVMLNKDVTHPK--MR-RRIENPR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 237 IALLNVELElkaekdnaeirvhtvedYQaivdaewnilydklekihqsgakVILSKlPIGDVATQYFADRDMFCAGRVPE 316
Cdd:cd03337 234 IVLLDCPLE-----------------YL-----------------------VITEK-GVSDLAQHYLVKAGITALRRVRK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 317 EDLKRTMMACGGSIQTSVNALVPDVLGH-CQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMI 395
Cdd:cd03337 273 TDNNRIARACGATIVNRPEELTESDVGTgAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 396 VRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQ-GGMW 474
Cdd:cd03337 353 ARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQgENST 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 238814391 475 YGVDINNENIADNFQAFVWEPAMVRINALTAASEAACLIVSVDETI 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 |
1.12e-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: 354.86 E-value: 1.12e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 24 SNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAE 103
Cdd:TIGR02342 13 SNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 104 FLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKQDkveqRKMLEKCAMTALSSKLISQQKVFFAKMVVDAV 183
Cdd:TIGR02342 93 LLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSD----REQLLKSATTSLSSKVVSQYSSLLAPLAVDAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 184 MML-----DELLQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAgfEMQPKKYKNPKIALlnVELELKAEKDNAEIRVh 258
Cdd:TIGR02342 169 LKVidpenAKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKS--AGGPTRIEKAKIGL--IQFQISPPKTDMENQI- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 259 TVEDYQA---IVDAEWNILYDKLEKIHQSGAKVILSKLPI-----GDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSI 330
Cdd:TIGR02342 244 IVNDYAQmdrVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 331 QTSVNALVPDVLGHCQVFEETQIGGERYNFFTGCPKA-KTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGG 409
Cdd:TIGR02342 324 IASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 410 GAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMWYGVDINNENIADNFQ 489
Cdd:TIGR02342 404 GAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITNMLE 483
|
490 500
....*....|....*....|....*....
gi 238814391 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 |
3.24e-114 |
|
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: 348.65 E-value: 3.24e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 5 PVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAK 84
Cdd:TIGR02344 1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 85 SQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKQDKVEQRKMLEKCamtaLS 164
Cdd:TIGR02344 81 TQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSC----IG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 165 SKLISQQKVFFAKMVVDAV--MMLDELLQlKMIGIK------KVQGGALEESQLVAGVAFKKTFSYAgfEMQpKKYKNPK 236
Cdd:TIGR02344 157 TKFVSRWSDLMCDLALDAVrtVQRDENGR-KEIDIKryakveKIPGGDIEDSCVLKGVMINKDVTHP--KMR-RYIENPR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 237 IALLNVELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHQSGAKVILSKLPIGDVATQYFADRDMFCAGRVPE 316
Cdd:TIGR02344 233 IVLLDCPLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 317 EDLKRTMMACGGSIQTSVNALV-PDVLGHCQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMI 395
Cdd:TIGR02344 313 TDNNRIARACGATIVNRPEELReSDVGTGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 396 VRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGM-W 474
Cdd:TIGR02344 393 ARNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNcT 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 238814391 475 YGVDINNENIADNFQAFVWEPAMVRINALTAASEAACLIVSVDETI 520
Cdd:TIGR02344 473 WGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
5-521 |
1.38e-110 |
|
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: 339.27 E-value: 1.38e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 5 PVILLKEGTDSS--QGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDI 82
Cdd:cd03339 6 PFIIVREQEKKKrlKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 83 AKSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKQDkvEQRKMLEKCAMTA 162
Cdd:cd03339 86 SKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSP--DNKEPLIQTAMTS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 163 LSSKLISQQKVFFAKMVVDAVMMLDEL----LQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAgfEMqPKKYKNPKIA 238
Cdd:cd03339 164 LGSKIVSRCHRQFAEIAVDAVLSVADLerkdVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHP--QM-PKEVKDAKIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 239 LLNVELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHQSGAKVILSKLPIGDVATQYFADRDMFCAGRVPEED 318
Cdd:cd03339 241 ILTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 319 LKRTMMACGGSIQTSVNALVPDVLGHCQVFEETQIGG--ERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIV 396
Cdd:cd03339 321 IELIAIATGGRIVPRFEDLSPEKLGKAGLVREISFGTtkDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 397 RRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARH-AQGGMWY 475
Cdd:cd03339 401 RNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPHL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 238814391 476 GVDINNENIADNFQAFVWEPAMVRINALTAASEAACLIVSVDETIK 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 |
2.44e-106 |
|
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: 328.36 E-value: 2.44e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 8 LLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATI--SNDGATILKLLDVVHPAAKTLVDIAKS 85
Cdd:TIGR02341 2 IFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSSSDASImvTNDGATILKSIGVDNPAAKVLVDMSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 86 QDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTvKKQDKVEQRKMLEKCAMTALSS 165
Cdd:TIGR02341 82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVD-NGSDEVKFRQDLMNIARTTLSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 166 KLISQQKVFFAKMVVDAVMMLDELLQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYagfeMQPKKYKNPKIALLNVELE 245
Cdd:TIGR02341 161 KILSQHKDHFAQLAVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGV----NQPKRIENAKILIANTGMD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 246 L-KAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHQSGAKVILSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMM 324
Cdd:TIGR02341 237 TdKVKIFGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 325 ACGGSIQTSVNALVPDVLGHCQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDS 404
Cdd:TIGR02341 317 VTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 405 VVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMWYGVDINNENI 484
Cdd:TIGR02341 397 TVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGTI 476
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 238814391 485 ADNFQAFVWEPAMVRINALTAASEAACLIVSVDETIK-NPRS 525
Cdd:TIGR02341 477 ADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKaAPRK 518
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
20-520 |
1.52e-100 |
|
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: 311.85 E-value: 1.52e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 20 PQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTL 99
Cdd:cd03341 8 EAVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 100 LAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAV-TVKKQDKVEQrkmLEKCAMTALSSKLISQQKvFFAKM 178
Cdd:cd03341 88 LAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVyKIEDLRNKEE---VSKALKTAIASKQYGNED-FLSPL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 179 VVDAVMML----DELLQLKMIGIKKVQGGALEESQLVAGVAFKKtfsyaGFEMQPKKYKNPKIALLNVELELkaekdnae 254
Cdd:cd03341 164 VAEACISVlpenIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKR-----EPEGSVKRVKKAKVAVFSCPFDI-------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 255 irvhtvedyqaivdaewnilydklekihqsGAKVILSKLPIGDVAtQYFADRDMFCAGRVPEE-DLKRTMMACGGSIQTS 333
Cdd:cd03341 231 ------------------------------GVNVIVAGGSVGDLA-LHYCNKYGIMVIKINSKfELRRLCRTVGATPLPR 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 334 VNALVPDVLGHCQVFEETQIGGERYNFFTGCPKA-KTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGGGAI 412
Cdd:cd03341 280 LGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDsKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGAT 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 413 EMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMWYGVDINNENIA--DNFQA 490
Cdd:cd03341 360 EIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDEGtkDAKEA 439
|
490 500 510
....*....|....*....|....*....|
gi 238814391 491 FVWEPAMVRINALTAASEAACLIVSVDETI 520
Cdd:cd03341 440 GIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
5-522 |
3.13e-98 |
|
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: 307.88 E-value: 3.13e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 5 PVILLKEGTDSSQ--GIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDI 82
Cdd:TIGR02343 10 PFIIIKDQDNKKRlkGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 83 AKSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVkkQDKVEQRKMLEKCAMTA 162
Cdd:TIGR02343 90 SKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEI--SADNNNREPLIQAAKTS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 163 LSSKLISQQKVFFAKMVVDAVMMLDEL----LQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAgfEMqPKKYKNPKIA 238
Cdd:TIGR02343 168 LGSKIVSKCHRRFAEIAVDAVLNVADMerrdVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHP--QM-PKEVEDAKIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 239 LLNVELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHQSGAKVILSKLPIGDVATQYFADRDMFCAGRVPEED 318
Cdd:TIGR02343 245 ILTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 319 LKRTMMACGGSIQTSVNALVPDVLGHCQVFEETQIG--GERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIV 396
Cdd:TIGR02343 325 LELIAIATGGRIVPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 397 RRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARH-AQGGMWY 475
Cdd:TIGR02343 405 RNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQlKEKNPNL 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 238814391 476 GVDINNENIADNFQAFVWEPAMVRINALTAASEAACLIVSVDETIKN 522
Cdd:TIGR02343 485 GVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVISP 531
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
8-520 |
5.94e-98 |
|
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: 307.03 E-value: 5.94e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 8 LLKEGTDSSQGIP-QLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQ 86
Cdd:TIGR02346 5 LLKEGYRHFSGLEeAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 87 DAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTvkKQDKVEQRKMLEKCAMTALSSK 166
Cdd:TIGR02346 85 ENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVW--EVKDLRDKDELIKALKASISSK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 167 LISQQkVFFAKMVVDAVMML----DELLQLKMIGIKKVQGGALEESQLVAGVAFKKTFsyagfEMQPKKYKNPKIALLNV 242
Cdd:TIGR02346 163 QYGNE-DFLAQLVAQACSTVlpknPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNREA-----EGSVKSVKNAKVAVFSC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 243 ELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHQSGAKVILSKLPIGDVAtQYFADRDMFCAGRVPEE-DLKR 321
Cdd:TIGR02346 237 PLDTATTETKGTVLIHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMA-LHYLNKYNIMVLKIPSKfELRR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 322 TMMACGGSIQTSVNALVPDVLGHCQVFEETQIGGERYNFFTGCPK-AKTCTIILRGGAEQFMEETERSLHDAIMIVRRAI 400
Cdd:TIGR02346 316 LCKTVGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGdSKISTIILRGSTDNLLDDIERAIDDGVNTVKALV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 401 KNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMWYGVDIN 480
Cdd:TIGR02346 396 KDGRLLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIE 475
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 238814391 481 NENIA--DNFQAFVWEPAMVRINALTAASEAACLIVSVDETI 520
Cdd:TIGR02346 476 AESDGvkDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQII 517
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
24-520 |
7.88e-98 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 305.46 E-value: 7.88e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 24 SNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHP----AAKTLVDIAKSQDAEVGDGTTSVTL 99
Cdd:COG0459 14 ANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTTTATV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 100 LAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVtvkkqdKVEQRKMLEKCAMTALSSKlisqqkVFFAKMV 179
Cdd:COG0459 94 LAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAK------PVDDKEELAQVATISANGD------EEIGELI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 180 VDAVMMLDellqlKMIGIKKVQGGALE-ESQLVAGVAFKKTFSYAGF----EMQPKKYKNPKIALLNVELELKAEkdnae 254
Cdd:COG0459 162 AEAMEKVG-----KDGVITVEEGKGLEtELEVVEGMQFDKGYLSPYFvtdpEKMPAELENAYILLTDKKISSIQD----- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 255 irvhtvedyqaivdaewniLYDKLEKIHQSGAK-VILSKlPIGDVATQYFADRDMFCAGRVP-----------EEDLKRT 322
Cdd:COG0459 232 -------------------LLPLLEKVAQSGKPlLIIAE-DIDGEALATLVVNGIRGVLRVVavkapgfgdrrKAMLEDI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 323 MMACGGSIQT-----SVNALVPDVLGHCqvfEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVR 397
Cdd:COG0459 292 AILTGGRVISedlglKLEDVTLDDLGRA---KRVEVDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALHATR 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 398 RAIKnDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRarhAQGGMWYGV 477
Cdd:COG0459 369 AAVE-EGIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVR---AAKDKGFGF 444
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 238814391 478 DINNENIADNFQAFVWEPAMVRINALTAASEAACLIVSVDETI 520
Cdd:COG0459 445 DAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVI 487
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
8-526 |
4.27e-83 |
|
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: 268.14 E-value: 4.27e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 8 LLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQD 87
Cdd:TIGR02347 4 LLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 88 AEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEiaVTVKKQDKVEqRKMLEKCAMTALSSKL 167
Cdd:TIGR02347 84 DITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDK--FKVKKEDEVD-REFLLNVARTSLRTKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 168 ISQQKVFFAKMVVDAVMML---DELLQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAGFemqPKKYKNPKIALLNVEL 244
Cdd:TIGR02347 161 PADLADQLTEIVVDAVLAIkkdGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDM---PRRVKNAYILTCNVSL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 245 ELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHQSGAKVILSKLPIG-DVATQ---------YFADRDMFCAGRV 314
Cdd:TIGR02347 238 EYEKTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCGKSPDKGfVVINQkgidppsldLLAKEGIMALRRA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 315 PEEDLKRTMMACGGSIQTSVNALVPDVLGHCQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIM 394
Cdd:TIGR02347 318 KRRNMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 395 IVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMW 474
Cdd:TIGR02347 398 AVKNAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEV 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 238814391 475 YGVDINNENIADNFQAFVWEPAMVRINALTAASEAACLIVSVDETIKNPRST 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 |
3.25e-82 |
|
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: 264.51 E-value: 3.25e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 25 NISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAEF 104
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 105 LKQVKPYVEEGLHPQIIIRAFrtatQLAVNKIKEIAVTVKKQDKVEQ-RKMLEKCAMTALSSKLISQQKVFFAKMVVDAV 183
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGF----ELAKNKALKFLESFKVPVEIDTdRELLLSVARTSLRTKLHADLADQLTEIVVDAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 184 MML---DELLQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAgfEMqPKKYKNPKIALLNVELElkaekdnaeirvhtv 260
Cdd:cd03342 173 LAIykpDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHP--DM-PKRVENAYILTCNVSLE--------------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 261 edyqaivdaewnilYDKLEKIHQSGAKVILSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALVPD 340
Cdd:cd03342 235 --------------YEKTEVNSGFFYSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 341 VLGHCQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYL 420
Cdd:cd03342 301 CLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 421 RDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMWYGVDINNENIADNFQAFVWEPAMVRI 500
Cdd:cd03342 381 KEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKR 460
|
490 500
....*....|....*....|.
gi 238814391 501 NALTAASEAACLIVSVDETIK 521
Cdd:cd03342 461 QILHSATVIASQLLLVDEIIR 481
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
152-402 |
6.45e-71 |
|
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: 225.81 E-value: 6.45e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 152 RKMLEKCAMTALSSKlISQQKVFFAKMVVDAVMML---DELLQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAGFemq 228
Cdd:cd03333 1 RELLLQVATTSLNSK-LSSWDDFLGKLVVDAVLKVgpdNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYM--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 229 PKKYKNPKIALLNVELELkaekdnaeirvhtvedyqaivdaewnilydklekihqsgakVILSKLPIGDVATQYFADRDM 308
Cdd:cd03333 77 PKRLENAKILLLDCPLEY-----------------------------------------VVIAEKGIDDLALHYLAKAGI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 309 FCAGRVPEEDLKRTMMACGGSIQTSVNALVPDVLGHCQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERS 388
Cdd:cd03333 116 MAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRS 195
|
250
....*....|....
gi 238814391 389 LHDAIMIVRRAIKN 402
Cdd:cd03333 196 LHDALCAVRAAVEE 209
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
26-534 |
5.64e-20 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 93.44 E-value: 5.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 26 ISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILK-------LLDVvhpAAKTLVDIAKSQDAEVGDGTTSVT 98
Cdd:PTZ00114 28 LKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKaiefsdrFENV---GAQLIRQVASKTNDKAGDGTTTAT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 99 LLAAEFLKQVKPYVEEGLHPQIIIRAFrtatQLAVNKIKEiavTVKKQDK-VEQRKMLEKCAMTALS-----SKLISQQk 172
Cdd:PTZ00114 105 ILARAIFREGCKAVAAGLNPMDLKRGI----DLAVKVVLE---SLKEQSRpVKTKEDILNVATISANgdveiGSLIADA- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 173 vfFAKMVVDAVMMLDEllqlkmigikkvqGGALE-ESQLVAGVAFkktfsyagfemqPKKYKNPkiALLNVELELKAEKD 251
Cdd:PTZ00114 177 --MDKVGKDGTITVED-------------GKTLEdELEVVEGMSF------------DRGYISP--YFVTNEKTQKVELE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 252 NAEIRVHT--VEDYQAIV----------------------DAEWNILYDKLekihQSGAKVILSKLP-IGDVATQYFADR 306
Cdd:PTZ00114 228 NPLILVTDkkISSIQSILpilehavknkrplliiaedvegEALQTLIINKL----RGGLKVCAVKAPgFGDNRKDILQDI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 307 DMFCAGRVPEEDlkrtmmacggSIQTSVNALVPDVLGHCQVFE----ETQIGG--------------------------- 355
Cdd:PTZ00114 304 AVLTGATVVSED----------NVGLKLDDFDPSMLGSAKKVTvtkdETVILTgggdkaeikervellrsqierttseyd 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 356 -----ERYNFFTGcpkaKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNdSVVAGGGAIEMELSKYLrDY---SRTI 427
Cdd:PTZ00114 374 keklkERLAKLSG----GVAVIKVGGASEVEVNEKKDRIEDALNATRAAVEE-GIVPGGGVALLRASKLL-DKleeDNEL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 428 PGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGgmwYGVDINNENIADNFQAFVWEPAMVRINALTAAS 507
Cdd:PTZ00114 448 TPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKKDPS---FGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAA 524
|
570 580 590
....*....|....*....|....*....|.
gi 238814391 508 EAACLI----VSVDETIKNPRSTVDPPAPSA 534
Cdd:PTZ00114 525 SVASLMltteAAIVDLPKEKKKNKNSAAPPM 555
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
31-539 |
9.34e-20 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 92.60 E-value: 9.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 31 VIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVV----HPAAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLK 106
Cdd:PRK12852 22 ILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 107 QVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKQDKVEQRKMLEKCAMTALsSKLISQQkvfFAKMVVDAVMML 186
Cdd:PRK12852 102 EGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAI-GKMIAQA---MQKVGNEGVITV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 187 DELLQLKMigikkvqggaleESQLVAGVAFKKTFSYAGFEMQPKKyknpkiallnveleLKAEKDNAEIRVH--TVEDYQ 264
Cdd:PRK12852 178 EENKSLET------------EVDIVEGMKFDRGYLSPYFVTNAEK--------------MTVELDDAYILLHekKLSGLQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 265 AIV------------------DAEWNILYDKLEKIHQSGAKVILSKLP-IGDVATQYFADRDMFCAGRVPEEDL------ 319
Cdd:PRK12852 232 AMLpvleavvqsgkplliiaeDVEGEALATLVVNRLRGGLKVAAVKAPgFGDRRKAMLEDIAILTGGQLISEDLgiklen 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 320 ---------KR-------TMMACGGSIQTSVNALVPDVLGHcqvFEETQIGGERYNFFTGCPK-AKTCTIILRGGA-EQF 381
Cdd:PRK12852 312 vtlkmlgraKKvvidkenTTIVNGAGKKADIEARVGQIKAQ---IEETTSDYDREKLQERLAKlAGGVAVIRVGGAtEVE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 382 MEETERSLHDAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYSRTIPgKQQLLIGAYAKALEIIPRQLCDNAGFDATNIL 461
Cdd:PRK12852 389 VKEKKDRVEDALNATRAAVQ-EGIVPGGGVALLRAKKAVGRINNDNA-DVQAGINIVLKALEAPIRQIAENAGVEGSIVV 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238814391 462 NKLRARHAQGgmwYGVDINNENIADNFQAFVWEPAMVRINALTAASEAACLIVSVDETIKN-PRSTVDPPAPSAGRGRG 539
Cdd:PRK12852 467 GKILENKSET---FGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAElPKKDAAPAMPAGGGMGG 542
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
30-519 |
1.73e-18 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 88.62 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 30 QVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKT---LVDIAKSQDAEV-GDGTTSVTLLAAEFL 105
Cdd:CHL00093 20 DILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTgvaLIRQAASKTNDVaGDGTTTATVLAYAIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 106 KQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKQDKVEQrkmlekcaMTALSS-------KLISQQkvfFAKM 178
Cdd:CHL00093 100 KQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQ--------VASISAgndeevgSMIADA---IEKV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 179 VVDAVMMLDEllqlkmigikkvQGGALEESQLVAGVAFKKTFSYAGFEMQPKK----YKNPKIALLNVELELkAEKDNAE 254
Cdd:CHL00093 169 GREGVISLEE------------GKSTVTELEITEGMRFEKGFISPYFVTDTERmevvQENPYILLTDKKITL-VQQDLLP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 255 IRVHTVEDYQAIVdaewnILYDKLEKihQSGAKVILSKL-----------P-IGDVATQYFADRDMFCAGRVPEED---- 318
Cdd:CHL00093 236 ILEQVTKTKRPLL-----IIAEDVEK--EALATLVLNKLrgivnvvavraPgFGDRRKAMLEDIAILTGGQVITEDagls 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 319 LKR-TMMACGGSIQTSVN----ALVPD-----VLGHC----QVFEETQIGGERYNFFTGCPKAKTCTIILRGGA--EQFM 382
Cdd:CHL00093 309 LETiQLDLLGQARRIIVTkdstTIIADgneeqVKARCeqlrKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAatETEM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 383 EETERSLHDAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYSRTiPGKQQLLIGAY--AKALEIIPRQLCDNAGFDATNI 460
Cdd:CHL00093 389 KDKKLRLEDAINATKAAVE-EGIVPGGGATLVHLSENLKTWAKN-NLKEDELIGALivARAILAPLKRIAENAGKNGSVI 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238814391 461 LNKLRARHAQggmwYGVDINNENIADNFQAFVWEPAMVRINAL-TAASEAA------CLIVSVDET 519
Cdd:CHL00093 467 IEKVQEQDFE----IGYNAANNKFVNMYEAGIIDPAKVTRSALqNAASIASmiltteCIIVDKKES 528
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
29-513 |
5.51e-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: 83.66 E-value: 5.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 29 CQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILK---LLDVVHPA-AKTLVDIAKSQDAEVGDGTTSVTLLAAEF 104
Cdd:cd03344 17 VNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKeieLEDPFENMgAQLVKEVASKTNDVAGDGTTTATVLARAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 105 LKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKQDKVEQrkmlekCAMTALSS-----KLISQQkvfFAKMV 179
Cdd:cd03344 97 IKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQ------VATISANGdeeigELIAEA---MEKVG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 180 VDAVMMLDEllqlkmigikkvqGGALE-ESQLVAGVAFKKTFSYAGFEMQPKKYKnpkiallnVELElkaekdNAEI--- 255
Cdd:cd03344 168 KDGVITVEE-------------GKTLEtELEVVEGMQFDRGYLSPYFVTDPEKME--------VELE------NPYIllt 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 256 --RVHTVEDYQAIvdaewnilydkLEKIHQSG---------------AKVILSKL-----------P---------IGDV 298
Cdd:cd03344 221 dkKISSIQELLPI-----------LELVAKAGrplliiaedvegealATLVVNKLrgglkvcavkaPgfgdrrkamLEDI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 299 AT----QYFADRDMFCAGRVPEEDLKR-----------TMMACGGS---IQTSVNALvpdvlghCQVFEETQIGGERYNF 360
Cdd:cd03344 290 AIltggTVISEELGLKLEDVTLEDLGRakkvvvtkddtTIIGGAGDkaaIKARIAQI-------RKQIEETTSDYDKEKL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 361 ------FTGcpkaKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKnDSVVAGGGAIEMELSKYLrDYSRTIPGKQQLL 434
Cdd:cd03344 363 qerlakLSG----GVAVIKVGGATEVELKEKKDRVEDALNATRAAVE-EGIVPGGGVALLRASPAL-DKLKALNGDEKLG 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238814391 435 IGAYAKALEIIPRQLCDNAGFDATNILNKLRArHAQGgmwYGVDINNENIADNFQAFVWEPAMVRINALTAASEAACLI 513
Cdd:cd03344 437 IEIVRRALEAPLRQIAENAGVDGSVVVEKVLE-SPDG---FGYDAATGEYVDMIEAGIIDPTKVVRSALQNAASVASLL 511
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
30-543 |
5.59e-17 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 83.93 E-value: 5.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 30 QVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDV----VHPAAKTLVDIA-KSQDAeVGDGTTSVTLLAAEF 104
Cdd:PRK14104 21 DILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVAsKSADA-AGDGTTTATVLAQAI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 105 LKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKQDKVEQRKMLEKCAMTALSSKLISQQKvffaKMVVDAVM 184
Cdd:PRK14104 100 VREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFLADAMK----KVGNEGVI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 185 MLDELLQLKMigikkvqggaleESQLVAGVAFKKTFSYAGFEMQPKKYK-----------NPKIALLNVELE-LKAEKDN 252
Cdd:PRK14104 176 TVEEAKSLET------------ELDVVEGMQFDRGYISPYFVTNADKMRvemddayilinEKKLSSLNELLPlLEAVVQT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 253 AEIRVHTVEDYQAivDAEWNILYDKLekihQSGAKVILSKLP-IGDVATQYFADRDMFCAGRVPEEDL------------ 319
Cdd:PRK14104 244 GKPLVIVAEDVEG--EALATLVVNRL----RGGLKVAAVKAPgFGDRRKAMLQDIAILTGGQAISEDLgiklenvtlqml 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 320 ----------KRTMMACGGSIQTSVNALVPDVLGHcqvFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERS- 388
Cdd:PRK14104 318 grakkvmidkENTTIVNGAGKKADIEARVAQIKAQ---IEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKd 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 389 -LHDAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYsRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAR 467
Cdd:PRK14104 395 rVDDAMHATRAAVE-EGIVPGGGVALLRASEQLKGI-KTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEK 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238814391 468 HAQGgmwYGVDINNENIADNFQAFVWEPA-MVRINALTAASEAACLIVSVDETIKNPRSTVDPPAPSAGRGRGQARF 543
Cdd:PRK14104 473 EQYS---YGFDSQTGEYGNLVSKGIIDPTkVVRTAIQNAASVAALLITTEAMVAELPKKGGAGPAMPPGGGMGGMDF 546
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
32-537 |
1.11e-14 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 76.68 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 32 IAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHP----AAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLKQ 107
Cdd:PRK12850 23 LANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 108 VKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKQDKVEQrkmleKCAMTALSSKLISQqkvffakMVVDAVmmlD 187
Cdd:PRK12850 103 GAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQ-----VATISANGDESIGE-------MIAEAM---D 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 188 ELLQLKMIGIKKVQGGALeESQLVAGVAFKKTFSYAGFEMQPKKyknpkiallnveleLKAEKDNAEIRVHT--VEDYQA 265
Cdd:PRK12850 168 KVGKEGVITVEEAKTLGT-ELDVVEGMQFDRGYLSPYFVTNPEK--------------MRAELEDPYILLHEkkISNLQD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 266 IVDAewnilydkLEKIHQSGAK-VILSK------------------LPIGDVATQYFADRD--------MFCAGRVPEED 318
Cdd:PRK12850 233 LLPI--------LEAVVQSGRPlLIIAEdvegealatlvvnklrggLKSVAVKAPGFGDRRkamlediaVLTGGQVISED 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 319 L---------------KR-------TMMACGGSIQTSVNALVPDVlgHCQVfEETQIGGERYNFFTGCPK-AKTCTIILR 375
Cdd:PRK12850 305 LgiklenvtldmlgraKRvlitkenTTIIDGAGDKKNIEARVKQI--RAQI-EETTSDYDREKLQERLAKlAGGVAVIRV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 376 GGA-EQFMEETERSLHDAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYsRTIPGKQQLLIGAYAKALEIIPRQLCDNAG 454
Cdd:PRK12850 382 GGAtEVEVKEKKDRVDDALHATRAAVE-EGIVPGGGVALLRARSALRGL-KGANADETAGIDIVRRALEEPLRQIATNAG 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 455 FDATNILNKLRARhaQGGmwYGVDINNENIADNFQAFVWEPAMVRINAL-TAASEAACLIVS----VDETIKNPRSTVDP 529
Cdd:PRK12850 460 FEGSVVVGKVAEL--PGN--FGFNAQTGEYGDMVEAGIIDPAKVTRTALqDAASIAALLITTeamvAEAPKKAAAAAAGP 535
|
....*...
gi 238814391 530 PAPSAGRG 537
Cdd:PRK12850 536 GPGMGGMG 543
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
197-377 |
9.46e-14 |
|
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: 71.48 E-value: 9.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 197 IKKVQGGALEESQLVAGVAFKKTFSYAGfeMqPKKYKNPKIALLNVELElkaekdnaeirVHTVE----DYQAIVDAEWN 272
Cdd:cd03334 52 IKKIPGGSPSDSEVVDGVVFTKNVAHKR--M-PSKIKNPRILLLQGPLE-----------YQRVEnkllSLDPVILQEKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 273 ILYDKLEKIHQSGAKVILSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALV-PDVLGHCQVFEET 351
Cdd:cd03334 118 YLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDLLtSPKLGTCESFRVR 197
|
170 180 190
....*....|....*....|....*....|.
gi 238814391 352 QIGGER-----YNFFTGCPKAKTCTIILRGG 377
Cdd:cd03334 198 TYVEEHgrsktLMFFEGCPKELGCTILLRGG 228
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
31-539 |
7.38e-13 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 70.93 E-value: 7.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 31 VIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHP----AAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLK 106
Cdd:PRK12851 22 ILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 107 QVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKQDKVEQRKMLEKCAMTALsSKLISQQkvfFAKMVVDAVMML 186
Cdd:PRK12851 102 EGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEI-GRLVAEA---MEKVGNEGVITV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 187 DEllqlkmigiKKVQGGALEesqLVAGVAFKKTFSYAGFEMQPKK----YKNPKIALlnVELELKAEKDNAEIRVHTVED 262
Cdd:PRK12851 178 EE---------SKTAETELE---VVEGMQFDRGYLSPYFVTDADKmeaeLEDPYILI--HEKKISNLQDLLPVLEAVVQS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 263 YQAIV----DAEWNILYDKLEKIHQSGAKVILSKLP-IGDVATQYFADRDMFCAGRVPEEDLKR---------------- 321
Cdd:PRK12851 244 GKPLLiiaeDVEGEALATLVVNKLRGGLKVAAVKAPgFGDRRKAMLEDIAILTGGTVISEDLGIklenvtleqlgrakkv 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 322 ------TMMACGGSIQTSVNALVPDVLGHcqvFEETQIGGERYNFFTGCPKAKTCTIILRGGA--EQFMEETERSLHDAI 393
Cdd:PRK12851 324 vvekenTTIIDGAGSKTEIEGRVAQIRAQ---IEETTSDYDREKLQERLAKLAGGVAVIRVGAstEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 394 MIVRRAIKnDSVVAGGGAIEMELSKYLrDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARhaQGGm 473
Cdd:PRK12851 401 HATRAAVE-EGIVPGGGVALLRAVKAL-DKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREK--PGG- 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238814391 474 wYGVDINNENIADNFQAFVWEPAMVRINALTAASEAACLIVSVDETIKNPRSTVDPPAPSAGRGRG 539
Cdd:PRK12851 476 -YGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAPPAPPGGGMD 540
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
33-538 |
9.15e-13 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 70.61 E-value: 9.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 33 AEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHP----AAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLKQV 108
Cdd:PRK12849 23 ADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQALVQEG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 109 KPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKQDKVEQrkmlekcaMTALSS-------KLISQQkvfFAKMVVD 181
Cdd:PRK12849 103 LKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQ--------VATISAngdeeigELIAEA---MEKVGKD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 182 AVMMLDEllqlkmigikkvqGGALE-ESQLVAGVAFKKTFSYAGFEMQPKKyknpkiallnveleLKAEKDNAEIRVH-- 258
Cdd:PRK12849 172 GVITVEE-------------SKTLEtELEVTEGMQFDRGYLSPYFVTDPER--------------MEAVLEDPLILLTdk 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 259 ---TVEDYQAIvdaewnilydkLEKIHQSG---------------AKVILSK----LPIGDVATQYFADR------DM-- 308
Cdd:PRK12849 225 kisSLQDLLPL-----------LEKVAQSGkplliiaedvegealATLVVNKlrggLKVAAVKAPGFGDRrkamleDIai 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 309 FCAGRVPEEDL---------------KR-------TMMACGGSIQTSVNALVPDVlghCQVFEET---------QiggER 357
Cdd:PRK12849 294 LTGGTVISEDLglkleevtlddlgraKRvtitkdnTTIVDGAGDKEAIEARVAQI---RRQIEETtsdydreklQ---ER 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 358 YNFFTGcpkakTCTIILRGGA-EQFMEETERSLHDAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYsRTIPGKQQLLIG 436
Cdd:PRK12849 368 LAKLAG-----GVAVIKVGAAtEVELKERKDRVEDALNATRAAVE-EGIVPGGGVALLRAAKALDEL-AGLNGDQAAGVE 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 437 AYAKALEIIPRQLCDNAGFDATNILNKLRaRHAQGgmwYGVDINNENIADNFQAFVWEPAMVRINALTAASEAACLIVSV 516
Cdd:PRK12849 441 IVRRALEAPLRQIAENAGLDGSVVVAKVL-ELEDG---FGFNAATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTT 516
|
570 580
....*....|....*....|..
gi 238814391 517 DETIKNPRSTVDPPAPSAGRGR 538
Cdd:PRK12849 517 EALVADKPEEEDPPGGMGGMGG 538
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
31-151 |
4.24e-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: 68.47 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 31 VIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHP----AAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLK 106
Cdd:TIGR02348 20 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVASKTNDVAGDGTTTATVLAQAIVK 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 238814391 107 QVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKQDKVEQ 151
Cdd:TIGR02348 100 EGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQ 144
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
31-151 |
8.47e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 64.37 E-value: 8.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 31 VIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHP----AAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLK 106
Cdd:PRK00013 21 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLAQAIVR 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 238814391 107 QVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKQDKVEQ 151
Cdd:PRK00013 101 EGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQ 145
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
32-525 |
1.87e-07 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 53.77 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 32 IAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILK---LLDVVHPAAKTLVDIAKSQDAEV-GDGTTSVTLLAAEFLKQ 107
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKeveLEDPVENIGAKLVRQAAAKTNDLaGDGTTTSVVLAQGLIAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 108 VKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAvtvkkqDKVEQRKMLEKCAMTALSSKLISQqkvffakmvvdavMMLD 187
Cdd:PLN03167 158 GVKVVAAGANPVQITRGIEKTAKALVKELKKMS------KEVEDSELADVAAVSAGNNYEVGN-------------MIAE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 188 ELLQLKMIGIKKVQGGALEESQL--VAGVAFKKTFSYAGFEMQPKK----YKNPKIALLNVELElkaekdNAEIRVHTVE 261
Cdd:PLN03167 219 AMSKVGRKGVVTLEEGKSAENNLyvVEGMQFDRGYISPYFVTDSEKmsveYDNCKLLLVDKKIT------NARDLIGILE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 262 D-----YQAIVDAEwNILYDKLEKI----HQSGAKVILSKLP-IGDVATQYFADRDMFCAGRVPEEDLKRTMMACG---- 327
Cdd:PLN03167 293 DairggYPLLIIAE-DIEQEALATLvvnkLRGSLKIAALKAPgFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGkevl 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 328 ------------------GSIQTSVNALVPDVLGHCQVFEETQiggERYNFFTGCPKAKTCTIILRGGAEQFMEETERSL 389
Cdd:PLN03167 372 gtaakvvltkdtttivgdGSTQEAVNKRVAQIKNLIEAAEQDY---EKEKLNERIAKLSGGVAVIQVGAQTETELKEKKL 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 390 --HDAIMIVRRAIKnDSVVAGGGAIEMELSKYLRDYSRTIPGKQQlLIGAyakalEIIPRQLC-------DNAGFDATNI 460
Cdd:PLN03167 449 rvEDALNATKAAVE-EGIVVGGGCTLLRLASKVDAIKDTLENDEQ-KVGA-----DIVKRALSyplkliaKNAGVNGSVV 521
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238814391 461 LNKLRarhAQGGMWYGVDINNENIADNFQAFVWEPA-MVRINALTAASEAACLIVS--VDETIKNPRS 525
Cdd:PLN03167 522 SEKVL---SNDNPKFGYNAATGKYEDLMAAGIIDPTkVVRCCLEHAASVAKTFLTSdcVVVEIKEPEP 586
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
405-537 |
1.02e-03 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 41.65 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 405 VVAGGGAIEMELSKYLrDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGgmwYGVDINNENI 484
Cdd:PRK00013 410 IVPGGGVALLRAAPAL-EALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKG---YGYNAATGEY 485
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814391 485 ADNFQAFVWEPAMVRINAL-TAASEAA------CLIVSVDETiknprstvDPPAPSAGRG 537
Cdd:PRK00013 486 VDMIEAGIIDPTKVTRSALqNAASVAGllltteAVVADKPEK--------KAAAPPMGGG 537
|
|
| |
