|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
9-529 |
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: 970.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 9 TIVVLKEGTDASQGKGQIISNINACIAIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDISR 88
Cdd:cd03340 1 PIILLKEGTDTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 89 AQDAEVGDGTTSVTILAGELMKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVSVEHEGS-RELLERCARTAMS 167
Cdd:cd03340 81 SQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKEEqRELLEKCAATALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 168 SKLIYKNADFFVKMCVDAVLSLDKDDLDDKlIGIKKIPGGAMEESMFIDGVAFKKTFSYAGFEQQPKNFKNPKILSLNVE 247
Cdd:cd03340 161 SKLIASEKEFFAKMVVDAVLSLDDDLDLDM-IGIKKVPGGSLEDSQLVNGVAFKKTFSYAGFEQQPKKFKNPKILLLNVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 248 LELKAEKDNAEVRVEQVSDYQAIVDAEWQIILDKLEQIKDTGANIVLSKLPIGDLATQYFADRNIFCAGRVSSDDMNRVI 327
Cdd:cd03340 240 LELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 328 QAVGGSIQSTTSDIKPDYLGTCETFEEIQIGAERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIVKRALQNK 407
Cdd:cd03340 320 QATGGSIQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKND 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 408 LVVAGGGAIEMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSKGE-KWFGVDFETE 486
Cdd:cd03340 400 SVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGgKWYGVDINNE 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 365983922 487 NIGDNFSKFVWEPALVKINALQSATEATNLILSVDETITNQEH 529
Cdd:cd03340 480 GIADNFEAFVWEPSLVKINALTAATEAACLILSVDETIKNPKS 522
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
7-529 |
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: 900.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 7 TPTIVVLKEGTDASQGKGQIISNINACIAIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDI 86
Cdd:TIGR02345 1 RPTIVLLKEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 87 SRAQDAEVGDGTTSVTILAGELMKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVSVEHEGSRELLERCARTAM 166
Cdd:TIGR02345 81 AKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKGEQRELLEKCAATAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 167 SSKLIYKNADFFVKMCVDAVLSLDKDDLDDKLIGIKKIPGGAMEESMFIDGVAFKKTFSYAGFEQQPKNFKNPKILSLNV 246
Cdd:TIGR02345 161 SSKLISHNKEFFSKMIVDAVLSLDRDDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAGFEQQPKKFANPKILLLNV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 247 ELELKAEKDNAEVRVEQVSDYQAIVDAEWQIILDKLEQIKDTGANIVLSKLPIGDLATQYFADRNIFCAGRVSSDDMNRV 326
Cdd:TIGR02345 241 ELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 327 IQAVGGSIQSTTSDIKPDYLGTCETFEEIQIGAERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIVKRALQN 406
Cdd:TIGR02345 321 IKACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 407 KLVVAGGGAIEMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSKGEKWFGVDFETE 486
Cdd:TIGR02345 401 KKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTE 480
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 365983922 487 NIGDNFSKFVWEPALVKINALQSATEATNLILSVDETITNQEH 529
Cdd:TIGR02345 481 DIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITNPKS 523
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
17-525 |
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: 549.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 17 TDASQGKGQIISNINACIAIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDISRAQDAEVGD 96
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 97 GTTSVTILAGELMKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVSVEhegSRELLERCARTAMSSKLIYKNAD 176
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVE---DREELLKVATTSLNSKLVSGGDD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 177 FFVKMCVDAVLSLDKDDLDDKL--IGIKKIPGGAMEESMFIDGVAFKKTFSYAGFeqqPKNFKNPKILSLNVELElkaek 254
Cdd:cd00309 158 FLGELVVDAVLKVGKENGDVDLgvIRVEKKKGGSLEDSELVVGMVFDKGYLSPYM---PKRLENAKILLLDCKLE----- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 255 dnaevrveqvsdyqaivdaewqiildkleqikdtgaNIVLSKLPIGDLATQYFADRNIFCAGRVSSDDMNRVIQAVGGSI 334
Cdd:cd00309 230 ------------------------------------YVVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 335 QSTTSDIKPDYLGTCETFEEIQIGAERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIVKRALQNKLVVAGGG 414
Cdd:cd00309 274 VSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 415 AIEMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSKGEKWFGVDFETENIGDNFSK 494
Cdd:cd00309 354 AAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKEA 433
|
490 500 510
....*....|....*....|....*....|.
gi 365983922 495 FVWEPALVKINALQSATEATNLILSVDETIT 525
Cdd:cd00309 434 GIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
36-524 |
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: 528.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 36 IQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDISRAQDAEVGDGTTSVTILAGELMKEAKPF 115
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 116 LEEGISSHIIMKGYRTAVRLAVEKIKELATdVSVEhEGSRELLERCARTAMSSKLIYKNADFFVKMCVDAVLSLDKDDLD 195
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIIS-IPVE-DVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 196 D--KLIGIKKIPGGAMEESMFIDGVAFKKTFSYagfEQQPKNFKNPKILSLNVELELKAEKDNAEVRVEQVSDYQAIVDA 273
Cdd:pfam00118 159 FdlGNIGVVKILGGSLEDSELVDGVVLDKGPLH---PDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 274 EWQIILDKLEQIKDTGANIVLSKLPIGDLATQYFADRNIFCAGRVSSDDMNRVIQAVGGSIQSTTSDIKPDYLGTCETFE 353
Cdd:pfam00118 236 EEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 354 EIQIGAERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIVKRALQNKLVVAGGGAIEMEISKYLRDYSKTIAG 433
Cdd:pfam00118 316 EEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 434 KQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSKGEKWFGVDFETENIGDNFSKFVWEPALVKINALQSATEA 513
Cdd:pfam00118 396 KEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEA 475
|
490
....*....|.
gi 365983922 514 TNLILSVDETI 524
Cdd:pfam00118 476 ASTILRIDDII 486
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
10-524 |
3.59e-162 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 471.74 E-value: 3.59e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 10 IVVLKEGTDASQGKGQIISNINACIAIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDISRA 89
Cdd:NF041083 3 VLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 90 QDAEVGDGTTSVTILAGELMKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVSVEhegSRELLERCARTAMSSK 169
Cdd:NF041083 83 QDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPD---DRETLKKIAETSLTSK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 170 LIYKNADFFVKMCVDAVLSLDKDDLDDKL-----IGIKKIPGGAMEESMFIDGVAFKKTFSYAGFeqqPKNFKNPKILSL 244
Cdd:NF041083 160 GVEEARDYLAEIAVKAVKQVAEKRDGKYYvdldnIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGM---PKRVENAKIALL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 245 NVELELKAEKDNAEVRVEQVSDYQAIVDAEWQIILDKLEQIKDTGANIVLSKLPIGDLATQYFADRNIFCAGRVSSDDMN 324
Cdd:NF041083 237 DAPLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDME 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 325 RVIQAVGGSIQSTTSDIKPDYLGTCETFEEIQIGAERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIVKRAL 404
Cdd:NF041083 317 KLAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 405 QNKLVVAGGGAIEMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSKGEKWFGVDFE 484
Cdd:NF041083 397 EDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVF 476
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 365983922 485 TENIGDNFSKFVWEPALVKINALQSATEATNLILSVDETI 524
Cdd:NF041083 477 TGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVI 516
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
10-524 |
4.03e-161 |
|
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: 469.05 E-value: 4.03e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 10 IVVLKEGTDASQGKGQIISNINACIAIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDISRA 89
Cdd:cd03343 1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 90 QDAEVGDGTTSVTILAGELMKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVSVEhegSRELLERCARTAMSSK 169
Cdd:cd03343 81 QDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPD---DKDTLRKIAKTSLTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 170 LIYKNADFFVKMCVDAVLSLDKDDLDDKL-----IGIKKIPGGAMEESMFIDGVAFKKTFSYagfEQQPKNFKNPKILSL 244
Cdd:cd03343 158 GAEAAKDKLADLVVDAVLQVAEKRDGKYVvdldnIKIEKKTGGSVDDTELIRGIVIDKEVVH---PGMPKRVENAKIALL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 245 NVELELKAEKDNAEVRVEQVSDYQAIVDAEWQIILDKLEQIKDTGANIVLSKLPIGDLATQYFADRNIFCAGRVSSDDMN 324
Cdd:cd03343 235 DAPLEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDME 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 325 RVIQAVGGSIQSTTSDIKPDYLGTCETFEEIQIGAERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIVKRAL 404
Cdd:cd03343 315 KLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADAL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 405 QNKLVVAGGGAIEMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSKGEKWFGVDFE 484
Cdd:cd03343 395 EDGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVY 474
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 365983922 485 TENIGDNFSKFVWEPALVKINALQSATEATNLILSVDETI 524
Cdd:cd03343 475 TGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVI 514
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
10-524 |
7.70e-160 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 465.51 E-value: 7.70e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 10 IVVLKEGTDASQGKGQIISNINACIAIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDISRA 89
Cdd:NF041082 3 ILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 90 QDAEVGDGTTSVTILAGELMKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVSVEhegSRELLERCARTAMSSK 169
Cdd:NF041082 83 QDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPD---DKETLKKIAATAMTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 170 LIYKNADFFVKMCVDAVLSLDKDDLDDK----LIGIKKIPGGAMEESMFIDGVAFKKTFSYAGFeqqPKNFKNPKILSLN 245
Cdd:NF041082 160 GAEAAKDKLADLVVDAVKAVAEKDGGYNvdldNIKVEKKVGGSIEDSELVEGVVIDKERVHPGM---PKRVENAKIALLD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 246 VELELKAEKDNAEVRVEQVSDYQAIVDAEWQIILDKLEQIKDTGANIVLSKLPIGDLATQYFADRNIFCAGRVSSDDMNR 325
Cdd:NF041082 237 APLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 326 VIQAVGGSIQSTTSDIKPDYLGTCETFEEIQIGAERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIVKRALQ 405
Cdd:NF041082 317 LAKATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 406 NKLVVAGGGAIEMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSKGEKWFGVDFET 485
Cdd:NF041082 397 DGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYT 476
|
490 500 510
....*....|....*....|....*....|....*....
gi 365983922 486 ENIGDNFSKFVWEPALVKINALQSATEATNLILSVDETI 524
Cdd:NF041082 477 GKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVI 515
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
10-524 |
2.91e-151 |
|
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: 443.74 E-value: 2.91e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 10 IVVLKEGTDASQGKGQIISNINACIAIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDISRA 89
Cdd:TIGR02339 2 VFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 90 QDAEVGDGTTSVTILAGELMKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVSVEhegSRELLERCARTAMSSK 169
Cdd:TIGR02339 82 QDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPE---DRDLLKKIAYTSLTSK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 170 LIY-KNADFFVKMCVDAVLSLDKDDLDDKL------IGIKKIPGGAMEESMFIDGVAFKKTFSYAGFeqqPKNFKNPKIL 242
Cdd:TIGR02339 159 ASAeVAKDKLADLVVEAVKQVAELRGDGKYyvdldnIKIVKKKGGSIEDTELVEGIVVDKEVVHPGM---PKRVENAKIA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 243 SLNVELELKAEKDNAEVRVEQVSDYQAIVDAEWQIILDKLEQIKDTGANIVLSKLPIGDLATQYFADRNIFCAGRVSSDD 322
Cdd:TIGR02339 236 LLDAPLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 323 MNRVIQAVGGSIQSTTSDIKPDYLGTCETFEEIQIGAERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIVKR 402
Cdd:TIGR02339 316 IEKLARATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVAN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 403 ALQNKLVVAGGGAIEMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSKGEKWFGVD 482
Cdd:TIGR02339 396 ALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGIN 475
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 365983922 483 FETENIGDNFSKFVWEPALVKINALQSATEATNLILSVDETI 524
Cdd:TIGR02339 476 VFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVI 517
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
29-525 |
2.85e-137 |
|
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: 408.21 E-value: 2.85e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 29 NINACIAIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDISRAQDAEVGDGTTSVTILAGEL 108
Cdd:cd03335 13 NVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 109 MKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATdVSVEHEGsRELLERCARTAMSSKLIYKNADFFVKMCVDAVLS 188
Cdd:cd03335 93 LKRANELVKQKIHPTTIISGYRLACKEAVKYIKEHLS-ISVDNLG-KESLINVAKTSMSSKIIGADSDFFANMVVDAILA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 189 LDKDDLDDKL------IGIKKIPGGAMEESMFIDGVAFKKTfsyAGFEQQPKNFKNPKILSLNVELELKAEKDNAEVRVE 262
Cdd:cd03335 171 VKTTNEKGKTkypikaVNILKAHGKSAKESYLVNGYALNCT---RASQGMPTRVKNAKIACLDFNLQKTKMKLGVQVVVT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 263 QVSDYQAIVDAEWQIILDKLEQIKDTGANIVLSKLPIGDLATQYFADRNIFCAGRVSSDDMNRVIQAVGGSIQSTTSDIK 342
Cdd:cd03335 248 DPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVSTLANLE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 343 ------PDYLGTCETFEEIQIGAERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIVKRALQNKLVVAGGGAI 416
Cdd:cd03335 328 geetfdPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGGAV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 417 EMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHS--------KGEKWFGVDFETENI 488
Cdd:cd03335 408 ETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAaaqvkpdkKHLKWYGLDLINGKV 487
|
490 500 510
....*....|....*....|....*....|....*..
gi 365983922 489 GDNFSKFVWEPALVKINALQSATEATNLILSVDETIT 525
Cdd:cd03335 488 RDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
16-533 |
1.81e-132 |
|
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: 396.40 E-value: 1.81e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 16 GTDASQGKGQIISNINACIAIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDISRAQDAEVG 95
Cdd:TIGR02340 4 GGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 96 DGTTSVTILAGELMKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKE-LATDVSvehEGSRELLERCARTAMSSKLIYKN 174
Cdd:TIGR02340 84 DGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVD---ELGREALINVAKTSMSSKIIGLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 175 ADFFVKMCVDAVLSLDKDDLDDKL------IGIKKIPGGAMEESMFIDGVAFKKTfsyAGFEQQPKNFKNPKILSLNVEL 248
Cdd:TIGR02340 161 SDFFSNIVVDAVLAVKTTNENGETkypikaINILKAHGKSARESMLVKGYALNCT---VASQQMPKRIKNAKIACLDFNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 249 ELKAEKDNAEVRVEQVSDYQAIVDAEWQIILDKLEQIKDTGANIVLSKLPIGDLATQYFADRNIFCAGRVSSDDMNRVIQ 328
Cdd:TIGR02340 238 QKAKMALGVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 329 AVGGSIQSTTSDIK------PDYLGTCETFEEIQIGAERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIVKR 402
Cdd:TIGR02340 318 ATGATLVSTLADLEgeetfeASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 403 ALQNKLVVAGGGAIEMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHS--------K 474
Cdd:TIGR02340 398 TLESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAaaqlkpekK 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 365983922 475 GEKWFGVDFETENIGDNFSKFVWEPALVKINALQSATEATNLILSVDETITNQEHQSAN 533
Cdd:TIGR02340 478 HLKWYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIKLNPEQSKG 536
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-524 |
2.19e-132 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 395.94 E-value: 2.19e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 1 MNFGNRTPTIvvLKEGtdASQGKGQI--ISNINACIAIQETLKPTLGPLGSD-ILIVTS----NQKTTISNDGATILRLL 73
Cdd:PTZ00212 1 MIMANVPPQV--LKQG--AQEEKGETarLQSFVGAIAVADLVKTTLGPKGMDkILQPMSegprSGNVTVTNDGATILKSV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 74 DVVHPAARTLVDISRAQDAEVGDGTTSVTILAGELMKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVSVEHEG 153
Cdd:PTZ00212 77 WLDNPAAKILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 154 SRELLERCARTAMSSKLIYKNADFFVKMCVDAVLSLDKDDLDDKlIGIKKIPGGAMEESMFIDGVAFKKTFSYAgfeqQP 233
Cdd:PTZ00212 157 FKEDLLNIARTTLSSKLLTVEKDHFAKLAVDAVLRLKGSGNLDY-IQIIKKPGGTLRDSYLEDGFILEKKIGVG----QP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 234 KNFKNPKILSLNVELEL-KAEKDNAEVRVEQVSDYQAIVDAEWQIILDKLEQIKDTGANIVLSKLPIGDLATQYFADRNI 312
Cdd:PTZ00212 232 KRLENCKILVANTPMDTdKIKIYGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 313 FCAGRVSSDDMNRVIQAVGGSIQSTTSDIKPDYLGTCETFEEIQIGAERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERS 392
Cdd:PTZ00212 312 MAIEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 393 LHDAIMIVKRALQNKLVVAGGGAIEMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAH 472
Cdd:PTZ00212 392 LHDALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEH 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 365983922 473 SKGEKWFGVDFETENIGDNFSKFVWEPALVKINALQSATEATNLILSVDETI 524
Cdd:PTZ00212 472 YKGNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDII 523
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
12-525 |
4.68e-123 |
|
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: 371.66 E-value: 4.68e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 12 VLKEGTDASQGKGQIISNINACIAIQETLKPTLGPLGSD-ILIVTSNQKT-TISNDGATILRLLDVVHPAARTLVDISRA 89
Cdd:cd03336 1 ILKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDkILQSVGRSGGvTVTNDGATILKSIGVDNPAAKVLVDISKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 90 QDAEVGDGTTSVTILAGELMKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVSVEHEGSRELLERCARTAMSSK 169
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEAFREDLLNIARTTLSSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 170 LIYKNADFFVKMCVDAVLSLDKDDLDDKlIGIKKIPGGAMEESMFIDGVAFKKTFSYAgfeqQPKNFKNPKILSLNVELE 249
Cdd:cd03336 161 ILTQDKEHFAELAVDAVLRLKGSGNLDA-IQIIKKLGGSLKDSYLDEGFLLDKKIGVN----QPKRIENAKILIANTPMD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 250 L-KAEKDNAEVRVEQVSDYQAIVDAEWQIILDKLEQIKDTGANIVLSKLPIGDLATQYFADRNIFCAGRVSSDDMNRVIQ 328
Cdd:cd03336 236 TdKIKIFGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLAL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 329 AVGGSIQSTTSDIKPDYLGTCETFEEIQIGAERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIVKRALQNKL 408
Cdd:cd03336 316 VTGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 409 VVAGGGAIEMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSKGEKWFGVDFETENI 488
Cdd:cd03336 396 VVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTV 475
|
490 500 510
....*....|....*....|....*....|....*..
gi 365983922 489 GDNFSKFVWEPALVKINALQSATEATNLILSVDETIT 525
Cdd:cd03336 476 GDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIK 512
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
10-524 |
2.04e-118 |
|
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: 358.15 E-value: 2.04e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 10 IVVLKEGTDASQGKGQIISNINACIAIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDISRA 89
Cdd:cd03337 2 VLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 90 QDAEVGDGTTSVTILAGELMKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVSVEhegSRELLERCARTAMSSK 169
Cdd:cd03337 82 QDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVN---DRAQMLKIIKSCIGTK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 170 LIYKNADFFVKMCVDAVLS-LDKDDLDDKLIGIK------KIPGGAMEESMFIDGVAFKKTFSYAGFEqqpKNFKNPKIL 242
Cdd:cd03337 159 FVSRWSDLMCNLALDAVKTvAVEENGRKKEIDIKryakveKIPGGEIEDSRVLDGVMLNKDVTHPKMR---RRIENPRIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 243 SLNVELElkaekdnaevrveqvsdYqaivdaewqiildkleqikdtganIVLSKLPIGDLATQYFADRNIFCAGRVSSDD 322
Cdd:cd03337 236 LLDCPLE-----------------Y------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 323 MNRVIQAVGGSIQSTTSDIKPDYLGTCETFEEIQ-IGAERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIVK 401
Cdd:cd03337 275 NNRIARACGATIVNRPEELTESDVGTGAGLFEVKkIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVAR 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 402 RALQNKLVVAGGGAIEMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSKGEK-WFG 480
Cdd:cd03337 355 NIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENsTWG 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 365983922 481 VDFETENIGDNFSKFVWEPALVKINALQSATEATNLILSVDETI 524
Cdd:cd03337 435 IDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
9-525 |
2.56e-113 |
|
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: 346.73 E-value: 2.56e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 9 TIVVLKEGTDASQGKGQIISNINACIAIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDISR 88
Cdd:TIGR02344 1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 89 AQDAEVGDGTTSVTILAGELMKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVSVEhegSRELLERCARTAMSS 168
Cdd:TIGR02344 81 TQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVN---DDAAMLKLIQSCIGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 169 KLIYKNADFFVKMCVDAVLSLDKDDLDDKLIGIK------KIPGGAMEESMFIDGVAFKKTFSYagfeqqPK---NFKNP 239
Cdd:TIGR02344 158 KFVSRWSDLMCDLALDAVRTVQRDENGRKEIDIKryakveKIPGGDIEDSCVLKGVMINKDVTH------PKmrrYIENP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 240 KILSLNVELELKAEKDNAEVRVEQVSDYQAIVDAEWQIILDKLEQIKDTGANIVLSKLPIGDLATQYFADRNIFCAGRVS 319
Cdd:TIGR02344 232 RIVLLDCPLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 320 SDDMNRVIQAVGGSIQSTTSDIKPDYLGT-CETFEEIQIGAERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIM 398
Cdd:TIGR02344 312 KTDNNRIARACGATIVNRPEELRESDVGTgCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 399 IVKRALQNKLVVAGGGAIEMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSKGEK- 477
Cdd:TIGR02344 392 VARNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNc 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 365983922 478 WFGVDFETENIGDNFSKFVWEPALVKINALQSATEATNLILSVDETIT 525
Cdd:TIGR02344 472 TWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVS 519
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
28-525 |
2.54e-108 |
|
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: 333.48 E-value: 2.54e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 28 SNINACIAIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDISRAQDAEVGDGTTSVTILAGE 107
Cdd:cd03338 12 SNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 108 LMKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVSVEhegSRELLERCARTAMSSKLIYKNADFFVKMCVDAVL 187
Cdd:cd03338 92 LLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLN---DRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 188 SLDKDDLDDKL----IGIKKIPGGAMEESMFIDGVAFKKTFSYAGfeQQPKNFKNPKILSLNVELE-LKAEKDNAEVrve 262
Cdd:cd03338 169 KVIDPATATNVdlkdIRIVKKLGGTIEDTELVDGLVFTQKASKKA--GGPTRIEKAKIGLIQFCLSpPKTDMDNNIV--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 263 qVSDYQA---IVDAEWQIILDKLEQIKDTGANIVL---SKL--PIGDLATQYFADRNIFCAGRVSSDDMNRVIQAVGGSI 334
Cdd:cd03338 244 -VNDYAQmdrILREERKYILNMCKKIKKSGCNVLLiqkSILrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 335 QSTTSDIKPDYLGTCETFEEIQIGAERYNLFKGCPQA-KTCTLLLRGGAEQVIAEVERSLHDAIMIVKRALQNKLVVAGG 413
Cdd:cd03338 323 VASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 414 GAIEMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSKGEKWFGVDFETENIGDNFS 493
Cdd:cd03338 403 GAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITNILE 482
|
490 500 510
....*....|....*....|....*....|..
gi 365983922 494 KFVWEPALVKINALQSATEATNLILSVDETIT 525
Cdd:cd03338 483 ENVVQPLLVSTSAITLATETVRMILKIDDIVL 514
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
11-525 |
4.40e-106 |
|
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: 328.10 E-value: 4.40e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 11 VVLKEGTDASQGKGQ--IISNINACIAIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDISR 88
Cdd:cd03339 8 IIVREQEKKKRLKGLeaHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 89 AQDAEVGDGTTSVTILAGELMKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVSVEHEgSRELLERCARTAMSS 168
Cdd:cd03339 88 SQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPD-NKEPLIQTAMTSLGS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 169 KLIYKNADFFVKMCVDAVLSLDKDDLDDKLIGIKKI---PGGAMEESMFIDGVAFKKTFSYAgfeQQPKNFKNPKILSLN 245
Cdd:cd03339 167 KIVSRCHRQFAEIAVDAVLSVADLERKDVNFELIKVegkVGGRLEDTKLVKGIVIDKDFSHP---QMPKEVKDAKIAILT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 246 VELELKAEKDNAEVRVEQVSDYQAIVDAEWQIILDKLEQIKDTGANIVLSKLPIGDLATQYFADRNIFCAGRVSSDDMNR 325
Cdd:cd03339 244 CPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 326 VIQAVGGSIQSTTSDIKPDYLGTCETFEEIQIGA--ERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIVKRA 403
Cdd:cd03339 324 IAIATGGRIVPRFEDLSPEKLGKAGLVREISFGTtkDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 404 LQNKLVVAGGGAIEMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSK-GEKWFGVD 482
Cdd:cd03339 404 IRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKeKNPHLGID 483
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 365983922 483 FETENIGDNFSKFVWEPALVKINALQSATEATNLILSVDETIT 525
Cdd:cd03339 484 CLGRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
28-522 |
1.16e-101 |
|
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: 316.34 E-value: 1.16e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 28 SNINACIAIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDISRAQDAEVGDGTTSVTILAGE 107
Cdd:TIGR02342 13 SNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 108 LMKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVSVeheGSRELLERCARTAMSSKLIYKNADFFVKMCVDAVL 187
Cdd:TIGR02342 93 LLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDL---SDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 188 SLDKDDLDDKL----IGIKKIPGGAMEESMFIDGVAFKKTFSYAgfEQQPKNFKNPKILSLNVELEL-KAEKDNAEVrve 262
Cdd:TIGR02342 170 KVIDPENAKNVdlndIKVVKKLGGTIDDTELIEGLVFTQKASKS--AGGPTRIEKAKIGLIQFQISPpKTDMENQII--- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 263 qVSDYQA---IVDAEWQIILDKLEQIKDTGANIVLSKLPI-----GDLATQYFADRNIFCAGRVSSDDMNRVIQAVGGSI 334
Cdd:TIGR02342 245 -VNDYAQmdrVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 335 QSTTSDIKPDYLGTCETFEEIQIGAERYNLFKGCPQA-KTCTLLLRGGAEQVIAEVERSLHDAIMIVKRALQNKLVVAGG 413
Cdd:TIGR02342 324 IASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 414 GAIEMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSKGEKWFGVDFETENIGDNFS 493
Cdd:TIGR02342 404 GAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITNMLE 483
|
490 500
....*....|....*....|....*....
gi 365983922 494 KFVWEPALVKINALQSATEATNLILSVDE 522
Cdd:TIGR02342 484 EHVLQPLLVTTSAITLASETVRSILKIDD 512
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
12-524 |
2.85e-99 |
|
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: 310.25 E-value: 2.85e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 12 VLKEGTDASQGKGQIISNINACIAIQETLKPTLGPLGSDILIVTSNQKTTI--SNDGATILRLLDVVHPAARTLVDISRA 89
Cdd:TIGR02341 2 IFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSSSDASImvTNDGATILKSIGVDNPAAKVLVDMSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 90 QDAEVGDGTTSVTILAGELMKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVSVEHEGSRELLERCARTAMSSK 169
Cdd:TIGR02341 82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVKFRQDLMNIARTTLSSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 170 LIYKNADFFVKMCVDAVLSLDKDDLDDKlIGIKKIPGGAMEESMFIDGVAFKKTFSYagfeQQPKNFKNPKILSLNVELE 249
Cdd:TIGR02341 162 ILSQHKDHFAQLAVDAVLRLKGSGNLEA-IQIIKKLGGSLADSYLDEGFLLDKKIGV----NQPKRIENAKILIANTGMD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 250 L-KAEKDNAEVRVEQVSDYQAIVDAEWQIILDKLEQIKDTGANIVLSKLPIGDLATQYFADRNIFCAGRVSSDDMNRVIQ 328
Cdd:TIGR02341 237 TdKVKIFGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 329 AVGGSIQSTTSDIKPDYLGTCETFEEIQIGAERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIVKRALQNKL 408
Cdd:TIGR02341 317 VTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 409 VVAGGGAIEMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSKGEKWFGVDFETENI 488
Cdd:TIGR02341 397 TVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGTI 476
|
490 500 510
....*....|....*....|....*....|....*.
gi 365983922 489 GDNFSKFVWEPALVKINALQSATEATNLILSVDETI 524
Cdd:TIGR02341 477 ADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNII 512
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
28-528 |
1.26e-98 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 307.78 E-value: 1.26e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 28 SNINACIAIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHP----AARTLVDISRAQDAEVGDGTTSVTI 103
Cdd:COG0459 14 ANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTTTATV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 104 LAGELMKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVSvehegSRELLERCARTAMSSKliyknaDFFVKMCV 183
Cdd:COG0459 94 LAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVD-----DKEELAQVATISANGD------EEIGELIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 184 DAVLsldkddlddkLIG----IKKIPGGAME-ESMFIDGVAFKKTFSYAGF----EQQPKNFKNPKILSLNVELELKaek 254
Cdd:COG0459 163 EAME----------KVGkdgvITVEEGKGLEtELEVVEGMQFDKGYLSPYFvtdpEKMPAELENAYILLTDKKISSI--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 255 dnaevrveqvsdyqaivdaewQIILDKLEQIKDTGANIVLSKLPIGDLATQYFADRNIFCAGRVSS-----------DDM 323
Cdd:COG0459 230 ---------------------QDLLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAvkapgfgdrrkAML 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 324 NRVIQAVGGSIQS-----TTSDIKPDYLGTCETfeeIQIGAERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIM 398
Cdd:COG0459 289 EDIAILTGGRVISedlglKLEDVTLDDLGRAKR---VEVDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 399 IVKRALQNKlVVAGGGAIEMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRlahSKGEKW 478
Cdd:COG0459 366 ATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVR---AAKDKG 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 365983922 479 FGVDFETENIGDNFSKFVWEPALVKINALQSATEATNLILSVDETITNQE 528
Cdd:COG0459 442 FGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKP 491
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
11-526 |
6.73e-96 |
|
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: 302.11 E-value: 6.73e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 11 VVLKEGTDASQGKGQ--IISNINACIAIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDISR 88
Cdd:TIGR02343 12 IIIKDQDNKKRLKGLeaKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 89 AQDAEVGDGTTSVTILAGELMKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVSVEhEGSRELLERCARTAMSS 168
Cdd:TIGR02343 92 SQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISAD-NNNREPLIQAAKTSLGS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 169 KLIYKNADFFVKMCVDAVLSLDKDDLDDKLIGIKKIP---GGAMEESMFIDGVAFKKTFSYAgfeQQPKNFKNPKILSLN 245
Cdd:TIGR02343 171 KIVSKCHRRFAEIAVDAVLNVADMERRDVDFDLIKVEgkvGGSLEDTKLIKGIIIDKDFSHP---QMPKEVEDAKIAILT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 246 VELELKAEKDNAEVRVEQVSDYQAIVDAEWQIILDKLEQIKDTGANIVLSKLPIGDLATQYFADRNIFCAGRVSSDDMNR 325
Cdd:TIGR02343 248 CPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELEL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 326 VIQAVGGSIQSTTSDIKPDYLGTCETFEEIQIGA--ERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIVKRA 403
Cdd:TIGR02343 328 IAIATGGRIVPRFQELSKDKLGKAGLVREISFGTtkDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 404 LQNKLVVAGGGAIEMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSKGEKWF-GVD 482
Cdd:TIGR02343 408 IKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNlGVD 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 365983922 483 FETENIGDNFSKFVWEPALVKINALQSATEATNLILSVDETITN 526
Cdd:TIGR02343 488 CLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVISP 531
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
24-524 |
2.36e-91 |
|
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: 288.35 E-value: 2.36e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 24 GQIISNINACIAIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDISRAQDAEVGDGTTSVTI 103
Cdd:cd03341 8 EAVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 104 LAGELMKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDvSVEHEGSRELLERCARTAMSSKlIYKNADFFVKMCV 183
Cdd:cd03341 88 LAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVY-KIEDLRNKEEVSKALKTAIASK-QYGNEDFLSPLVA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 184 DAVLSLDKDDLDD---KLIGIKKIPGGAMEESMFIDGVAFKKtfsyaGFEQQPKNFKNPKILSLNVELelkaekdnaevr 260
Cdd:cd03341 166 EACISVLPENIGNfnvDNIRVVKILGGSLEDSKVVRGMVFKR-----EPEGSVKRVKKAKVAVFSCPF------------ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 261 veqvsdyqaivdaewqiildkleqikDTGANIVLSKLPIGDLAtQYFADRNIFCAGRVSSD-DMNRVIQAVGGSIQSTTS 339
Cdd:cd03341 229 --------------------------DIGVNVIVAGGSVGDLA-LHYCNKYGIMVIKINSKfELRRLCRTVGATPLPRLG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 340 DIKPDYLGTCETFEEIQIGAERYNLFKGCPQA-KTCTLLLRGGAEQVIAEVERSLHDAIMIVKRALQNKLVVAGGGAIEM 418
Cdd:cd03341 282 APTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDsKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 419 EISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSKGEKWFGVDFETENIG--DNFSKFV 496
Cdd:cd03341 362 ELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDEGtkDAKEAGI 441
|
490 500
....*....|....*....|....*...
gi 365983922 497 WEPALVKINALQSATEATNLILSVDETI 524
Cdd:cd03341 442 FDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
12-524 |
4.40e-87 |
|
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: 278.91 E-value: 4.40e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 12 VLKEGTDASQG-KGQIISNINACIAIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDISRAQ 90
Cdd:TIGR02346 5 LLKEGYRHFSGlEEAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 91 DAEVGDGTTSVTILAGELMKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDvSVEHEGSRELLERCARTAMSSKL 170
Cdd:TIGR02346 85 ENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVW-EVKDLRDKDELIKALKASISSKQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 171 iYKNADFFVKMCVDAVLSLDKDDLDD---KLIGIKKIPGGAMEESMFIDGVAFKKTfsyagFEQQPKNFKNPKILSLNVE 247
Cdd:TIGR02346 164 -YGNEDFLAQLVAQACSTVLPKNPQNfnvDNIRVCKILGGSLSNSEVLKGMVFNRE-----AEGSVKSVKNAKVAVFSCP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 248 LELKAEKDNAEVRV---EQVSDYQaivDAEWQIILDKLEQIKDTGANIVLSKLPIGDLAtQYFADRNIFCAGRVSSD-DM 323
Cdd:TIGR02346 238 LDTATTETKGTVLIhnaEELLNYS---KGEENQIEAMIKAIADSGVNVIVTGGSVGDMA-LHYLNKYNIMVLKIPSKfEL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 324 NRVIQAVGGSIQSTTSDIKPDYLGTCETFEEIQIGAERYNLFKGCPQ-AKTCTLLLRGGAEQVIAEVERSLHDAIMIVKR 402
Cdd:TIGR02346 314 RRLCKTVGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGdSKISTIILRGSTDNLLDDIERAIDDGVNTVKA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 403 ALQNKLVVAGGGAIEMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSKGEKWFGVD 482
Cdd:TIGR02346 394 LVKDGRLLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGID 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 365983922 483 FETENIG--DNFSKFVWEPALVKINALQSATEATNLILSVDETI 524
Cdd:TIGR02346 474 IEAESDGvkDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQII 517
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
29-524 |
1.30e-79 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239458 [Multi-domain] Cd Length: 484 Bit Score: 257.96 E-value: 1.30e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 29 NINACIAIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDISRAQDAEVGDGTTSVTILAGEL 108
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 109 MKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELAtdVSVEHEGSRELLERCARTAMSSKLIYKNADFFVKMCVDAVLS 188
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGFELAKNKALKFLESFK--VPVEIDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAVLA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 189 LDKDDLDD--KLIGIKKIPGGAMEESMFIDGVAFKKTFSYAGFeqqPKNFKNPKILSLNVELELkaEKdnAEVRVEQVSd 266
Cdd:cd03342 175 IYKPDEPIdlHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDM---PKRVENAYILTCNVSLEY--EK--TEVNSGFFY- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 267 yqaivdaewqiildkleqikdtgaNIVLSKLPIGDLATQYFADRNIFCAGRVSSDDMNRVIQAVGGSIQSTTSDIKPDYL 346
Cdd:cd03342 247 ------------------------SVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPECL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 347 GTCETFEEIQIGAERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIVKRALQNKLVVAGGGAIEMEISKYLRD 426
Cdd:cd03342 303 GYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHLKE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 427 YSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSKGEKWFGVDFETENIGDNFSKFVWEPALVKINA 506
Cdd:cd03342 383 FKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQI 462
|
490
....*....|....*...
gi 365983922 507 LQSATEATNLILSVDETI 524
Cdd:cd03342 463 LHSATVIASQLLLVDEII 480
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
29-524 |
2.58e-78 |
|
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274088 [Multi-domain] Cd Length: 531 Bit Score: 255.81 E-value: 2.58e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 29 NINACIAIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDISRAQDAEVGDGTTSVTILAGEL 108
Cdd:TIGR02347 21 NINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 109 MKEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELAtdVSVEHEGSRELLERCARTAMSSKLIYKNADFFVKMCVDAVLS 188
Cdd:TIGR02347 101 LKQAERYILEGVHPRIITEGFEIARKEALQFLDKFK--VKKEDEVDREFLLNVARTSLRTKLPADLADQLTEIVVDAVLA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 189 LDKDDLDDK--LIGIKKIPGGAMEESMFIDGVAFKKTFSYAGFeqqPKNFKNPKILSLNVELELKAEKDNAEVRVEQVSD 266
Cdd:TIGR02347 179 IKKDGEDIDlfMVEIMEMKHKSATDTTLIRGLVLDHGARHPDM---PRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 267 YQAIVDAEWQIILDKLEQIKDTgANIVLSKLP-----------IGDLATQYFADRNIFCAGRVSSDDMNRVIQAVGGSIQ 335
Cdd:TIGR02347 256 REKLVKAERKFVDDRVKKIIEL-KKKVCGKSPdkgfvvinqkgIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEAL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 336 STTSDIKPDYLGTCETFEEIQIGAERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIVKRALQNKLVVAGGGA 415
Cdd:TIGR02347 335 NSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAGA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 416 IEMEISKYLRDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSKGEKWFGVDFETENIGDNFSKF 495
Cdd:TIGR02347 415 FEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGVDLNTGEPIDPEIKG 494
|
490 500 510
....*....|....*....|....*....|
gi 365983922 496 VWEPALVKINALQSATE-ATNLILsVDETI 524
Cdd:TIGR02347 495 IWDNYRVKKQLIQSATViASQLLL-VDEVM 523
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
155-406 |
6.35e-64 |
|
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: 207.70 E-value: 6.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 155 RELLERCARTAMSSKlIYKNADFFVKMCVDAVLSLDKDDLDDKL--IGIKKIPGGAMEESMFIDGVAFKKTFSYAGFeqq 232
Cdd:cd03333 1 RELLLQVATTSLNSK-LSSWDDFLGKLVVDAVLKVGPDNRMDDLgvIKVEKIPGGSLEDSELVVGVVFDKGYASPYM--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 233 PKNFKNPKILSLNVELElkaekdnaevrveqvsdyqaivdaewqiildkleqikdtgaNIVLSKLPIGDLATQYFADRNI 312
Cdd:cd03333 77 PKRLENAKILLLDCPLE-----------------------------------------YVVIAEKGIDDLALHYLAKAGI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 313 FCAGRVSSDDMNRVIQAVGGSIQSTTSDIKPDYLGTCETFEEIQIGAERYNLFKGCPQAKTCTLLLRGGAEQVIAEVERS 392
Cdd:cd03333 116 MAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRS 195
|
250
....*....|....
gi 365983922 393 LHDAIMIVKRALQN 406
Cdd:cd03333 196 LHDALCAVRAAVEE 209
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
201-400 |
1.25e-18 |
|
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: 85.74 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 201 IKKIPGGAMEESMFIDGVAFKKTfsyAGFEQQPKNFKNPKILSLNVELELKaekdnaevRVE-QVSDYQAIVDAEwQIIL 279
Cdd:cd03334 52 IKKIPGGSPSDSEVVDGVVFTKN---VAHKRMPSKIKNPRILLLQGPLEYQ--------RVEnKLLSLDPVILQE-KEYL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 280 DKLEQ-IKDTGANIVLSKLPIGDLATQYFADRNIFCAGRVSSDDMNRVIQAVGGSIQSTTSD-IKPDYLGTCETFEEIQI 357
Cdd:cd03334 120 KNLVSrIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDlLTSPKLGTCESFRVRTY 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 365983922 358 GAER-----YNLFKGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIV 400
Cdd:cd03334 200 VEEHgrsktLMFFEGCPKELGCTILLRGGDLEELKKVKRVVEFMVFAA 247
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
43-541 |
9.46e-15 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 76.87 E-value: 9.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 43 TLGPLGSDILIVTSNQKTTISNDGATIL-------RLLDVvhpAARTLVDISRAQDAEVGDGTTSVTILAGELMKEAKPF 115
Cdd:PTZ00114 41 TLGPKGRNVIIEQEYGSPKITKDGVTVAkaiefsdRFENV---GAQLIRQVASKTNDKAGDGTTTATILARAIFREGCKA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 116 LEEGISSHIIMKGYRTAVRLAVEKIKELATDVSvehegSRELLERCARTAMS-----SKLIyknADFFVKMCVDAVlsld 190
Cdd:PTZ00114 118 VAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVK-----TKEDILNVATISANgdveiGSLI---ADAMDKVGKDGT---- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 191 kddlddkligIKKIPGGAME-ESMFIDGVAFKKTFSYAGFEQQPKN----FKNPKILS-----LNVE-----LEL-KAEK 254
Cdd:PTZ00114 186 ----------ITVEDGKTLEdELEVVEGMSFDRGYISPYFVTNEKTqkveLENPLILVtdkkiSSIQsilpiLEHaVKNK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 255 DNAEVRVEQVSDyqaivDAEWQIILDKLEQikdtGANIVLSKLP-IGDLATQYFADRNIFCAGRVSSDDmnrviqAVGGS 333
Cdd:PTZ00114 256 RPLLIIAEDVEG-----EALQTLIINKLRG----GLKVCAVKAPgFGDNRKDILQDIAVLTGATVVSED------NVGLK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 334 IqsttSDIKPDYLGTCETFE--------------EIQIgAERYNLFKGcpQAKTCT--------------------LLLR 379
Cdd:PTZ00114 321 L----DDFDPSMLGSAKKVTvtkdetviltgggdKAEI-KERVELLRS--QIERTTseydkeklkerlaklsggvaVIKV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 380 GGAEQV-IAEVERSLHDAIMIVKRALQNKlVVAGGGAIEMEISKYLrDYSKT---IAGKQQLIINAFAKALEVIPRQLCE 455
Cdd:PTZ00114 394 GGASEVeVNEKKDRIEDALNATRAAVEEG-IVPGGGVALLRASKLL-DKLEEdneLTPDQRTGVKIVRNALRLPTKQIAE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 456 NAGFDAVELLNKLRlahSKGEKWFGVDFETENIGDNFSKFVWEPALVKINALQSATEATNLILSVDETITNQEHQSANAG 535
Cdd:PTZ00114 472 NAGVEGAVVVEKIL---EKKDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKKKNK 548
|
....*.
gi 365983922 536 MMPPAP 541
Cdd:PTZ00114 549 NSAAPP 554
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
40-541 |
1.79e-12 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 69.87 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 40 LKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVV----HPAARTLVDISRAQDAEVGDGTTSVTILAGELMKEAKPF 115
Cdd:PRK12852 27 VKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKTNDLAGDGTTTATVLAQAIVREGAKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 116 LEEGISSHIIMKGYRTAVRLAVEKIKELATDVSveheGSRELLERCARTAMSSKLIYKN-ADFFVKMCVDAVLSLDKDDL 194
Cdd:PRK12852 107 VAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVA----SSAEIAQVGTISANGDAAIGKMiAQAMQKVGNEGVITVEENKS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 195 DDKLIGIkkipggameesmfIDGVAFKKTFsyagfeQQPKNFKNPKilslnvelELKAEKDNAEVRV--EQVSDYQA--- 269
Cdd:PRK12852 183 LETEVDI-------------VEGMKFDRGY------LSPYFVTNAE--------KMTVELDDAYILLheKKLSGLQAmlp 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 270 IVDAEWQ------IILDKLEqiKDTGANIVLSK----LPIGDLATQYFADRN--------IFCAGRVSSDDM-----NRV 326
Cdd:PRK12852 236 VLEAVVQsgkpllIIAEDVE--GEALATLVVNRlrggLKVAAVKAPGFGDRRkamlediaILTGGQLISEDLgikleNVT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 327 IQAVGGS----IQSTTSDI------KPDYLGTCETF----EEIQIGAERYNLFKGCPQAKTCTLLLR-GGAEQV-IAEVE 390
Cdd:PRK12852 314 LKMLGRAkkvvIDKENTTIvngagkKADIEARVGQIkaqiEETTSDYDREKLQERLAKLAGGVAVIRvGGATEVeVKEKK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 391 RSLHDAIMIVKRALQNKlVVAGGGAIEMEISKYLRDYSKTIAgKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRl 470
Cdd:PRK12852 394 DRVEDALNATRAAVQEG-IVPGGGVALLRAKKAVGRINNDNA-DVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKIL- 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 365983922 471 aHSKGEKwFGVDFETENIGDNFSKFVWEPALVKINALQSATEATNLILSVDETITNQEHQSAnAGMMPPAP 541
Cdd:PRK12852 471 -ENKSET-FGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDA-APAMPAGG 538
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
41-540 |
2.03e-12 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 69.77 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 41 KPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHP----AARTLVDISRAQDAEVGDGTTSVTILAGELMKEAKPFL 116
Cdd:PRK12851 28 KVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAIVREGAKAV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 117 EEGISSHIIMKGYRTAVRLAVEKIKELATDVsvehEGSRELLERCARTAMSSKLIYKN-ADFFVKMCVDAVLSLDKDdld 195
Cdd:PRK12851 108 AAGANPMDLKRGIDRAVAAVVEELKANARPV----TTNAEIAQVATISANGDAEIGRLvAEAMEKVGNEGVITVEES--- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 196 dkligikKIPGGAMEesmFIDGVAFKKTFSYAGF----EQQPKNFKNPKILSlnVELELKAEKDNAEVrVEQV--SDYQA 269
Cdd:PRK12851 181 -------KTAETELE---VVEGMQFDRGYLSPYFvtdaDKMEAELEDPYILI--HEKKISNLQDLLPV-LEAVvqSGKPL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 270 IVDAE-------WQIILDKLEqikdTGANIVLSKLP-IGDLATQYFADRNIFCAGRVSSDDmnrviqaVGGSIQSTTSDI 341
Cdd:PRK12851 248 LIIAEdvegealATLVVNKLR----GGLKVAAVKAPgFGDRRKAMLEDIAILTGGTVISED-------LGIKLENVTLEQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 342 kpdyLGTCetfEEIQIGAERYNLFKGCPQAKTctllLRGGAEQVIAEVERS----------------------------- 392
Cdd:PRK12851 317 ----LGRA---KKVVVEKENTTIIDGAGSKTE----IEGRVAQIRAQIEETtsdydreklqerlaklaggvavirvgast 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 393 ----------LHDAIMIVKRALQNKlVVAGGGAIEMEISKYLrDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAV 462
Cdd:PRK12851 386 evevkekkdrVDDALHATRAAVEEG-IVPGGGVALLRAVKAL-DKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGS 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 365983922 463 ELLNKLRlahsKGEKWFGVDFETENIGDNFSKFVWEPALVKINALQSATEATNLILSVDETITNQEHQSANAGMMPPA 540
Cdd:PRK12851 464 VVVGKLR----EKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAPPAPPGG 537
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
38-525 |
1.33e-11 |
|
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: 67.10 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 38 ETLKPTLGPLGSDILIVTSNQKTTISNDGATILR---LLDVVHPAARTLV-DISRAQDAEVGDGTTSVTILAGELMKEAK 113
Cdd:cd03344 22 DAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKeieLEDPFENMGAQLVkEVASKTNDVAGDGTTTATVLARAIIKEGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 114 PFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVSveheGSRELlercARTAMSS--------KLIyknADFFVKMCVDA 185
Cdd:cd03344 102 KAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVK----TKEEI----AQVATISangdeeigELI---AEAMEKVGKDG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 186 VLSLDKddlddkligikkipGGAMEESM-FIDGVAFKKTFSYAGFEQQPKN----FKNPKILSlnVELELKAEKDNAEVR 260
Cdd:cd03344 171 VITVEE--------------GKTLETELeVVEGMQFDRGYLSPYFVTDPEKmeveLENPYILL--TDKKISSIQELLPIL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 261 vEQVSDYQA---IV------DAEWQIILDKLEqikdTGANIVLSKLP-IGDLATQYFADRNIFCAGRVSSDDmnrviqaV 330
Cdd:cd03344 235 -ELVAKAGRpllIIaedvegEALATLVVNKLR----GGLKVCAVKAPgFGDRRKAMLEDIAILTGGTVISEE-------L 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 331 GGSIqsttSDIKPDYLGTCetfEEIQIGAERynlfkgcpqaktcTLLLRGG---------AEQVIAEVERS--------- 392
Cdd:cd03344 303 GLKL----EDVTLEDLGRA---KKVVVTKDD-------------TTIIGGAgdkaaikarIAQIRKQIEETtsdydkekl 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 393 ------------------------------LHDAIMIVKRALQNKlVVAGGGAIEMEISKYLrDYSKTIAGKQQLIINAF 442
Cdd:cd03344 363 qerlaklsggvavikvggatevelkekkdrVEDALNATRAAVEEG-IVPGGGVALLRASPAL-DKLKALNGDEKLGIEIV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 443 AKALEVIPRQLCENAGFDAVELLNKLrLAHSKGekwFGVDFETENIGDNFSKFVWEPALVKINALQSATEATNLILSVDE 522
Cdd:cd03344 441 RRALEAPLRQIAENAGVDGSVVVEKV-LESPDG---FGYDAATGEYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEA 516
|
...
gi 365983922 523 TIT 525
Cdd:cd03344 517 LVV 519
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
36-541 |
1.38e-10 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 63.90 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 36 IQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDV----VHPAARTLVDI-SRAQDAeVGDGTTSVTILAGELMK 110
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVaSKSADA-AGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 111 EAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVSveheGSRELLERCARTAMSSKLIYKN-ADFFVKMCVDAVLSL 189
Cdd:PRK14104 102 EGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVT----SNDEIAQVGTISANGDAEIGKFlADAMKKVGNEGVITV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 190 DKDDLDDKLIGIkkipggameesmfIDGVAFKKTFSYAGFEQQPKNFK-----------NPKILSLNVELEL-KAEKDNA 257
Cdd:PRK14104 178 EEAKSLETELDV-------------VEGMQFDRGYISPYFVTNADKMRvemddayilinEKKLSSLNELLPLlEAVVQTG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 258 EVRVEQVSDYQAivDAEWQIILDKLEqikdTGANIVLSKLP-IGDLATQYFADRNIFCAGRVSSDDM-----NRVIQAVG 331
Cdd:PRK14104 245 KPLVIVAEDVEG--EALATLVVNRLR----GGLKVAAVKAPgFGDRRKAMLQDIAILTGGQAISEDLgikleNVTLQMLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 332 GSI------QSTT--------SDIKPDYLGTCETFEEIQIGAERYNLFKGCPQAKTCTLLLR-GGAEQVIAEVERSLHDA 396
Cdd:PRK14104 319 RAKkvmidkENTTivngagkkADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRvGGATEVEVKERKDRVDD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 397 IMIVKRALQNKLVVAGGGAIEMEISKYLRDYsKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRlahSKGE 476
Cdd:PRK14104 399 AMHATRAAVEEGIVPGGGVALLRASEQLKGI-KTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKIL---EKEQ 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 365983922 477 KWFGVDFETENIGDNFSKFVWEPALVKINALQSATEATNLILSVDETITNQEHQSANAGMMPPAP 541
Cdd:PRK14104 475 YSYGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGGAGPAMPPGG 539
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
41-541 |
4.27e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 62.04 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 41 KPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHP----AARTLVDISRAQDAEVGDGTTSVTILAGELMKEAKPFL 116
Cdd:PRK12850 28 KVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVREGAKLV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 117 EEGISSHIIMKGYRTAVRLAVEKIKELATDVsvehEGSRELlercARTAMssklIYKNADFFV-KMCVDAVlsldKDDLD 195
Cdd:PRK12850 108 AAGMNPMDLKRGIDLAVAAVVDELKKIAKKV----TSSKEI----AQVAT----ISANGDESIgEMIAEAM----DKVGK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 196 DKLIGIKKIPGGAMEESMfIDGVAFKKTFSYAGF----EQQPKNFKNPKILSLNVELelkaekdnaevrveqvsdyqaiv 271
Cdd:PRK12850 172 EGVITVEEAKTLGTELDV-VEGMQFDRGYLSPYFvtnpEKMRAELEDPYILLHEKKI----------------------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 272 dAEWQIILDKLEQIKDTG---------------ANIVLSKL-----------P-IGDLATQYFADRNIFCAGRVSSDDM- 323
Cdd:PRK12850 228 -SNLQDLLPILEAVVQSGrplliiaedvegealATLVVNKLrgglksvavkaPgFGDRRKAMLEDIAVLTGGQVISEDLg 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 324 --------------NRVI------QAVGGS-----IQSTTSDIKPDylgtcetFEEIQIGAERYNLfkgcpQAKTCTL-- 376
Cdd:PRK12850 307 iklenvtldmlgraKRVLitkentTIIDGAgdkknIEARVKQIRAQ-------IEETTSDYDREKL-----QERLAKLag 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 377 ---LLR-GGAEQV-IAEVERSLHDAIMIVKRALQNKlVVAGGGAIEMEISKYLRDYsKTIAGKQQLIINAFAKALEVIPR 451
Cdd:PRK12850 375 gvaVIRvGGATEVeVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRARSALRGL-KGANADETAGIDIVRRALEEPLR 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 452 QLCENAGFDAVELLNKLRlahsKGEKWFGVDFETENIGDNFSKFVWEPALVKINALQSATEATNLILSVDETITnQEHQS 531
Cdd:PRK12850 453 QIATNAGFEGSVVVGKVA----ELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVA-EAPKK 527
|
570
....*....|
gi 365983922 532 ANAGMMPPAP 541
Cdd:PRK12850 528 AAAAAAGPGP 537
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
35-526 |
3.77e-09 |
|
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: 59.23 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 35 AIQETLKPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHP----AARTLVDI-SRAQDAeVGDGTTSVTILAGELM 109
Cdd:TIGR02348 20 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVaSKTNDV-AGDGTTTATVLAQAIV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 110 KEAKPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVsvehEGSRELLERCARTAMSS----KLIyknADFFVKMCVDA 185
Cdd:TIGR02348 99 KEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPV----KGKKEIAQVATISANNDeeigSLI---AEAMEKVGKDG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 186 VLSLDKDDlddkligikkipgGAMEESMFIDGVAFKKTFSYAGF----EQQPKNFKNPKILSlnVELELKAEKDNAEV-- 259
Cdd:TIGR02348 172 VITVEESK-------------SLETELEVVEGMQFDRGYISPYFvtdaEKMEVELENPYILI--TDKKISNIKDLLPLle 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 260 RVEQVSDYQAI----VDAEWQ--IILDKLEQIkdtgANIVLSKLP-IGDLATQYFADRNIFCAGRVSSDDM--------- 323
Cdd:TIGR02348 237 KVAQSGKPLLIiaedVEGEALatLVVNKLRGT----LNVCAVKAPgFGDRRKAMLEDIAILTGGQVISEELglkleevtl 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 324 --------------NRVIQAVGG---SIQSTTSDIKPDYLGTCETF--EEIQigaERYnlfkgcpqAKtctllLRGGAeQ 384
Cdd:TIGR02348 313 ddlgkakkvtvdkdNTTIVEGAGdkaAIKARVAQIKAQIEETTSDYdrEKLQ---ERL--------AK-----LAGGV-A 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 385 VI-----AEVERS-----LHDAIMIVKRALQNKlVVAGGGAIEMEISKYLRDYsKTIAGKQQLIINAFAKALEVIPRQLC 454
Cdd:TIGR02348 376 VIkvgaaTETEMKekklrIEDALNATRAAVEEG-IVPGGGVALLRAAAALEGL-KGDGEDEAIGIDIVKRALEAPLRQIA 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 365983922 455 ENAGFDAVELLNKLRlaHSKGEkwFGVDFETENIGDNFSKFVWEPALVKINALQSATEATNLILSVDETITN 526
Cdd:TIGR02348 454 ENAGLDGAVVAEKVK--ELKGN--FGFNAATGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVAD 521
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
41-541 |
1.07e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 54.43 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 41 KPTLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHP----AARTLVDISRAQDAEVGDGTTSVTILAGELMKEAKPFL 116
Cdd:PRK12849 27 KVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQALVQEGLKNV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 117 EEGISSHIIMKGYRTAVRLAVEKIKELATDVSveheGSRELlercARTAMSS--------KLIyknADFFVKMCVDAVLS 188
Cdd:PRK12849 107 AAGANPMDLKRGIDKAVEAVVEELKALARPVS----GSEEI----AQVATISangdeeigELI---AEAMEKVGKDGVIT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 189 LDKddlddkligikkipGGAME-ESMFIDGVAFKKTFSYAGF----EQQPKNFKNPKILSLNvelelkaekdnaevrvEQ 263
Cdd:PRK12849 176 VEE--------------SKTLEtELEVTEGMQFDRGYLSPYFvtdpERMEAVLEDPLILLTD----------------KK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 264 VSDYQAIVDAewqiildkLEQIKDTG---------------ANIVLSK----LPIGDLATQYFADRN--------IFCAG 316
Cdd:PRK12849 226 ISSLQDLLPL--------LEKVAQSGkplliiaedvegealATLVVNKlrggLKVAAVKAPGFGDRRkamlediaILTGG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 317 RVSSDDmnrviqaVGGSIQSTTsdikPDYLGTCetfEEIQIGAERynlfkgcpqaktcTLLLRGGA---------EQVIA 387
Cdd:PRK12849 298 TVISED-------LGLKLEEVT----LDDLGRA---KRVTITKDN-------------TTIVDGAGdkeaiearvAQIRR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 388 EVERS---------------------------------------LHDAIMIVKRALQNKlVVAGGGAIEMEISKYLRDYs 428
Cdd:PRK12849 351 QIEETtsdydreklqerlaklaggvavikvgaatevelkerkdrVEDALNATRAAVEEG-IVPGGGVALLRAAKALDEL- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 429 KTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRlahsKGEKWFGVDFETENIGDNFSKFVWEPALVKINALQ 508
Cdd:PRK12849 429 AGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVL----ELEDGFGFNAATGEYGDLIAAGIIDPVKVTRSALQ 504
|
570 580 590
....*....|....*....|....*....|...
gi 365983922 509 SATEATNLILSVDETITNQEHQSANAGMMPPAP 541
Cdd:PRK12849 505 NAASVAGLLLTTEALVADKPEEEDPPGGMGGMG 537
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
409-539 |
2.57e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 53.20 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 409 VVAGGGAIEMEISKYLrDYSKTIAGKQQLIINAFAKALEVIPRQLCENAGFDAVELLNKLRLAHSKGekwFGVDFETENI 488
Cdd:PRK00013 410 IVPGGGVALLRAAPAL-EALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKG---YGYNAATGEY 485
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 365983922 489 GDNFSKFVWEPALVKINALQSATEATNLILSVDETITNQEHQSANAGMMPP 539
Cdd:PRK00013 486 VDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAAAPPMGG 536
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
38-148 |
5.62e-05 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 45.88 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 38 ETLKPTLGPLGSDILIVTSNQKTTISNDGATILR---LLDVVHPAARTLVD--ISRAQDAeVGDGTTSVTILAGELMKEA 112
Cdd:PRK00013 24 DAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKeieLEDPFENMGAQLVKevASKTNDV-AGDGTTTATVLAQAIVREG 102
|
90 100 110
....*....|....*....|....*....|....*.
gi 365983922 113 KPFLEEGISSHIIMKGYRTAVRLAVEKIKELATDVS 148
Cdd:PRK00013 103 LKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVE 138
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
43-536 |
1.02e-04 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 44.92 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 43 TLGPLGSDILIVTSNQKTTISNDGATILRLLDVVHPAARTLVDISRAQDAEV----GDGTTSVTILAGELMKEAKPFLEE 118
Cdd:PLN03167 85 TLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAAKTndlaGDGTTTSVVLAQGLIAEGVKVVAA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 119 GISSHIIMKGYRTAVRLAVEKIKELATDVsvehEGSrELLERCARTAmsskliyKNADFFVKMCVDAVlsldkddlddKL 198
Cdd:PLN03167 165 GANPVQITRGIEKTAKALVKELKKMSKEV----EDS-ELADVAAVSA-------GNNYEVGNMIAEAM----------SK 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 199 IGIKKI----PGGAMEESMF-IDGVAFKKTFSYAGF----EQQPKNFKNPKILSlnVELELKAEKDNAEVRVEQVSDYQA 269
Cdd:PLN03167 223 VGRKGVvtleEGKSAENNLYvVEGMQFDRGYISPYFvtdsEKMSVEYDNCKLLL--VDKKITNARDLIGILEDAIRGGYP 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 270 IVdaewqIILDKLEQikDTGANIVLSKLP------------IGDLATQYFADRNIFCAGRVSSDDMNRVIQAVGGSIQST 337
Cdd:PLN03167 301 LL-----IIAEDIEQ--EALATLVVNKLRgslkiaalkapgFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 338 TSDI-----KPDYLGTCETFEEIQIG-AERYNLFKGCPQAKTCTLL------LRGGAE--QVIAEVERSL-------HDA 396
Cdd:PLN03167 374 AAKVvltkdTTTIVGDGSTQEAVNKRvAQIKNLIEAAEQDYEKEKLneriakLSGGVAviQVGAQTETELkekklrvEDA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365983922 397 IMIVKRALQNKLVVAGGGAIemeiskyLRDYSKTIAGKQQLIINAFAKALEVIPRQLC-------ENAGFDAVELLNKLr 469
Cdd:PLN03167 454 LNATKAAVEEGIVVGGGCTL-------LRLASKVDAIKDTLENDEQKVGADIVKRALSyplkliaKNAGVNGSVVSEKV- 525
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 365983922 470 LAHSKGEkwFGVDFETENIGDNFSKFVWEPALVKINALQSATEATNLILSVDETITN-QEHQSANAGM 536
Cdd:PLN03167 526 LSNDNPK--FGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEiKEPEPVPAGN 591
|
|
| |
