|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
15-514 |
0e+00 |
|
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: 1053.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 15 SHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGA 94
Cdd:cd03339 27 SHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 95 LLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLT 174
Cdd:cd03339 107 LLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPDNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAVLS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 175 VADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYK 254
Cdd:cd03339 187 VADLERKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIAILTCPFEPPKPKTKHKLDITSVEDYK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 255 ALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGF 334
Cdd:cd03339 267 KLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFEDLSPEKLGK 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 335 AGLVQEISFGTTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQ 414
Cdd:cd03339 347 AGLVREISFGTTKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGGGAAEISCSLAVEK 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 415 EADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGTNDMKQQHVIETLIGKKQ 494
Cdd:cd03339 427 AADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNPHLGIDCLGRGTNDMKEQKVFETLISKKQ 506
|
490 500
....*....|....*....|
gi 807066360 495 QISLATQMVRMILKIDDIRK 514
Cdd:cd03339 507 QILLATQVVKMILKIDDVIV 526
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
15-516 |
0e+00 |
|
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: 959.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 15 SHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGA 94
Cdd:TIGR02343 31 SNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVVVLAGA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 95 LLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLT 174
Cdd:TIGR02343 111 LLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREPLIQAAKTSLGSKIVSKCHRRFAEIAVDAVLN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 175 VADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYK 254
Cdd:TIGR02343 191 VADMERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAILTCPFEPPKPKTKHKLDISSVEEYK 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 255 ALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGF 334
Cdd:TIGR02343 271 KLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPRFQELSKDKLGK 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 335 AGLVQEISFGTTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQ 414
Cdd:TIGR02343 351 AGLVREISFGTTKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGGGAAEISCSLAVSQ 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 415 EADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGTNDMKQQHVIETLIGKKQ 494
Cdd:TIGR02343 431 EADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNLGVDCLGYGTNDMKEQFVFETLIGKKQ 510
|
490 500
....*....|....*....|..
gi 807066360 495 QISLATQMVRMILKIDDIRKPG 516
Cdd:TIGR02343 511 QILLATQLVRMILKIDDVISPG 532
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
15-512 |
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: 591.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 15 SHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGA 94
Cdd:cd00309 12 SNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDGTTTVVVLAGE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 95 LLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLT 174
Cdd:cd00309 92 LLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVP--IDVEDREELLKVATTSLNSKLVSGGDDFLGELVVDAVLK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 175 VADMErRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPpkpktkhkldvtsvedyk 254
Cdd:cd00309 170 VGKEN-GDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY------------------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 255 alqkyekekfeemiqqiketganLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGF 334
Cdd:cd00309 231 -----------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLEDLTPEDLGT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 335 AGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQ 414
Cdd:cd00309 288 AGLVEETKIG--DEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGAAEIELSKALEE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 415 EADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAlGIDCLHKGTNDMKQQHVIETLIGKKQ 494
Cdd:cd00309 366 LAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNA-GGDVETGEIVDMKEAGIIDPLKVKRQ 444
|
490
....*....|....*...
gi 807066360 495 QISLATQMVRMILKIDDI 512
Cdd:cd00309 445 ALKSATEAASLILTIDDI 462
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
23-512 |
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: 560.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 23 VANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQL 102
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 103 LDRGIHPIRIADGYEQAARVAIEHLDKIsDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVADMERrD 182
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSI-ISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDG-S 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 183 VDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKE 262
Cdd:pfam00118 159 FDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 263 KFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGLVQEIS 342
Cdd:pfam00118 239 QILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 343 FGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTL 422
Cdd:pfam00118 319 IG--DEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 423 EQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEmNPALGIDCLHKGTNDMKQQHVIETLIGKKQQISLATQM 502
Cdd:pfam00118 397 EQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASG-EKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEA 475
|
490
....*....|
gi 807066360 503 VRMILKIDDI 512
Cdd:pfam00118 476 ASTILRIDDI 485
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
15-512 |
0e+00 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 541.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 15 SHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGA 94
Cdd:NF041082 21 NNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 95 LLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKIsdSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLT 174
Cdd:NF041082 101 LLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEI--AIKVDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVKA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 175 VADME-RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDY 253
Cdd:NF041082 179 VAEKDgGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDAKISITDPDQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 254 KALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLG 333
Cdd:NF041082 259 QAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSIDDLSPEDLG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 334 FAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVS 413
Cdd:NF041082 339 YAGLVEERKVG--GDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEVELALRLR 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 414 QEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAlGIDCLHKGTNDMKQQHVIETLIGKK 493
Cdd:NF041082 417 EYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTA-GLDVYTGKVVDMLEIGVVEPLRVKT 495
|
490
....*....|....*....
gi 807066360 494 QQISLATQMVRMILKIDDI 512
Cdd:NF041082 496 QAIKSATEAAVMILRIDDV 514
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
15-512 |
0e+00 |
|
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: 526.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 15 SHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGA 94
Cdd:cd03343 19 MNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 95 LLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLT 174
Cdd:cd03343 99 LLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIK--VDPDDKDTLRKIAKTSLTGKGAEAAKDKLADLVVDAVLQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 175 VADME--RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVED 252
Cdd:cd03343 177 VAEKRdgKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAKIRITSPDQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 253 YKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKL 332
Cdd:cd03343 257 LQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTNIDDLTPEDL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 333 GFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAV 412
Cdd:cd03343 337 GEAELVEERKVG--DDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGAVEIELAKRL 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 413 SQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAlGIDCLHKGTNDMKQQHVIETLIGK 492
Cdd:cd03343 415 REYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNA-GLDVYTGEVVDMLEKGVIEPLRVK 493
|
490 500
....*....|....*....|
gi 807066360 493 KQQISLATQMVRMILKIDDI 512
Cdd:cd03343 494 KQAIKSATEAATMILRIDDV 513
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
17-512 |
0e+00 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 526.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 17 IMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALL 96
Cdd:NF041083 23 IMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAVVLAGELL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 97 EEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVA 176
Cdd:NF041083 103 KKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEK--VDPDDRETLKKIAETSLTSKGVEEARDYLAEIAVKAVKQVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 177 dmERRD----VDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVED 252
Cdd:NF041083 181 --EKRDgkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAEIRITDPDQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 253 YKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKL 332
Cdd:NF041083 259 LQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVTNIDDLTPEDL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 333 GFAGLVQEISFGTtkDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAV 412
Cdd:NF041083 339 GYAELVEERKVGD--DKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGAPEVELAKRL 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 413 SQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEmNPALGIDCLHKGTNDMKQQHVIETLIGK 492
Cdd:NF041083 417 REYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKG-KKWAGINVFTGEVVDMWELGVIEPLRVK 495
|
490 500
....*....|....*....|
gi 807066360 493 KQQISLATQMVRMILKIDDI 512
Cdd:NF041083 496 TQAIKSATEAATMILRIDDV 515
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
15-512 |
3.59e-172 |
|
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: 495.74 E-value: 3.59e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 15 SHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGA 94
Cdd:TIGR02339 20 NNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 95 LLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlVDIKDTEPLIQTAKTTLGSKVVNSCHRQ-MAEIAVNAVL 173
Cdd:TIGR02339 100 LLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATK--ISPEDRDLLKKIAYTSLTSKASAEVAKDkLADLVVEAVK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 174 TVADME---RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSV 250
Cdd:TIGR02339 178 QVAELRgdgKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAPLEVEKTEIDAKIRITDP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 251 EDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAE 330
Cdd:TIGR02339 258 DQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVSSIDEITES 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 331 KLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCAL 410
Cdd:TIGR02339 338 DLGYAELVEERKVG--EDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVAGGGAVEIELAL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 411 AVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEmNPALGIDCLHKGTNDMKQQHVIETLI 490
Cdd:TIGR02339 416 RLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKG-NKNAGINVFTGEIEDMLELGVIEPLR 494
|
490 500
....*....|....*....|..
gi 807066360 491 GKKQQISLATQMVRMILKIDDI 512
Cdd:TIGR02339 495 VKEQAIKSATEAATMILRIDDV 516
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
14-512 |
1.13e-153 |
|
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: 448.66 E-value: 1.13e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 14 VSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAG 93
Cdd:cd03338 11 LSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 94 ALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKIsdSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVL 173
Cdd:cd03338 91 ALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSM--SIPVDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 174 TVADMER-RDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSH-PQMPKKVEDAKIAILTCPFEPPKPKTKHKLdvtSVE 251
Cdd:cd03338 169 KVIDPATaTNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDMDNNI---VVN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 252 DYKA---LQKYEKEKFEEMIQQIKETGANLAICQW-----GFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPR 323
Cdd:cd03338 246 DYAQmdrILREERKYILNMCKKIKKSGCNVLLIQKsilrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVAS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 324 FSELTAEKLGFAGLVQEISFGTtkDKMLVIEQCKNS-RAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGG 402
Cdd:cd03338 326 IDHFTEDKLGSADLVEEVSLGD--GKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 403 AAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVK-EMNpaLGIDCLHKGTNDMK 481
Cdd:cd03338 404 APEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQgEKN--AGINVRKGAITNIL 481
|
490 500 510
....*....|....*....|....*....|.
gi 807066360 482 QQHVIETLIGKKQQISLATQMVRMILKIDDI 512
Cdd:cd03338 482 EENVVQPLLVSTSAITLATETVRMILKIDDI 512
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
15-512 |
6.76e-141 |
|
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: 416.11 E-value: 6.76e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 15 SHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGA 94
Cdd:TIGR02342 13 SNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 95 LLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLT 174
Cdd:TIGR02342 93 LLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIP--VDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVLK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 175 VADMER-RDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQ-MPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVED 252
Cdd:TIGR02342 171 VIDPENaKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDYAQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 253 YKALQKYEKEKFEEMIQQIKETGANLAICQW-----GFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSEL 327
Cdd:TIGR02342 251 MDRVLKEERAYILNIVKKIKKTGCNVLLIQKsilrdAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASIDHF 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 328 TAEKLGFAGLVQEIsfGTTKDKMLVIEQCKN-SRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEI 406
Cdd:TIGR02342 331 TADKLGSAELVEEV--DSDGGKIIKITGIQNaGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPEI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 407 SCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVK-EMNpaLGIDCLHKGTNDMKQQHV 485
Cdd:TIGR02342 409 EIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANgEKT--AGISVRKGGITNMLEEHV 486
|
490 500
....*....|....*....|....*..
gi 807066360 486 IETLIGKKQQISLATQMVRMILKIDDI 512
Cdd:TIGR02342 487 LQPLLVTTSAITLASETVRSILKIDDI 513
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
17-512 |
3.29e-125 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 375.19 E-value: 3.29e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 17 IMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLA 92
Cdd:COG0459 16 IRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFenmgAQLVKEVASKTNDEAGDGTTTATVLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 93 GALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdsvlVDIKDTEPLIQTAKTTLGSKvvnschRQMAEIAVNAV 172
Cdd:COG0459 96 GALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIA----KPVDDKEELAQVATISANGD------EEIGELIAEAM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 173 LTVADMERrdvdfelIKVEgKVGGRLEDTKLIKGVIVDKDFSHPQ-------MPKKVEDAKIAILTCPFEPPKPktkhkl 245
Cdd:COG0459 166 EKVGKDGV-------ITVE-EGKGLETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDKKISSIQD------ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 246 dvtsvedykalqkyekekFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVR---WVGGP--------EIELIAI 314
Cdd:COG0459 232 ------------------LLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLrvvAVKAPgfgdrrkaMLEDIAI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 315 ATGGRIV-----PRFSELTAEKLGFAGLVQEisfgtTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIR 389
Cdd:COG0459 294 LTGGRVIsedlgLKLEDVTLDDLGRAKRVEV-----DKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALHATR 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 390 NLIRDnRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvkemNPALG 469
Cdd:COG0459 369 AAVEE-GIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAK----DKGFG 443
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 807066360 470 IDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDI 512
Cdd:COG0459 444 FDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAV 486
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
10-512 |
1.09e-124 |
|
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: 373.17 E-value: 1.09e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 10 EKLSVSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVV 89
Cdd:cd03337 15 RKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 90 VLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAV 169
Cdd:cd03337 95 ILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIP--VDVNDRAQMLKIIKSCIGTKFVSRWSDLMCNLAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 170 NAVLTVA---DMERRDVDFE-LIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEppkpktkhkl 245
Cdd:cd03337 173 DAVKTVAveeNGRKKEIDIKrYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPLE---------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 246 dvtsvedYkalqkyekekfeemiqqiketganLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFS 325
Cdd:cd03337 243 -------Y------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARACGATIVNRPE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 326 ELTAEKLGFAGLVQEISFGtTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAE 405
Cdd:cd03337 292 ELTESDVGTGAGLFEVKKI-GDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILNPKLVPGGGATE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 406 ISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGTNDMKQQHV 485
Cdd:cd03337 371 MAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTWGIDGETGDIVDMKELGI 450
|
490 500
....*....|....*....|....*..
gi 807066360 486 IETLIGKKQQISLATQMVRMILKIDDI 512
Cdd:cd03337 451 WDPLAVKAQTYKTAIEAACMLLRIDDI 477
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
11-512 |
5.19e-119 |
|
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: 360.21 E-value: 5.19e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 11 KLSVSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVV 90
Cdd:TIGR02344 16 KAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVII 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 91 LAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKIsdSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVN 170
Cdd:TIGR02344 96 LAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEI--SIPVDVNDDAAMLKLIQSCIGTKFVSRWSDLMCDLALD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 171 AVLTVA--DMERRDVDFE-LIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDV 247
Cdd:TIGR02344 174 AVRTVQrdENGRKEIDIKrYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLEYKKGESQTNIEI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 248 TSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSEL 327
Cdd:TIGR02344 254 TKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACGATIVNRPEEL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 328 TAEKLGF-AGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEI 406
Cdd:TIGR02344 334 RESDVGTgCGLFEVKKIG--DEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKLVPGGGATEM 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 407 SCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGTNDMKQQHVI 486
Cdd:TIGR02344 412 AVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTWGIDGETGKIVDMKEKGIW 491
|
490 500
....*....|....*....|....*.
gi 807066360 487 ETLIGKKQQISLATQMVRMILKIDDI 512
Cdd:TIGR02344 492 EPLAVKLQTYKTAIESACLLLRIDDI 517
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
15-514 |
3.74e-112 |
|
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: 342.39 E-value: 3.74e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 15 SHIMAAKAVANTMRTSLGPNGLDKMM--VDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLA 92
Cdd:cd03336 17 SSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDGTTSVTVLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 93 GALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKDT-EPLIQTAKTTLGSKVVNSCHRQMAEIAVNA 171
Cdd:cd03336 97 AELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEAFrEDLLNIARTTLSSKILTQDKEHFAELAVDA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 172 VLTVADmerrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKKVEDAKIAILTCPFEPPKPKT-KHKLDVTSV 250
Cdd:cd03336 177 VLRLKG----SGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTPMDTDKIKIfGAKVRVDST 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 251 EDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAE 330
Cdd:cd03336 252 AKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTGGEIASTFDHPELV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 331 KLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCAL 410
Cdd:cd03336 332 KLGTCKLIEEIMIG--EDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRVVLGGGCSEMLMAK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 411 AVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAlGIDCLHKGTNDMKQQHVIETLI 490
Cdd:cd03336 410 AVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTA-GLDMRKGTVGDMKELGITESFK 488
|
490 500
....*....|....*....|....
gi 807066360 491 GKKQQISLATQMVRMILKIDDIRK 514
Cdd:cd03336 489 VKRQVLLSASEAAEMILRVDDIIK 512
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
15-512 |
7.09e-111 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 339.70 E-value: 7.09e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 15 SHIMAAKAVANTMRTSLGPNGLDKMMV-----DKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVV 89
Cdd:PTZ00212 26 QSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGDGTTSVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 90 VLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKD-TEPLIQTAKTTLGSKVVNSCHRQMAEIA 168
Cdd:PTZ00212 106 VLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEKfKEDLLNIARTTLSSKLLTVEKDHFAKLA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 169 VNAVLTVadmeRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKKVEDAKIAILTCPFEPPKPKT-KHKLDV 247
Cdd:PTZ00212 186 VDAVLRL----KGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVGQ-PKRLENCKILVANTPMDTDKIKIyGAKVKV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 248 TSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSEL 327
Cdd:PTZ00212 261 DSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 328 TAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEIS 407
Cdd:PTZ00212 341 EKVKLGHCDLIEEIMIG--EDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKDTRVVLGGGCSEML 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 408 CALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAlGIDCLHKGTNDMKQQHVIE 487
Cdd:PTZ00212 419 MANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTA-GIDMEKGTVGDMKELGITE 497
|
490 500
....*....|....*....|....*
gi 807066360 488 TLIGKKQQISLATQMVRMILKIDDI 512
Cdd:PTZ00212 498 SYKVKLSQLCSATEAAEMILRVDDI 522
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
14-510 |
3.45e-109 |
|
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: 335.03 E-value: 3.45e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 14 VSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAG 93
Cdd:cd03340 19 ISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 94 ALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKIsdSVLVDIKDTEP----LIQTAKTTLGSKVVNSCHRQMAEIAV 169
Cdd:cd03340 99 EFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEI--AVNIDKEDKEEqrelLEKCAATALNSKLIASEKEFFAKMVV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 170 NAVLTVADmerrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFS---HPQMPKKVEDAKIAILTCPFEPPKPKTKHKLD 246
Cdd:cd03340 177 DAVLSLDD----DLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSyagFEQQPKKFKNPKILLLNVELELKAEKDNAEVR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 247 VTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSE 326
Cdd:cd03340 253 VEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQTTVSN 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 327 LTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEI 406
Cdd:cd03340 333 ITDDVLGTCGLFEERQVG--GERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAIEM 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 407 SCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGTNDMKQQHVI 486
Cdd:cd03340 411 ELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKWYGVDINNEGIADNFEAFVW 490
|
490 500
....*....|....*....|....
gi 807066360 487 ETLIGKKQQISLATQMVRMILKID 510
Cdd:cd03340 491 EPSLVKINALTAATEAACLILSVD 514
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
17-514 |
3.91e-105 |
|
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: 324.62 E-value: 3.91e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 17 IMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALL 96
Cdd:cd03335 14 VTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAELL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 97 EEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKiSDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVA 176
Cdd:cd03335 94 KRANELVKQKIHPTTIISGYRLACKEAVKYIKE-HLSISVDNLGKESLINVAKTSMSSKIIGADSDFFANMVVDAILAVK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 177 DM-ERRDV-----DFELIKVEGKvggRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEppkpKTKHKLDV--- 247
Cdd:cd03335 173 TTnEKGKTkypikAVNILKAHGK---SAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQ----KTKMKLGVqvv 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 248 -TSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSE 326
Cdd:cd03335 246 vTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVSTLAN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 327 LTAE------KLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYG 400
Cdd:cd03335 326 LEGEetfdpsYLGEAEEVVQERIG--DDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 401 GGAAEisCALAVSQE--ADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPA-------LGID 471
Cdd:cd03335 404 GGAVE--TALSIYLEnfATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKPdkkhlkwYGLD 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 807066360 472 cLHKGT-NDMKQQHVIETLIGKKQQISLATQMVRMILKIDDIRK 514
Cdd:cd03335 482 -LINGKvRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
14-516 |
7.07e-104 |
|
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: 321.32 E-value: 7.07e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 14 VSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAG 93
Cdd:TIGR02345 21 ISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 94 ALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSV-LVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAV 172
Cdd:TIGR02345 101 ELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIdEEKGEQRELLEKCAATALSSKLISHNKEFFSKMIVDAV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 173 LTvadMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFS---HPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTS 249
Cdd:TIGR02345 181 LS---LDRDDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSyagFEQQPKKFANPKILLLNVELELKAEKDNAEIRVED 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 250 VEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTA 329
Cdd:TIGR02345 258 VEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTTSDLEA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 330 EKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCA 409
Cdd:TIGR02345 338 DVLGTCALFEERQIG--SERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIEMELS 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 410 LAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEmNPALGIDCLHKGTNDMKQQHVIETL 489
Cdd:TIGR02345 416 KCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKG-GKWYGVDINTEDIGDNFEAFVWEPA 494
|
490 500
....*....|....*....|....*...
gi 807066360 490 IGKKQQISLATQMVRMILKIDD-IRKPG 516
Cdd:TIGR02345 495 LVKINALKAAFEAACTILSVDEtITNPK 522
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
17-520 |
1.28e-102 |
|
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274081 [Multi-domain] Cd Length: 536 Bit Score: 318.20 E-value: 1.28e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 17 IMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALL 96
Cdd:TIGR02340 18 VTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVIIAAELL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 97 EEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKiSDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVA 176
Cdd:TIGR02340 98 KRADELVKNKIHPTSVISGYRLACKEAVKYIKE-NLSVSVDELGREALINVAKTSMSSKIIGLDSDFFSNIVVDAVLAVK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 177 DM-ERRDVDF--ELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEppkpKTKHKLDVT-SVED 252
Cdd:TIGR02340 177 TTnENGETKYpiKAINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQ----KAKMALGVQiVVDD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 253 YKALQKYEKEKFE---EMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTA 329
Cdd:TIGR02340 253 PEKLEQIRQREADitkERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVSTLADLEG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 330 E------KLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGA 403
Cdd:TIGR02340 333 EetfeasYLGFADEVVQERIA--DDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGGA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 404 AEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEM-NPA------LGIDCLHKG 476
Cdd:TIGR02340 411 VEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAQlKPEkkhlkwYGLDLVNGK 490
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 807066360 477 TNDMKQQHVIETLIGKKQQISLATQMVRMILKIDD-IRKPGESEE 520
Cdd:TIGR02340 491 IRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDlIKLNPEQSK 535
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
17-512 |
1.51e-101 |
|
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: 313.39 E-value: 1.51e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 17 IMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALL 96
Cdd:cd03341 14 IEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGELL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 97 EEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKDTEPLIQTAKTTLGSKVV-NSCHrqMAEIAVNAVLTV 175
Cdd:cd03341 94 EKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLRNKEEVSKALKTAIASKQYgNEDF--LSPLVAEACISV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 176 ADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDfSHPQMpKKVEDAKIAILTCPFeppkpktkhkldvtsvedyka 255
Cdd:cd03341 172 LPENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKRE-PEGSV-KRVKKAKVAVFSCPF--------------------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 256 lqkyekekfeemiqqikETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFA 335
Cdd:cd03341 229 -----------------DIGVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEEIGYC 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 336 GLVQEISFGTTkdKMLVIEQCKNSRAV-TIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQ 414
Cdd:cd03341 292 DSVYVEEIGDT--KVVVFRQNKEDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAKKLKE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 415 EADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKE-MNPALGIDCLHKGTNDMKQQHVIETLIGKK 493
Cdd:cd03341 370 YGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGnKSAGVDIESGDEGTKDAKEAGIFDHLATKK 449
|
490
....*....|....*....
gi 807066360 494 QQISLATQMVRMILKIDDI 512
Cdd:cd03341 450 WAIKLATEAAVTVLRVDQI 468
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
17-512 |
9.14e-98 |
|
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274087 [Multi-domain] Cd Length: 531 Bit Score: 305.49 E-value: 9.14e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 17 IMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALL 96
Cdd:TIGR02346 24 IEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGELL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 97 EEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKDTEPLIQTAKTTLGSKVVNScHRQMAEIAVNAVLTVA 176
Cdd:TIGR02346 104 NKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDLRDKDELIKALKASISSKQYGN-EDFLAQLVAQACSTVL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 177 DMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFShpQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYKAL 256
Cdd:TIGR02346 183 PKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNREAE--GSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNAEELLNY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 257 QKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAG 336
Cdd:TIGR02346 261 SKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPEEIGYVD 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 337 LVQEISFGTtkDKMLVIEQCK-NSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQE 415
Cdd:TIGR02346 341 SVYVSEIGG--DKVTVFKQENgDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELASRLTKY 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 416 ADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKEMNPALGID--CLHKGTNDMKQQHVIETLIGKK 493
Cdd:TIGR02346 419 GEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAH-KKGNKSKGIDieAESDGVKDASEAGIYDMLATKK 497
|
490
....*....|....*....
gi 807066360 494 QQISLATQMVRMILKIDDI 512
Cdd:TIGR02346 498 WAIKLATEAAVTVLRVDQI 516
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
10-514 |
2.76e-93 |
|
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: 293.69 E-value: 2.76e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 10 EKLSVSHIMAAKAVANTMRTSLGPNGLDKMMV--DKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTG 87
Cdd:TIGR02341 13 ENARLSSFVGAIAIGDLVKSTLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEVGDGTTS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 88 VVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKIS-DSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAE 166
Cdd:TIGR02341 93 VTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAvDNGSDEVKFRQDLMNIARTTLSSKILSQHKDHFAQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 167 IAVNAVLTVadmeRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKKVEDAKIAILTCPFEPPKPKT-KHKL 245
Cdd:TIGR02341 173 LAVDAVLRL----KGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTDKVKIfGSRV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 246 DVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFS 325
Cdd:TIGR02341 248 RVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIVSTFD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 326 ELTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAE 405
Cdd:TIGR02341 328 HPELVKLGSCDLIEEIMIG--EDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGGGCSE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 406 ISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRArQVKEMNPALGIDcLHKGT-NDMKQQH 484
Cdd:TIGR02341 406 MLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRA-AHYNGNTTMGLD-MNEGTiADMRQLG 483
|
490 500 510
....*....|....*....|....*....|
gi 807066360 485 VIETLIGKKQQISLATQMVRMILKIDDIRK 514
Cdd:TIGR02341 484 ITESYKVKRAVVSSAAEAAEVILRVDNIIK 513
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
17-518 |
1.03e-84 |
|
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: 271.61 E-value: 1.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 17 IMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALL 96
Cdd:TIGR02347 22 INAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGELL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 97 EEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVA 176
Cdd:TIGR02347 102 KQAERYILEGVHPRIITEGFEIARKEALQFLDKFK-VKKEDEVDREFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 177 DMErRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYKAL 256
Cdd:TIGR02347 181 KDG-EDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQREKL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 257 QKYEKEKFEEMIQQIKE-------TGAN---LAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSE 326
Cdd:TIGR02347 260 VKAERKFVDDRVKKIIElkkkvcgKSPDkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEALNSVED 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 327 LTAEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEI 406
Cdd:TIGR02347 340 LTPECLGWAGLVYETTIG--EEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAGAFEI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 407 SCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPaLGIDcLHKGTN-DMKQQHV 485
Cdd:TIGR02347 418 AAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEV-VGVD-LNTGEPiDPEIKGI 495
|
490 500 510
....*....|....*....|....*....|...
gi 807066360 486 IETLIGKKQQISLATQMVRMILKIDDIRKPGES 518
Cdd:TIGR02347 496 WDNYRVKKQLIQSATVIASQLLLVDEVMRAGRS 528
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
17-516 |
5.47e-84 |
|
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: 268.36 E-value: 5.47e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 17 IMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALL 96
Cdd:cd03342 18 ISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGELL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 97 EEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIkDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVa 176
Cdd:cd03342 98 KQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDT-DRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAI- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 177 dmERRDVDFELIKVE-GKVGGRLE-DTKLIKGVIVDKDFSHPQMPKKVEDAkiAILTCPFeppkpktkhkldvtSVEdyk 254
Cdd:cd03342 176 --YKPDEPIDLHMVEiMQMQHKSDsDTKLIRGLVLDHGARHPDMPKRVENA--YILTCNV--------------SLE--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 255 alqkYEK-EKFEEMIQqiketgaNLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLG 333
Cdd:cd03342 235 ----YEKtEVNSGFFY-------SVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPECLG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 334 FAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVS 413
Cdd:cd03342 304 YAGLVYERTLG--EEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHLK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 414 QEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRaRQVKEMNPALGIDCLHKGTNDMKQQHVIETLIGKK 493
Cdd:cd03342 382 EFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQ-DEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKR 460
|
490 500
....*....|....*....|...
gi 807066360 494 QQISLATQMVRMILKIDDIRKPG 516
Cdd:cd03342 461 QILHSATVIASQLLLVDEIIRAG 483
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
142-394 |
1.60e-76 |
|
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: 239.68 E-value: 1.60e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 142 EPLIQTAKTTLGSKVvNSCHRQMAEIAVNAVLTVADMERrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKK 221
Cdd:cd03333 2 ELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNR-MDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 222 VEDAKIAILTCPFEPpkpktkhkldvtsvedykalqkyekekfeemiqqiketganLAICQWGFDDEANHLLLQNNLPAV 301
Cdd:cd03333 80 LENAKILLLDCPLEY-----------------------------------------VVIAEKGIDDLALHYLAKAGIMAV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 302 RWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGLVQEISFGTtkDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSL 381
Cdd:cd03333 119 RRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGE--EKLTFIEGCKGGKAATILLRGATEVELDEVKRSL 196
|
250
....*....|...
gi 807066360 382 HDALCVIRNLIRD 394
Cdd:cd03333 197 HDALCAVRAAVEE 209
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
166-392 |
1.09e-15 |
|
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. Fab1p is important for vacuole size regulation, presumably by modulating PtdIns(3,5)P2 effector activity. In the human homolog p235/PIKfyve deletion of this domain leads to loss of catalytic activity. However no exact function this domain has been defined. In general, chaperonins are involved in productive folding of proteins.
Pssm-ID: 239450 [Multi-domain] Cd Length: 261 Bit Score: 76.88 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 166 EIAVNAVLTVADMERRDVDF-------ELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPK 238
Cdd:cd03334 21 DILLPLVWKAASNVKPDVRAgddmdirQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 239 PKTKhkldVTSVEDYKAlqkYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGG 318
Cdd:cd03334 101 VENK----LLSLDPVIL---QEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807066360 319 RIVPRFSELTAE-KLGFAGLVQEISF----GTTKDKMLvIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 392
Cdd:cd03334 174 DIISSMDDLLTSpKLGTCESFRVRTYveehGRSKTLMF-FEGCPKELGCTILLRGGDLEELKKVKRVVEFMVFAAYHLK 251
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
20-486 |
2.89e-15 |
|
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: 78.27 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 20 AKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATI---LSMMD-VDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGAL 95
Cdd:cd03344 17 VNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVakeIELEDpFENMGAQLVKEVASKTNDVAGDGTTTATVLARAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 96 LEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdsvlVDIKDTEPLIQTAKT------TLGSKVVNSchrqMAEIAV 169
Cdd:cd03344 97 IKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLS----KPVKTKEEIAQVATIsangdeEIGELIAEA----MEKVGK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 170 NAVLTVADmerrdvdfelikvegkvGGRLEDT-KLIKGVIVDKDFSHPQM---PKK----VEDAKIAIltcpfeppkpkT 241
Cdd:cd03344 169 DGVITVEE-----------------GKTLETElEVVEGMQFDRGYLSPYFvtdPEKmeveLENPYILL-----------T 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 242 KHKLDvtSVEDYKALqkyekekfeemIQQIKETGANLAICQWGFDDEANHLLLQNNLP------AVRwvgGPE------- 308
Cdd:cd03344 221 DKKIS--SIQELLPI-----------LELVAKAGRPLLIIAEDVEGEALATLVVNKLRgglkvcAVK---APGfgdrrka 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 309 -IELIAIATGGRIVP-----RFSELTAEKLGFAGLVQeisfgTTKDKMLV-------------IEQCKNSRAVT------ 363
Cdd:cd03344 285 mLEDIAILTGGTVISeelglKLEDVTLEDLGRAKKVV-----VTKDDTTIiggagdkaaikarIAQIRKQIEETtsdydk 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 364 ----------------IFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNrVVYGGGAAEISCALAVSQEADKCPtLEQYAM 427
Cdd:cd03344 360 eklqerlaklsggvavIKVGGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPALDKLKALNG-DEKLGI 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 807066360 428 RAFADALEVIPMALSENSGMNPiqtmtEVRARQVKEMNPALGIDCLHKGTNDMKQQHVI 486
Cdd:cd03344 438 EIVRRALEAPLRQIAENAGVDG-----SVVVEKVLESPDGFGYDAATGEYVDMIEAGII 491
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
21-192 |
9.25e-13 |
|
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: 70.40 E-value: 9.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 21 KAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALL 96
Cdd:TIGR02348 19 DKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFenmgAQLVKEVASKTNDVAGDGTTTATVLAQAIV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 97 EEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdsvlVDIKDTEPLIQTAKTTLGS--KVVNSCHRQMAEIAVNAVLT 174
Cdd:TIGR02348 99 KEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLS----KPVKGKKEIAQVATISANNdeEIGSLIAEAMEKVGKDGVIT 174
|
170
....*....|....*...
gi 807066360 175 VAdmERRDVDFELIKVEG 192
Cdd:TIGR02348 175 VE--ESKSLETELEVVEG 190
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
22-335 |
2.19e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 66.28 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 22 AVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKL---MV-ELSKSQDDEIGDGTTGVVVLAGALLE 97
Cdd:PRK12850 22 ILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMgaqMVkEVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 98 EAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdsvlVDIKDTEPLIQTA------KTTLGSKVVnschRQMAEIAVNA 171
Cdd:PRK12850 102 EGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIA----KKVTSSKEIAQVAtisangDESIGEMIA----EAMDKVGKEG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 172 VLTVAdmERRDVDFELIKVEGKvggRLEDTKLIKGVIVDKDfshpQMPKKVEDAKIAIltcpfeppkpktkHKLDVTSVE 251
Cdd:PRK12850 174 VITVE--EAKTLGTELDVVEGM---QFDRGYLSPYFVTNPE----KMRAELEDPYILL-------------HEKKISNLQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 252 DYKALqkyekekfeemIQQIKETGANLAICQWGFDDEANHLLLQNNL------PAVRWVG-----GPEIELIAIATGGRI 320
Cdd:PRK12850 232 DLLPI-----------LEAVVQSGRPLLIIAEDVEGEALATLVVNKLrgglksVAVKAPGfgdrrKAMLEDIAVLTGGQV 300
|
330 340
....*....|....*....|
gi 807066360 321 VP-----RFSELTAEKLGFA 335
Cdd:PRK12850 301 ISedlgiKLENVTLDMLGRA 320
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
21-448 |
4.74e-11 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 64.93 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 21 KAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATIL-------SMMDVDhqiAKLMVELSKSQDDEIGDGTTGVVVLAG 93
Cdd:PTZ00114 32 ERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAkaiefsdRFENVG---AQLIRQVASKTNDKAGDGTTTATILAR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 94 ALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDsvlvDIKDTEPLIQTAKTT------LGSKVVNSchrqMAEI 167
Cdd:PTZ00114 109 AIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSR----PVKTKEDILNVATISangdveIGSLIADA----MDKV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 168 AVNAVLTVADmerrdvdfelikvegkvGGRLEDT-KLIKGVIVDKDFSHPQMPKKVEDAKIaILTCPFeppkpktkhkld 246
Cdd:PTZ00114 181 GKDGTITVED-----------------GKTLEDElEVVEGMSFDRGYISPYFVTNEKTQKV-ELENPL------------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 247 vTSVEDYKALQkyekekfeemIQQI-------KETGANLAICQWGFDDEANHLLLQNNLP------AVRWVGGPE----- 308
Cdd:PTZ00114 231 -ILVTDKKISS----------IQSIlpilehaVKNKRPLLIIAEDVEGEALQTLIINKLRgglkvcAVKAPGFGDnrkdi 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 309 IELIAIATGGRIVPR------FSELTAEKLGFAGLVQ-----EISFGTTKDKMLVIEQCKNSRA---------------- 361
Cdd:PTZ00114 300 LQDIAVLTGATVVSEdnvglkLDDFDPSMLGSAKKVTvtkdeTVILTGGGDKAEIKERVELLRSqierttseydkeklke 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 362 ---------VTIFIRGGNKMIIEEAKRSLHDALCVIRNLIrDNRVVYGGGAAEI--SCALAVSQEADKCPTLEQYAMRAF 430
Cdd:PTZ00114 380 rlaklsggvAVIKVGGASEVEVNEKKDRIEDALNATRAAV-EEGIVPGGGVALLraSKLLDKLEEDNELTPDQRTGVKIV 458
|
490
....*....|....*...
gi 807066360 431 ADALEVIPMALSENSGMN 448
Cdd:PTZ00114 459 RNALRLPTKQIAENAGVE 476
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
6-192 |
2.67e-10 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 62.63 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 6 GPTIEKLSVshimAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEI 81
Cdd:PLN03167 65 GSAIKKLQA----GVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVenigAKLVRQAAAKTNDLA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 82 GDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVlvdiKDTEpLIQTAKTTLGS--KVVNS 159
Cdd:PLN03167 141 GDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEV----EDSE-LADVAAVSAGNnyEVGNM 215
|
170 180 190
....*....|....*....|....*....|...
gi 807066360 160 CHRQMAEIAVNAVLTVAdmERRDVDFELIKVEG 192
Cdd:PLN03167 216 IAEAMSKVGRKGVVTLE--EGKSAENNLYVVEG 246
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
22-148 |
1.26e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 60.52 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 22 AVANTMRTSLGPNG----LDKmmvdKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAG 93
Cdd:PRK00013 21 KLADAVKVTLGPKGrnvvLEK----SFGAPTITKDGVTVAKEIELEDPFenmgAQLVKEVASKTNDVAGDGTTTATVLAQ 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 807066360 94 ALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdsvlVDIKDTEPLIQTA 148
Cdd:PRK00013 97 AIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKIS----KPVEDKEEIAQVA 147
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
20-192 |
2.04e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 59.76 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 20 AKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGAL 95
Cdd:PRK12851 20 VNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFenmgAQMVREVASKTNDVAGDGTTTATVLAQAI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 96 LEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLV--DIKDTEPLIQTAKTTLGSKVVNSchrqMAEIAVNAVL 173
Cdd:PRK12851 100 VREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTnaEIAQVATISANGDAEIGRLVAEA----MEKVGNEGVI 175
|
170
....*....|....*....
gi 807066360 174 TVAdmERRDVDFELIKVEG 192
Cdd:PRK12851 176 TVE--ESKTAETELEVVEG 192
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
22-346 |
2.66e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 59.44 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 22 AVANTMRTSLGPNGLDkMMVDKD-GDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALL 96
Cdd:PRK12849 21 KLADAVKVTLGPKGRN-VVIDKSfGAPTITKDGVSIAKEIELEDPFenlgAQLVKEVASKTNDVAGDGTTTATVLAQALV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 97 EEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdsvlVDIKDTEPLIQTAKT------TLGSKVVnschRQMAEIAVN 170
Cdd:PRK12849 100 QEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALA----RPVSGSEEIAQVATIsangdeEIGELIA----EAMEKVGKD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 171 AVLTVAdmERRDVDFELIKVEGkvggrledtklikgVIVDKDFSHPQM---PKK----VEDAKIAIltcpfeppkpkTKH 243
Cdd:PRK12849 172 GVITVE--ESKTLETELEVTEG--------------MQFDRGYLSPYFvtdPERmeavLEDPLILL-----------TDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 244 KLdvTSVEDYKALqkyekekfeemIQQIKETGANLAICQWGFDDEANHLLLQN----NLPAVRwVGGPE--------IEL 311
Cdd:PRK12849 225 KI--SSLQDLLPL-----------LEKVAQSGKPLLIIAEDVEGEALATLVVNklrgGLKVAA-VKAPGfgdrrkamLED 290
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 807066360 312 IAIATGGRIVPR-----FSELTAEKLGFAGLVqEISFGTT 346
Cdd:PRK12849 291 IAILTGGTVISEdlglkLEEVTLDDLGRAKRV-TITKDNT 329
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
23-192 |
1.10e-08 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 57.73 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 23 VANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 98
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFenmgAQMVREVASKSADAAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 99 AEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLV--DIKDTEPLIQTAKTTLGSKVVNSchrqMAEIAVNAVLTVA 176
Cdd:PRK14104 103 GAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSndEIAQVGTISANGDAEIGKFLADA----MKKVGNEGVITVE 178
|
170
....*....|....*.
gi 807066360 177 dmERRDVDFELIKVEG 192
Cdd:PRK14104 179 --EAKSLETELDVVEG 192
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
23-192 |
8.51e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 54.85 E-value: 8.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 23 VANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 98
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFenmgAQMVREVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 99 AEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVL--VDIKDTEPLIQTAKTTLGSKVVNSchrqMAEIAVNAVLTVA 176
Cdd:PRK12852 103 GAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVAssAEIAQVGTISANGDAAIGKMIAQA----MQKVGNEGVITVE 178
|
170
....*....|....*.
gi 807066360 177 DMERRDVDFELikVEG 192
Cdd:PRK12852 179 ENKSLETEVDI--VEG 192
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
20-153 |
6.57e-07 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 52.03 E-value: 6.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066360 20 AKAVANTmrtsLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL-----SKSqDDEIGDGTTGVVVLAGA 94
Cdd:CHL00093 23 AEAVSVT----LGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALirqaaSKT-NDVAGDGTTTATVLAYA 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 807066360 95 LLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlvdIKDTEPLIQTAKTTLG 153
Cdd:CHL00093 98 IVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARP----VEDIQAITQVASISAG 152
|
|
| |
