|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
1-497 |
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: 1044.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:cd03339 30 LAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGALLE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 81 EAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVAD 160
Cdd:cd03339 110 QAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPDNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAVLSVAD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 161 MERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYKALQ 240
Cdd:cd03339 190 LERKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIAILTCPFEPPKPKTKHKLDITSVEDYKKLQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 241 KYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGL 320
Cdd:cd03339 270 EYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFEDLSPEKLGKAGL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 321 VQEISFGTTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEAD 400
Cdd:cd03339 350 VREISFGTTKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGGGAAEISCSLAVEKAAD 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 401 KCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGTNDMKQQHVIETLIGKKQQIS 480
Cdd:cd03339 430 KCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNPHLGIDCLGRGTNDMKEQKVFETLISKKQQIL 509
|
490
....*....|....*..
gi 807066366 481 LATQMVRMILKIDDIRK 497
Cdd:cd03339 510 LATQVVKMILKIDDVIV 526
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
1-499 |
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: 951.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:TIGR02343 34 AAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 81 EAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVAD 160
Cdd:TIGR02343 114 QAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREPLIQAAKTSLGSKIVSKCHRRFAEIAVDAVLNVAD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 161 MERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYKALQ 240
Cdd:TIGR02343 194 MERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAILTCPFEPPKPKTKHKLDISSVEEYKKLQ 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 241 KYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGL 320
Cdd:TIGR02343 274 KYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPRFQELSKDKLGKAGL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 321 VQEISFGTTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEAD 400
Cdd:TIGR02343 354 VREISFGTTKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGGGAAEISCSLAVSQEAD 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 401 KCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGTNDMKQQHVIETLIGKKQQIS 480
Cdd:TIGR02343 434 KYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNLGVDCLGYGTNDMKEQFVFETLIGKKQQIL 513
|
490
....*....|....*....
gi 807066366 481 LATQMVRMILKIDDIRKPG 499
Cdd:TIGR02343 514 LATQLVRMILKIDDVISPG 532
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
1-495 |
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: 586.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:cd00309 15 NAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDGTTTVVVLAGELLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 81 EAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVAD 160
Cdd:cd00309 95 EAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVP--IDVEDREELLKVATTSLNSKLVSGGDDFLGELVVDAVLKVGK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 161 MErRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPpkpktkhkldvtsvedykalq 240
Cdd:cd00309 173 EN-GDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY--------------------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 241 kyekekfeemiqqiketganLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGL 320
Cdd:cd00309 231 --------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLEDLTPEDLGTAGL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 321 VQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEAD 400
Cdd:cd00309 291 VEETKIG--DEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGAAEIELSKALEELAK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 401 KCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAlGIDCLHKGTNDMKQQHVIETLIGKKQQIS 480
Cdd:cd00309 369 TLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNA-GGDVETGEIVDMKEAGIIDPLKVKRQALK 447
|
490
....*....|....*
gi 807066366 481 LATQMVRMILKIDDI 495
Cdd:cd00309 448 SATEAASLILTIDDI 462
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
6-495 |
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: 559.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 6 VANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQL 85
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 86 LDRGIHPIRIADGYEQAARVAIEHLDKIsDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVADMERrD 165
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSI-ISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDG-S 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 166 VDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKE 245
Cdd:pfam00118 159 FDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 246 KFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGLVQEIS 325
Cdd:pfam00118 239 QILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 326 FGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTL 405
Cdd:pfam00118 319 IG--DEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 406 EQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEmNPALGIDCLHKGTNDMKQQHVIETLIGKKQQISLATQM 485
Cdd:pfam00118 397 EQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASG-EKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEA 475
|
490
....*....|
gi 807066366 486 VRMILKIDDI 495
Cdd:pfam00118 476 ASTILRIDDI 485
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
1-495 |
0e+00 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 537.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:NF041082 24 MAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGELLK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 81 EAEQLLDRGIHPIRIADGYEQAARVAIEHLDKIsdSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVAD 160
Cdd:NF041082 104 KAEELLDQDIHPTIIAEGYRLAAEKALEILDEI--AIKVDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVKAVAE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 161 ME-RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYKAL 239
Cdd:NF041082 182 KDgGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDAKISITDPDQLQAF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 240 QKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAG 319
Cdd:NF041082 262 LDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSIDDLSPEDLGYAG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 320 LVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEA 399
Cdd:NF041082 342 LVEERKVG--GDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEVELALRLREYA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 400 DKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAlGIDCLHKGTNDMKQQHVIETLIGKKQQI 479
Cdd:NF041082 420 ASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTA-GLDVYTGKVVDMLEIGVVEPLRVKTQAI 498
|
490
....*....|....*.
gi 807066366 480 SLATQMVRMILKIDDI 495
Cdd:NF041082 499 KSATEAAVMILRIDDV 514
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
1-495 |
0e+00 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 522.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:NF041083 24 MAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAVVLAGELLK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 81 EAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVAd 160
Cdd:NF041083 104 KAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEK--VDPDDRETLKKIAETSLTSKGVEEARDYLAEIAVKAVKQVA- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 161 mERRD----VDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDY 236
Cdd:NF041083 181 -EKRDgkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAEIRITDPDQL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 237 KALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLG 316
Cdd:NF041083 260 QKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVTNIDDLTPEDLG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 317 FAGLVQEISFGTtkDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVS 396
Cdd:NF041083 340 YAELVEERKVGD--DKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGAPEVELAKRLR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 397 QEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEmNPALGIDCLHKGTNDMKQQHVIETLIGKK 476
Cdd:NF041083 418 EYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKG-KKWAGINVFTGEVVDMWELGVIEPLRVKT 496
|
490
....*....|....*....
gi 807066366 477 QQISLATQMVRMILKIDDI 495
Cdd:NF041083 497 QAIKSATEAATMILRIDDV 515
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
1-495 |
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: 521.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:cd03343 22 AAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 81 EAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVAD 160
Cdd:cd03343 102 KAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIK--VDPDDKDTLRKIAKTSLTGKGAEAAKDKLADLVVDAVLQVAE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 161 ME--RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYKA 238
Cdd:cd03343 180 KRdgKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAKIRITSPDQLQA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 239 LQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFA 318
Cdd:cd03343 260 FLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTNIDDLTPEDLGEA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 319 GLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQE 398
Cdd:cd03343 340 ELVEERKVG--DDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGAVEIELAKRLREY 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 399 ADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAlGIDCLHKGTNDMKQQHVIETLIGKKQQ 478
Cdd:cd03343 418 ARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNA-GLDVYTGEVVDMLEKGVIEPLRVKKQA 496
|
490
....*....|....*..
gi 807066366 479 ISLATQMVRMILKIDDI 495
Cdd:cd03343 497 IKSATEAATMILRIDDV 513
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
1-495 |
8.28e-171 |
|
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: 491.89 E-value: 8.28e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:TIGR02339 23 AAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 81 EAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlVDIKDTEPLIQTAKTTLGSKVVNSCHRQ-MAEIAVNAVLTVA 159
Cdd:TIGR02339 103 KAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATK--ISPEDRDLLKKIAYTSLTSKASAEVAKDkLADLVVEAVKQVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 160 DME---RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDY 236
Cdd:TIGR02339 181 ELRgdgKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAPLEVEKTEIDAKIRITDPDQI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 237 KALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLG 316
Cdd:TIGR02339 261 KKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVSSIDEITESDLG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 317 FAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVS 396
Cdd:TIGR02339 341 YAELVEERKVG--EDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVAGGGAVEIELALRLR 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 397 QEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEmNPALGIDCLHKGTNDMKQQHVIETLIGKK 476
Cdd:TIGR02339 419 SYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKG-NKNAGINVFTGEIEDMLELGVIEPLRVKE 497
|
490
....*....|....*....
gi 807066366 477 QQISLATQMVRMILKIDDI 495
Cdd:TIGR02339 498 QAIKSATEAATMILRIDDV 516
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
1-495 |
1.14e-152 |
|
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: 445.19 E-value: 1.14e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:cd03338 15 QAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGALLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 81 EAEQLLDRGIHPIRIADGYEQAARVAIEHLDKIsdSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVAD 160
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSM--SIPVDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVID 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 161 MER-RDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSH-PQMPKKVEDAKIAILTCPFEPPKPKTKHKLdvtSVEDYKA 238
Cdd:cd03338 173 PATaTNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDMDNNI---VVNDYAQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 239 ---LQKYEKEKFEEMIQQIKETGANLAICQW-----GFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSEL 310
Cdd:cd03338 250 mdrILREERKYILNMCKKIKKSGCNVLLIQKsilrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVASIDHF 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 311 TAEKLGFAGLVQEISFGTtkDKMLVIEQCKNS-RAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEI 389
Cdd:cd03338 330 TEDKLGSADLVEEVSLGD--GKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGAPEI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 390 SCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVK-EMNpaLGIDCLHKGTNDMKQQHV 468
Cdd:cd03338 408 EIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQgEKN--AGINVRKGAITNILEENV 485
|
490 500
....*....|....*....|....*..
gi 807066366 469 IETLIGKKQQISLATQMVRMILKIDDI 495
Cdd:cd03338 486 VQPLLVSTSAITLATETVRMILKIDDI 512
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
1-495 |
8.60e-140 |
|
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: 412.64 E-value: 8.60e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:TIGR02342 16 VAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGALLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 81 EAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVAD 160
Cdd:TIGR02342 96 ACERLLNKGIHPTIISESFQSAADEAIKILDEMSIP--VDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVLKVID 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 161 MER-RDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQ-MPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYKA 238
Cdd:TIGR02342 174 PENaKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDYAQMDR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 239 LQKYEKEKFEEMIQQIKETGANLAICQW-----GFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAE 313
Cdd:TIGR02342 254 VLKEERAYILNIVKKIKKTGCNVLLIQKsilrdAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASIDHFTAD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 314 KLGFAGLVQEIsfGTTKDKMLVIEQCKN-SRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCA 392
Cdd:TIGR02342 334 KLGSAELVEEV--DSDGGKIIKITGIQNaGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPEIEIA 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 393 LAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVK-EMNpaLGIDCLHKGTNDMKQQHVIET 471
Cdd:TIGR02342 412 RRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANgEKT--AGISVRKGGITNMLEEHVLQP 489
|
490 500
....*....|....*....|....
gi 807066366 472 LIGKKQQISLATQMVRMILKIDDI 495
Cdd:TIGR02342 490 LLVTTSAITLASETVRSILKIDDI 513
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
1-495 |
4.10e-124 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 371.72 E-value: 4.10e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAG 76
Cdd:COG0459 17 RGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFenmgAQLVKEVASKTNDEAGDGTTTATVLAG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 77 ALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdsvlVDIKDTEPLIQTAKTTLGSKvvnschRQMAEIAVNAVL 156
Cdd:COG0459 97 ALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIA----KPVDDKEELAQVATISANGD------EEIGELIAEAME 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 157 TVADMERrdvdfelIKVEgKVGGRLEDTKLIKGVIVDKDFSHPQ-------MPKKVEDAKIAILTCPFEPPKPktkhkld 229
Cdd:COG0459 167 KVGKDGV-------ITVE-EGKGLETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDKKISSIQD------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 230 vtsvedykalqkyekekFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVR---WVGGP--------EIELIAIA 298
Cdd:COG0459 232 -----------------LLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLrvvAVKAPgfgdrrkaMLEDIAIL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 299 TGGRIV-----PRFSELTAEKLGFAGLVQEisfgtTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRN 373
Cdd:COG0459 295 TGGRVIsedlgLKLEDVTLDDLGRAKRVEV-----DKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALHATRA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 374 LIRDnRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvkemNPALGI 453
Cdd:COG0459 370 AVEE-GIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAK----DKGFGF 444
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 807066366 454 DCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDI 495
Cdd:COG0459 445 DAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAV 486
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
1-495 |
2.29e-123 |
|
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: 369.32 E-value: 2.29e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:cd03337 23 QAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILAGEILA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 81 EAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVA- 159
Cdd:cd03337 103 VAEPFLERGIHPTVIIKAYRKALEDALKILEEISIP--VDVNDRAQMLKIIKSCIGTKFVSRWSDLMCNLALDAVKTVAv 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 160 --DMERRDVDFE-LIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEppkpktkhkldvtsvedY 236
Cdd:cd03337 181 eeNGRKKEIDIKrYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPLE-----------------Y 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 237 kalqkyekekfeemiqqiketganLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLG 316
Cdd:cd03337 244 ------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARACGATIVNRPEELTESDVG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 317 FAGLVQEISFGtTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVS 396
Cdd:cd03337 300 TGAGLFEVKKI-GDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILNPKLVPGGGATEMAVSHALS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 397 QEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGTNDMKQQHVIETLIGKK 476
Cdd:cd03337 379 EKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTWGIDGETGDIVDMKELGIWDPLAVKA 458
|
490
....*....|....*....
gi 807066366 477 QQISLATQMVRMILKIDDI 495
Cdd:cd03337 459 QTYKTAIEAACMLLRIDDI 477
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
2-495 |
1.52e-117 |
|
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: 355.97 E-value: 1.52e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 2 AAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 81
Cdd:TIGR02344 24 AAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILAGEMLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 82 AEQLLDRGIHPIRIADGYEQAARVAIEHLDKIsdSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVA-- 159
Cdd:TIGR02344 104 AEPFLEQNIHPTVIIRAYRKALDDALSVLEEI--SIPVDVNDDAAMLKLIQSCIGTKFVSRWSDLMCDLALDAVRTVQrd 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 160 DMERRDVDFE-LIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYKA 238
Cdd:TIGR02344 182 ENGRKEIDIKrYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLEYKKGESQTNIEITKEEDWNR 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 239 LQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGF- 317
Cdd:TIGR02344 262 ILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACGATIVNRPEELRESDVGTg 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 318 AGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQ 397
Cdd:TIGR02344 342 CGLFEVKKIG--DEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKLVPGGGATEMAVSVALTE 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 398 EADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGTNDMKQQHVIETLIGKKQ 477
Cdd:TIGR02344 420 KSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTWGIDGETGKIVDMKEKGIWEPLAVKLQ 499
|
490
....*....|....*...
gi 807066366 478 QISLATQMVRMILKIDDI 495
Cdd:TIGR02344 500 TYKTAIESACLLLRIDDI 517
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
1-497 |
9.02e-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: 340.85 E-value: 9.02e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 1 MAAKAVANTMRTSLGPNGLDKMM--VDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGAL 78
Cdd:cd03336 20 VGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDGTTSVTVLAAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 79 LEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKDT-EPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLT 157
Cdd:cd03336 100 LREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEAFrEDLLNIARTTLSSKILTQDKEHFAELAVDAVLR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 158 VADmerrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKKVEDAKIAILTCPFEPPKPKT-KHKLDVTSVEDY 236
Cdd:cd03336 180 LKG----SGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTPMDTDKIKIfGAKVRVDSTAKV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 237 KALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLG 316
Cdd:cd03336 255 AEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTGGEIASTFDHPELVKLG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 317 FAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVS 396
Cdd:cd03336 335 TCKLIEEIMIG--EDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRVVLGGGCSEMLMAKAVE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 397 QEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAlGIDCLHKGTNDMKQQHVIETLIGKK 476
Cdd:cd03336 413 ELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTA-GLDMRKGTVGDMKELGITESFKVKR 491
|
490 500
....*....|....*....|.
gi 807066366 477 QQISLATQMVRMILKIDDIRK 497
Cdd:cd03336 492 QVLLSASEAAEMILRVDDIIK 512
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-495 |
3.56e-110 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 337.00 E-value: 3.56e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 1 MAAKAVANTMRTSLGPNGLDKMMV-----DKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLA 75
Cdd:PTZ00212 29 VGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGDGTTSVVVLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 76 GALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKD-TEPLIQTAKTTLGSKVVNSCHRQMAEIAVNA 154
Cdd:PTZ00212 109 GELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEKfKEDLLNIARTTLSSKLLTVEKDHFAKLAVDA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 155 VLTVadmeRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKKVEDAKIAILTCPFEPPKPKT-KHKLDVTSV 233
Cdd:PTZ00212 189 VLRL----KGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVGQ-PKRLENCKILVANTPMDTDKIKIyGAKVKVDSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 234 EDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAE 313
Cdd:PTZ00212 264 EKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPEKV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 314 KLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCAL 393
Cdd:PTZ00212 344 KLGHCDLIEEIMIG--EDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKDTRVVLGGGCSEMLMAN 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 394 AVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPAlGIDCLHKGTNDMKQQHVIETLI 473
Cdd:PTZ00212 422 AVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTA-GIDMEKGTVGDMKELGITESYK 500
|
490 500
....*....|....*....|..
gi 807066366 474 GKKQQISLATQMVRMILKIDDI 495
Cdd:PTZ00212 501 VKLSQLCSATEAAEMILRVDDI 522
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
2-493 |
1.65e-107 |
|
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: 330.02 E-value: 1.65e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 2 AAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 81
Cdd:cd03340 24 ACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLKE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 82 AEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKDT--EPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVA 159
Cdd:cd03340 104 AKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKEEqrELLEKCAATALNSKLIASEKEFFAKMVVDAVLSLD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 160 DmerrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFS---HPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDY 236
Cdd:cd03340 184 D----DLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSyagFEQQPKKFKNPKILLLNVELELKAEKDNAEVRVEDPEEY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 237 KALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLG 316
Cdd:cd03340 260 QAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQTTVSNITDDVLG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 317 FAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVS 396
Cdd:cd03340 340 TCGLFEERQVG--GERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 397 QEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGTNDMKQQHVIETLIGKK 476
Cdd:cd03340 418 DYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKWYGVDINNEGIADNFEAFVWEPSLVKI 497
|
490
....*....|....*..
gi 807066366 477 QQISLATQMVRMILKID 493
Cdd:cd03340 498 NALTAATEAACLILSVD 514
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
1-497 |
4.79e-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: 323.85 E-value: 4.79e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:cd03335 15 TAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAELLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 81 EAEQLLDRGIHPIRIADGYEQAARVAIEHLDKiSDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVAD 160
Cdd:cd03335 95 RANELVKQKIHPTTIISGYRLACKEAVKYIKE-HLSISVDNLGKESLINVAKTSMSSKIIGADSDFFANMVVDAILAVKT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 161 M-ERRDV-----DFELIKVEGKvggRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEppkpKTKHKLDV---- 230
Cdd:cd03335 174 TnEKGKTkypikAVNILKAHGK---SAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQ----KTKMKLGVqvvv 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 231 TSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSEL 310
Cdd:cd03335 247 TDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVSTLANL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 311 TAE------KLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGG 384
Cdd:cd03335 327 EGEetfdpsYLGEAEEVVQERIG--DDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 385 GAAEisCALAVSQE--ADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPA-------LGIDc 455
Cdd:cd03335 405 GAVE--TALSIYLEnfATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKPdkkhlkwYGLD- 481
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 807066366 456 LHKGT-NDMKQQHVIETLIGKKQQISLATQMVRMILKIDDIRK 497
Cdd:cd03335 482 LINGKvRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
1-503 |
2.03e-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: 317.43 E-value: 2.03e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:TIGR02340 19 TAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVIIAAELLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 81 EAEQLLDRGIHPIRIADGYEQAARVAIEHLDKiSDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVAD 160
Cdd:TIGR02340 99 RADELVKNKIHPTSVISGYRLACKEAVKYIKE-NLSVSVDELGREALINVAKTSMSSKIIGLDSDFFSNIVVDAVLAVKT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 161 M-ERRDVDF--ELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEppkpKTKHKLDVT-SVEDY 236
Cdd:TIGR02340 178 TnENGETKYpiKAINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQ----KAKMALGVQiVVDDP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 237 KALQKYEKEKFE---EMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAE 313
Cdd:TIGR02340 254 EKLEQIRQREADitkERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVSTLADLEGE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 314 ------KLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAA 387
Cdd:TIGR02340 334 etfeasYLGFADEVVQERIA--DDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGGAV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 388 EISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEM-NPA------LGIDCLHKGT 460
Cdd:TIGR02340 412 EAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAQlKPEkkhlkwYGLDLVNGKI 491
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 807066366 461 NDMKQQHVIETLIGKKQQISLATQMVRMILKIDD-IRKPGESEE 503
Cdd:TIGR02340 492 RDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDlIKLNPEQSK 535
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
2-499 |
3.00e-102 |
|
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: 316.32 E-value: 3.00e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 2 AAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 81
Cdd:TIGR02345 26 ACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGELLKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 82 AEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSV-LVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTvad 160
Cdd:TIGR02345 106 AKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIdEEKGEQRELLEKCAATALSSKLISHNKEFFSKMIVDAVLS--- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 161 MERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFS---HPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYK 237
Cdd:TIGR02345 183 LDRDDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSyagFEQQPKKFANPKILLLNVELELKAEKDNAEIRVEDVEDYQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 238 ALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGF 317
Cdd:TIGR02345 263 AIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTTSDLEADVLGT 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 318 AGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQ 397
Cdd:TIGR02345 343 CALFEERQIG--SERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIEMELSKCLRD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 398 EADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEmNPALGIDCLHKGTNDMKQQHVIETLIGKKQ 477
Cdd:TIGR02345 421 YSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKG-GKWYGVDINTEDIGDNFEAFVWEPALVKIN 499
|
490 500
....*....|....*....|...
gi 807066366 478 QISLATQMVRMILKIDD-IRKPG 499
Cdd:TIGR02345 500 ALKAAFEAACTILSVDEtITNPK 522
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
2-495 |
2.54e-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: 312.23 E-value: 2.54e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 2 AAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 81
Cdd:cd03341 16 ACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGELLEK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 82 AEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKDTEPLIQTAKTTLGSKVV-NSCHrqMAEIAVNAVLTVAD 160
Cdd:cd03341 96 AEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLRNKEEVSKALKTAIASKQYgNEDF--LSPLVAEACISVLP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 161 MERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDfSHPQMpKKVEDAKIAILTCPFeppkpktkhkldvtsvedykalq 240
Cdd:cd03341 174 ENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKRE-PEGSV-KRVKKAKVAVFSCPF----------------------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 241 kyekekfeemiqqikETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGL 320
Cdd:cd03341 229 ---------------DIGVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEEIGYCDS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 321 VQEISFGTTkdKMLVIEQCKNSRAV-TIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEA 399
Cdd:cd03341 294 VYVEEIGDT--KVVVFRQNKEDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAKKLKEYG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 400 DKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKE-MNPALGIDCLHKGTNDMKQQHVIETLIGKKQQ 478
Cdd:cd03341 372 EKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGnKSAGVDIESGDEGTKDAKEAGIFDHLATKKWA 451
|
490
....*....|....*..
gi 807066366 479 ISLATQMVRMILKIDDI 495
Cdd:cd03341 452 IKLATEAAVTVLRVDQI 468
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
2-495 |
1.59e-97 |
|
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: 304.33 E-value: 1.59e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 2 AAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 81
Cdd:TIGR02346 26 ACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGELLNK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 82 AEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKDTEPLIQTAKTTLGSKVVNScHRQMAEIAVNAVLTVADM 161
Cdd:TIGR02346 106 AEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDLRDKDELIKALKASISSKQYGN-EDFLAQLVAQACSTVLPK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 162 ERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFShpQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYKALQK 241
Cdd:TIGR02346 185 NPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNREAE--GSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNAEELLNYSK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 242 YEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGLV 321
Cdd:TIGR02346 263 GEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPEEIGYVDSV 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 322 QEISFGTtkDKMLVIEQCK-NSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEAD 400
Cdd:TIGR02346 343 YVSEIGG--DKVTVFKQENgDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELASRLTKYGE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 401 KCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKEMNPALGID--CLHKGTNDMKQQHVIETLIGKKQQ 478
Cdd:TIGR02346 421 KLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAH-KKGNKSKGIDieAESDGVKDASEAGIYDMLATKKWA 499
|
490
....*....|....*..
gi 807066366 479 ISLATQMVRMILKIDDI 495
Cdd:TIGR02346 500 IKLATEAAVTVLRVDQI 516
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
1-497 |
8.84e-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: 291.76 E-value: 8.84e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 1 MAAKAVANTMRTSLGPNGLDKMMV--DKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGAL 78
Cdd:TIGR02341 21 VGAIAIGDLVKSTLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEVGDGTTSVTVLAAEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 79 LEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKIS-DSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLT 157
Cdd:TIGR02341 101 LREAEKLINQKIHPQTIIAGYREATKAARDALLKSAvDNGSDEVKFRQDLMNIARTTLSSKILSQHKDHFAQLAVDAVLR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 158 VadmeRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKKVEDAKIAILTCPFEPPKPKT-KHKLDVTSVEDY 236
Cdd:TIGR02341 181 L----KGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTDKVKIfGSRVRVDSTAKV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 237 KALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLG 316
Cdd:TIGR02341 256 AELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIVSTFDHPELVKLG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 317 FAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVS 396
Cdd:TIGR02341 336 SCDLIEEIMIG--EDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGGGCSEMLMSKAVT 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 397 QEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRArQVKEMNPALGIDcLHKGT-NDMKQQHVIETLIGK 475
Cdd:TIGR02341 414 QEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRA-AHYNGNTTMGLD-MNEGTiADMRQLGITESYKVK 491
|
490 500
....*....|....*....|..
gi 807066366 476 KQQISLATQMVRMILKIDDIRK 497
Cdd:TIGR02341 492 RAVVSSAAEAAEVILRVDNIIK 513
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
2-501 |
1.27e-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: 270.84 E-value: 1.27e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 2 AAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 81
Cdd:TIGR02347 24 AARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 82 AEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVADM 161
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFLDKFK-VKKEDEVDREFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIKKD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 162 ErRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYKALQK 241
Cdd:TIGR02347 183 G-EDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQREKLVK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 242 YEKEKFEEMIQQIKE-------TGAN---LAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELT 311
Cdd:TIGR02347 262 AERKFVDDRVKKIIElkkkvcgKSPDkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEALNSVEDLT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 312 AEKLGFAGLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISC 391
Cdd:TIGR02347 342 PECLGWAGLVYETTIG--EEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAGAFEIAA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 392 ALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPaLGIDcLHKGTN-DMKQQHVIE 470
Cdd:TIGR02347 420 YRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEV-VGVD-LNTGEPiDPEIKGIWD 497
|
490 500 510
....*....|....*....|....*....|.
gi 807066366 471 TLIGKKQQISLATQMVRMILKIDDIRKPGES 501
Cdd:TIGR02347 498 NYRVKKQLIQSATVIASQLLLVDEVMRAGRS 528
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
2-499 |
6.01e-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: 267.59 E-value: 6.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 2 AAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 81
Cdd:cd03342 20 AAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGELLKQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 82 AEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIkDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVadm 161
Cdd:cd03342 100 AERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDT-DRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAI--- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 162 ERRDVDFELIKVE-GKVGGRLE-DTKLIKGVIVDKDFSHPQMPKKVEDAkiAILTCPFeppkpktkhkldvtSVEdykal 239
Cdd:cd03342 176 YKPDEPIDLHMVEiMQMQHKSDsDTKLIRGLVLDHGARHPDMPKRVENA--YILTCNV--------------SLE----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 240 qkYEK-EKFEEMIQqiketgaNLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFA 318
Cdd:cd03342 235 --YEKtEVNSGFFY-------SVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPECLGYA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 319 GLVQEISFGttKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQE 398
Cdd:cd03342 306 GLVYERTLG--EEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHLKEF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 399 ADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRaRQVKEMNPALGIDCLHKGTNDMKQQHVIETLIGKKQQ 478
Cdd:cd03342 384 KKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQ-DEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQI 462
|
490 500
....*....|....*....|.
gi 807066366 479 ISLATQMVRMILKIDDIRKPG 499
Cdd:cd03342 463 LHSATVIASQLLLVDEIIRAG 483
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
125-377 |
1.49e-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: 239.29 E-value: 1.49e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 125 EPLIQTAKTTLGSKVvNSCHRQMAEIAVNAVLTVADMERrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKK 204
Cdd:cd03333 2 ELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNR-MDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 205 VEDAKIAILTCPFEPpkpktkhkldvtsvedykalqkyekekfeemiqqiketganLAICQWGFDDEANHLLLQNNLPAV 284
Cdd:cd03333 80 LENAKILLLDCPLEY-----------------------------------------VVIAEKGIDDLALHYLAKAGIMAV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 285 RWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGLVQEISFGTtkDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSL 364
Cdd:cd03333 119 RRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGE--EKLTFIEGCKGGKAATILLRGATEVELDEVKRSL 196
|
250
....*....|...
gi 807066366 365 HDALCVIRNLIRD 377
Cdd:cd03333 197 HDALCAVRAAVEE 209
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
149-375 |
8.92e-16 |
|
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: 77.26 E-value: 8.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 149 EIAVNAVLTVADMERRDVDF-------ELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPK 221
Cdd:cd03334 21 DILLPLVWKAASNVKPDVRAgddmdirQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 222 PKTKhkldVTSVEDYKAlqkYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGG 301
Cdd:cd03334 101 VENK----LLSLDPVIL---QEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807066366 302 RIVPRFSELTAE-KLGFAGLVQEISF----GTTKDKMLvIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 375
Cdd:cd03334 174 DIISSMDDLLTSpKLGTCESFRVRTYveehGRSKTLMF-FEGCPKELGCTILLRGGDLEELKKVKRVVEFMVFAAYHLK 251
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
3-469 |
3.94e-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: 77.88 E-value: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 3 AKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATI---LSMMD-VDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGAL 78
Cdd:cd03344 17 VNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVakeIELEDpFENMGAQLVKEVASKTNDVAGDGTTTATVLARAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 79 LEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdsvlVDIKDTEPLIQTAKT------TLGSKVVNSchrqMAEIAV 152
Cdd:cd03344 97 IKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLS----KPVKTKEEIAQVATIsangdeEIGELIAEA----MEKVGK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 153 NAVLTVADmerrdvdfelikvegkvGGRLEDT-KLIKGVIVDKDFSHPQM---PKK----VEDAKIAIltcpfeppkpkT 224
Cdd:cd03344 169 DGVITVEE-----------------GKTLETElEVVEGMQFDRGYLSPYFvtdPEKmeveLENPYILL-----------T 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 225 KHKLDvtSVEDYKALqkyekekfeemIQQIKETGANLAICQWGFDDEANHLLLQNNLP------AVRwvgGPE------- 291
Cdd:cd03344 221 DKKIS--SIQELLPI-----------LELVAKAGRPLLIIAEDVEGEALATLVVNKLRgglkvcAVK---APGfgdrrka 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 292 -IELIAIATGGRIVP-----RFSELTAEKLGFAGLVQeisfgTTKDKMLV-------------IEQCKNSRAVT------ 346
Cdd:cd03344 285 mLEDIAILTGGTVISeelglKLEDVTLEDLGRAKKVV-----VTKDDTTIiggagdkaaikarIAQIRKQIEETtsdydk 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 347 ----------------IFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNrVVYGGGAAEISCALAVSQEADKCPtLEQYAM 410
Cdd:cd03344 360 eklqerlaklsggvavIKVGGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPALDKLKALNG-DEKLGI 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 807066366 411 RAFADALEVIPMALSENSGMNPiqtmtEVRARQVKEMNPALGIDCLHKGTNDMKQQHVI 469
Cdd:cd03344 438 EIVRRALEAPLRQIAENAGVDG-----SVVVEKVLESPDGFGYDAATGEYVDMIEAGII 491
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
4-175 |
1.05e-12 |
|
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES cytosolic chaperonin. It is found in bacteria, organelles derived from bacteria, and occasionally in the Archaea. The bacterial GroEL/GroES group I chaperonin is replaced a group II chaperonin, usually called the thermosome in the Archaeota and CCT (chaperone-containing TCP) in the Eukaryota. GroEL, thermosome subunits, and CCT subunits all fall under the scope of pfam00118. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274089 Cd Length: 524 Bit Score: 70.01 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 4 KAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALL 79
Cdd:TIGR02348 19 DKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFenmgAQLVKEVASKTNDVAGDGTTTATVLAQAIV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 80 EEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdsvlVDIKDTEPLIQTAKTTLGS--KVVNSCHRQMAEIAVNAVLT 157
Cdd:TIGR02348 99 KEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLS----KPVKGKKEIAQVATISANNdeEIGSLIAEAMEKVGKDGVIT 174
|
170
....*....|....*...
gi 807066366 158 VAdmERRDVDFELIKVEG 175
Cdd:TIGR02348 175 VE--ESKSLETELEVVEG 190
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
5-318 |
2.86e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 65.51 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 5 AVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKL---MV-ELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:PRK12850 22 ILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMgaqMVkEVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 81 EAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdsvlVDIKDTEPLIQTA------KTTLGSKVVnschRQMAEIAVNA 154
Cdd:PRK12850 102 EGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIA----KKVTSSKEIAQVAtisangDESIGEMIA----EAMDKVGKEG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 155 VLTVAdmERRDVDFELIKVEGKvggRLEDTKLIKGVIVDKDfshpQMPKKVEDAKIAIltcpfeppkpktkHKLDVTSVE 234
Cdd:PRK12850 174 VITVE--EAKTLGTELDVVEGM---QFDRGYLSPYFVTNPE----KMRAELEDPYILL-------------HEKKISNLQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 235 DYKALqkyekekfeemIQQIKETGANLAICQWGFDDEANHLLLQNNL------PAVRWVG-----GPEIELIAIATGGRI 303
Cdd:PRK12850 232 DLLPI-----------LEAVVQSGRPLLIIAEDVEGEALATLVVNKLrgglksVAVKAPGfgdrrKAMLEDIAVLTGGQV 300
|
330 340
....*....|....*....|
gi 807066366 304 VP-----RFSELTAEKLGFA 318
Cdd:PRK12850 301 ISedlgiKLENVTLDMLGRA 320
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
4-431 |
5.15e-11 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 64.93 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 4 KAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATIL-------SMMDVDhqiAKLMVELSKSQDDEIGDGTTGVVVLAG 76
Cdd:PTZ00114 32 ERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAkaiefsdRFENVG---AQLIRQVASKTNDKAGDGTTTATILAR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 77 ALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDsvlvDIKDTEPLIQTAKTT------LGSKVVNSchrqMAEI 150
Cdd:PTZ00114 109 AIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSR----PVKTKEDILNVATISangdveIGSLIADA----MDKV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 151 AVNAVLTVADmerrdvdfelikvegkvGGRLEDT-KLIKGVIVDKDFSHPQMPKKVEDAKIaILTCPFeppkpktkhkld 229
Cdd:PTZ00114 181 GKDGTITVED-----------------GKTLEDElEVVEGMSFDRGYISPYFVTNEKTQKV-ELENPL------------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 230 vTSVEDYKALQkyekekfeemIQQI-------KETGANLAICQWGFDDEANHLLLQNNLP------AVRWVGGPE----- 291
Cdd:PTZ00114 231 -ILVTDKKISS----------IQSIlpilehaVKNKRPLLIIAEDVEGEALQTLIINKLRgglkvcAVKAPGFGDnrkdi 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 292 IELIAIATGGRIVPR------FSELTAEKLGFAGLVQ-----EISFGTTKDKMLVIEQCKNSRA---------------- 344
Cdd:PTZ00114 300 LQDIAVLTGATVVSEdnvglkLDDFDPSMLGSAKKVTvtkdeTVILTGGGDKAEIKERVELLRSqierttseydkeklke 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 345 ---------VTIFIRGGNKMIIEEAKRSLHDALCVIRNLIrDNRVVYGGGAAEI--SCALAVSQEADKCPTLEQYAMRAF 413
Cdd:PTZ00114 380 rlaklsggvAVIKVGGASEVEVNEKKDRIEDALNATRAAV-EEGIVPGGGVALLraSKLLDKLEEDNELTPDQRTGVKIV 458
|
490
....*....|....*...
gi 807066366 414 ADALEVIPMALSENSGMN 431
Cdd:PTZ00114 459 RNALRLPTKQIAENAGVE 476
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
6-175 |
5.59e-10 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 61.86 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 6 VANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 81
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVenigAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 82 AEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVlvdiKDTEpLIQTAKTTLGS--KVVNSCHRQMAEIAVNAVLTVA 159
Cdd:PLN03167 158 GVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEV----EDSE-LADVAAVSAGNnyEVGNMIAEAMSKVGRKGVVTLE 232
|
170
....*....|....*.
gi 807066366 160 dmERRDVDFELIKVEG 175
Cdd:PLN03167 233 --EGKSAENNLYVVEG 246
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
5-131 |
1.35e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 60.52 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 5 AVANTMRTSLGPNG----LDKmmvdKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAG 76
Cdd:PRK00013 21 KLADAVKVTLGPKGrnvvLEK----SFGAPTITKDGVTVAKEIELEDPFenmgAQLVKEVASKTNDVAGDGTTTATVLAQ 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 807066366 77 ALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdsvlVDIKDTEPLIQTA 131
Cdd:PRK00013 97 AIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKIS----KPVEDKEEIAQVA 147
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
3-175 |
2.39e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 59.76 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 3 AKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGAL 78
Cdd:PRK12851 20 VNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFenmgAQMVREVASKTNDVAGDGTTTATVLAQAI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 79 LEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLV--DIKDTEPLIQTAKTTLGSKVVNSchrqMAEIAVNAVL 156
Cdd:PRK12851 100 VREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTnaEIAQVATISANGDAEIGRLVAEA----MEKVGNEGVI 175
|
170
....*....|....*....
gi 807066366 157 TVAdmERRDVDFELIKVEG 175
Cdd:PRK12851 176 TVE--ESKTAETELEVVEG 192
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
5-329 |
3.78e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 59.05 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 5 AVANTMRTSLGPNGLDkMMVDKD-GDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALL 79
Cdd:PRK12849 21 KLADAVKVTLGPKGRN-VVIDKSfGAPTITKDGVSIAKEIELEDPFenlgAQLVKEVASKTNDVAGDGTTTATVLAQALV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 80 EEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISdsvlVDIKDTEPLIQTAKT------TLGSKVVnschRQMAEIAVN 153
Cdd:PRK12849 100 QEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALA----RPVSGSEEIAQVATIsangdeEIGELIA----EAMEKVGKD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 154 AVLTVAdmERRDVDFELIKVEGkvggrledtklikgVIVDKDFSHPQM---PKK----VEDAKIAIltcpfeppkpkTKH 226
Cdd:PRK12849 172 GVITVE--ESKTLETELEVTEG--------------MQFDRGYLSPYFvtdPERmeavLEDPLILL-----------TDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 227 KLdvTSVEDYKALqkyekekfeemIQQIKETGANLAICQWGFDDEANHLLLQN----NLPAVRwVGGPE--------IEL 294
Cdd:PRK12849 225 KI--SSLQDLLPL-----------LEKVAQSGKPLLIIAEDVEGEALATLVVNklrgGLKVAA-VKAPGfgdrrkamLED 290
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 807066366 295 IAIATGGRIVPR-----FSELTAEKLGFAGLVqEISFGTT 329
Cdd:PRK12849 291 IAILTGGTVISEdlglkLEEVTLDDLGRAKRV-TITKDNT 329
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
6-175 |
1.15e-08 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 57.35 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 6 VANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 81
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFenmgAQMVREVASKSADAAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 82 AEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLV--DIKDTEPLIQTAKTTLGSKVVNSchrqMAEIAVNAVLTVA 159
Cdd:PRK14104 103 GAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSndEIAQVGTISANGDAEIGKFLADA----MKKVGNEGVITVE 178
|
170
....*....|....*.
gi 807066366 160 dmERRDVDFELIKVEG 175
Cdd:PRK14104 179 --EAKSLETELDVVEG 192
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
6-175 |
9.50e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 54.47 E-value: 9.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 6 VANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 81
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFenmgAQMVREVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 82 AEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVL--VDIKDTEPLIQTAKTTLGSKVVNSchrqMAEIAVNAVLTVA 159
Cdd:PRK12852 103 GAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVAssAEIAQVGTISANGDAAIGKMIAQA----MQKVGNEGVITVE 178
|
170
....*....|....*.
gi 807066366 160 DMERRDVDFELikVEG 175
Cdd:PRK12852 179 ENKSLETEVDI--VEG 192
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
3-136 |
6.28e-07 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 52.03 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066366 3 AKAVANTmrtsLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVEL-----SKSqDDEIGDGTTGVVVLAGA 77
Cdd:CHL00093 23 AEAVSVT----LGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALirqaaSKT-NDVAGDGTTTATVLAYA 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 807066366 78 LLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSvlvdIKDTEPLIQTAKTTLG 136
Cdd:CHL00093 98 IVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARP----VEDIQAITQVASISAG 152
|
|
| |
