|
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: 1032.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:cd03339 30 LAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGALLE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 81 EAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVLVDINNPEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVLTVAD 160
Cdd:cd03339 110 QAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPDNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAVLSVAD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 161 MERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEPPKPKTKHKLDVMSVEDYKALQ 240
Cdd:cd03339 190 LERKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIAILTCPFEPPKPKTKHKLDITSVEDYKKLQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 241 KYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTSEKLGFAGV 320
Cdd:cd03339 270 EYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFEDLSPEKLGKAGL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 321 VQEISFGTTKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEAD 400
Cdd:cd03339 350 VREISFGTTKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGGGAAEISCSLAVEKAAD 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 401 KCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPALGIDCLHKGSNDMQYQHVIETLIGKKQQIS 480
Cdd:cd03339 430 KCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNPHLGIDCLGRGTNDMKEQKVFETLISKKQQIL 509
|
490
....*....|....*..
gi 1130413408 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: 942.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:TIGR02343 34 AAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 81 EAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVLVDINNPEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVLTVAD 160
Cdd:TIGR02343 114 QAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREPLIQAAKTSLGSKIVSKCHRRFAEIAVDAVLNVAD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 161 MERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEPPKPKTKHKLDVMSVEDYKALQ 240
Cdd:TIGR02343 194 MERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAILTCPFEPPKPKTKHKLDISSVEEYKKLQ 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 241 KYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTSEKLGFAGV 320
Cdd:TIGR02343 274 KYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPRFQELSKDKLGKAGL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 321 VQEISFGTTKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEAD 400
Cdd:TIGR02343 354 VREISFGTTKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGGGAAEISCSLAVSQEAD 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 401 KCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPALGIDCLHKGSNDMQYQHVIETLIGKKQQIS 480
Cdd:TIGR02343 434 KYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNLGVDCLGYGTNDMKEQFVFETLIGKKQQIL 513
|
490
....*....|....*....
gi 1130413408 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: 576.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:cd00309 15 NAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDGTTTVVVLAGELLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 81 EAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKvlVDINNPEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVLTVAD 160
Cdd:cd00309 95 EAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVP--IDVEDREELLKVATTSLNSKLVSGGDDFLGELVVDAVLKVGK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 161 MErRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEPpkpktkhkldvmsvedykalq 240
Cdd:cd00309 173 EN-GDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY--------------------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 241 kyekekfeemikqiketganLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTSEKLGFAGV 320
Cdd:cd00309 231 --------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLEDLTPEDLGTAGL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 321 VQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEAD 400
Cdd:cd00309 291 VEETKIG--DEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGAAEIELSKALEELAK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 401 KCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPAlGIDCLHKGSNDMQYQHVIETLIGKKQQIS 480
Cdd:cd00309 369 TLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNA-GGDVETGEIVDMKEAGIIDPLKVKRQALK 447
|
490
....*....|....*
gi 1130413408 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: 552.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 6 VANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQL 85
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 86 LDRGIHPIRIADGYEQAARIAIQHLDKIsDKVLVDINNPEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVLTVADMERrD 165
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSI-ISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDG-S 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 166 VDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEPPKPKTKHKLDVMSVEDYKALQKYEKE 245
Cdd:pfam00118 159 FDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 246 KFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTSEKLGFAGVVQEIS 325
Cdd:pfam00118 239 QILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 326 FGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTL 405
Cdd:pfam00118 319 IG--DEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 406 EQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKESNPALGIDCLHKGSNDMQYQHVIETLIGKKQQISLATQM 485
Cdd:pfam00118 397 EQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAH-ASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEA 475
|
490
....*....|
gi 1130413408 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: 526.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:NF041082 24 MAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGELLK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 81 EAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKvlVDINNPEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVLTVAD 160
Cdd:NF041082 104 KAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIK--VDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVKAVAE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 161 ME-RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEPPKPKTKHKLDVMSVEDYKAL 239
Cdd:NF041082 182 KDgGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDAKISITDPDQLQAF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 240 QKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTSEKLGFAG 319
Cdd:NF041082 262 LDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSIDDLSPEDLGYAG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 320 VVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEA 399
Cdd:NF041082 342 LVEERKVG--GDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEVELALRLREYA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 400 DKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPAlGIDCLHKGSNDMQYQHVIETLIGKKQQI 479
Cdd:NF041082 420 ASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTA-GLDVYTGKVVDMLEIGVVEPLRVKTQAI 498
|
490
....*....|....*.
gi 1130413408 480 SLATQMVRMILKIDDI 495
Cdd:NF041082 499 KSATEAAVMILRIDDV 514
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
1-495 |
1.56e-180 |
|
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: 516.43 E-value: 1.56e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:cd03343 22 AAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 81 EAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKvlVDINNPEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVLTVAD 160
Cdd:cd03343 102 KAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIK--VDPDDKDTLRKIAKTSLTGKGAEAAKDKLADLVVDAVLQVAE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 161 ME--RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEPPKPKTKHKLDVMSVEDYKA 238
Cdd:cd03343 180 KRdgKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAKIRITSPDQLQA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 239 LQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTSEKLGFA 318
Cdd:cd03343 260 FLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTNIDDLTPEDLGEA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 319 GVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQE 398
Cdd:cd03343 340 ELVEERKVG--DDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGAVEIELAKRLREY 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 399 ADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKESNPALGIDCLHKGSNDMQYQHVIETLIGKKQQ 478
Cdd:cd03343 418 ARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAH-EKGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQA 496
|
490
....*....|....*..
gi 1130413408 479 ISLATQMVRMILKIDDI 495
Cdd:cd03343 497 IKSATEAATMILRIDDV 513
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
1-495 |
4.41e-180 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 515.27 E-value: 4.41e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:NF041083 24 MAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAVVLAGELLK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 81 EAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKvlVDINNPEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVLTVAd 160
Cdd:NF041083 104 KAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEK--VDPDDRETLKKIAETSLTSKGVEEARDYLAEIAVKAVKQVA- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 161 mERRD----VDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEPPKPKTKHKLDVMSVEDY 236
Cdd:NF041083 181 -EKRDgkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAEIRITDPDQL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 237 KALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTSEKLG 316
Cdd:NF041083 260 QKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVTNIDDLTPEDLG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 317 FAGVVQEISFGTtkDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVS 396
Cdd:NF041083 340 YAELVEERKVGD--DKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGAPEVELAKRLR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 397 QEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKESNPALGIDCLHKGSNDMQYQHVIETLIGKK 476
Cdd:NF041083 418 EYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAH-EKGKKWAGINVFTGEVVDMWELGVIEPLRVKT 496
|
490
....*....|....*....
gi 1130413408 477 QQISLATQMVRMILKIDDI 495
Cdd:NF041083 497 QAIKSATEAATMILRIDDV 515
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
1-495 |
2.37e-169 |
|
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: 488.04 E-value: 2.37e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:TIGR02339 23 AAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 81 EAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKvlVDINNPEPLIQTAKTTLGSKVINSCHRQ-MAEIAVNAVLTVA 159
Cdd:TIGR02339 103 KAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATK--ISPEDRDLLKKIAYTSLTSKASAEVAKDkLADLVVEAVKQVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 160 DME---RRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEPPKPKTKHKLDVMSVEDY 236
Cdd:TIGR02339 181 ELRgdgKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAPLEVEKTEIDAKIRITDPDQI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 237 KALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTSEKLG 316
Cdd:TIGR02339 261 KKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVSSIDEITESDLG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 317 FAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVS 396
Cdd:TIGR02339 341 YAELVEERKVG--EDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVAGGGAVEIELALRLR 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 397 QEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEsNPALGIDCLHKGSNDMQYQHVIETLIGKK 476
Cdd:TIGR02339 419 SYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKG-NKNAGINVFTGEIEDMLELGVIEPLRVKE 497
|
490
....*....|....*....
gi 1130413408 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 |
9.77e-151 |
|
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: 440.57 E-value: 9.77e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:cd03338 15 QAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGALLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 81 EAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKvlVDINNPEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVLTVAD 160
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIP--VDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVID 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 161 MER-RDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSH-PQMPKKVVDAKIAILTCPFEPPKPKTKHKLdvmSVEDYKA 238
Cdd:cd03338 173 PATaTNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDMDNNI---VVNDYAQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 239 ---LQKYEKEKFEEMIKQIKETGANLAICQW-----GFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSEL 310
Cdd:cd03338 250 mdrILREERKYILNMCKKIKKSGCNVLLIQKsilrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVASIDHF 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 311 TSEKLGFAGVVQEISFGTtkDKMLVIEKCKNS-RAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEI 389
Cdd:cd03338 330 TEDKLGSADLVEEVSLGD--GKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGAPEI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 390 SCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKESNPALGIDCLHKGSNDMQYQHVI 469
Cdd:cd03338 408 EIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRH-AQGEKNAGINVRKGAITNILEENVV 486
|
490 500
....*....|....*....|....*.
gi 1130413408 470 ETLIGKKQQISLATQMVRMILKIDDI 495
Cdd:cd03338 487 QPLLVSTSAITLATETVRMILKIDDI 512
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
1-495 |
2.35e-136 |
|
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: 403.78 E-value: 2.35e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:TIGR02342 16 VAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGALLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 81 EAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKvlVDINNPEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVLTVAD 160
Cdd:TIGR02342 96 ACERLLNKGIHPTIISESFQSAADEAIKILDEMSIP--VDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVLKVID 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 161 MER-RDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQ-MPKKVVDAKIAILTCPFEPPKPKTKHKLdvmSVEDYKA 238
Cdd:TIGR02342 174 PENaKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDMENQI---IVNDYAQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 239 LQKYEKEK---FEEMIKQIKETGANLAICQW-----GFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSEL 310
Cdd:TIGR02342 251 MDRVLKEErayILNIVKKIKKTGCNVLLIQKsilrdAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASIDHF 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 311 TSEKLGFAGVVQEIsfGTTKDKMLVIEKCKN-SRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEI 389
Cdd:TIGR02342 331 TADKLGSAELVEEV--DSDGGKIIKITGIQNaGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPEI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 390 SCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKESNPALGIDCLHKGSNDMQYQHVI 469
Cdd:TIGR02342 409 EIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRH-ANGEKTAGISVRKGGITNMLEEHVL 487
|
490 500
....*....|....*....|....*.
gi 1130413408 470 ETLIGKKQQISLATQMVRMILKIDDI 495
Cdd:TIGR02342 488 QPLLVTTSAITLASETVRSILKIDDI 513
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
1-495 |
2.20e-121 |
|
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: 364.31 E-value: 2.20e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:cd03337 23 QAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILAGEILA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 81 EAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKvlVDINNPEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVLTVA- 159
Cdd:cd03337 103 VAEPFLERGIHPTVIIKAYRKALEDALKILEEISIP--VDVNDRAQMLKIIKSCIGTKFVSRWSDLMCNLALDAVKTVAv 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 160 --DMERRDVDFE-LIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEppkpktkhkldvmsvedY 236
Cdd:cd03337 181 eeNGRKKEIDIKrYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPLE-----------------Y 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 237 kalqkyekekfeemikqiketganLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTSEKLG 316
Cdd:cd03337 244 ------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARACGATIVNRPEELTESDVG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 317 FAGVVQEISFGtTKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVS 396
Cdd:cd03337 300 TGAGLFEVKKI-GDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILNPKLVPGGGATEMAVSHALS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 397 QEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPALGIDCLHKGSNDMQYQHVIETLIGKK 476
Cdd:cd03337 379 EKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTWGIDGETGDIVDMKELGIWDPLAVKA 458
|
490
....*....|....*....
gi 1130413408 477 QQISLATQMVRMILKIDDI 495
Cdd:cd03337 459 QTYKTAIEAACMLLRIDDI 477
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
1-495 |
4.62e-120 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 361.32 E-value: 4.62e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAG 76
Cdd:COG0459 17 RGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFenmgAQLVKEVASKTNDEAGDGTTTATVLAG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 77 ALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdkvlVDINNPEPLIQTAKTTLGSKvinschRQMAEIAVNAVL 156
Cdd:COG0459 97 ALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIA----KPVDDKEELAQVATISANGD------EEIGELIAEAME 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 157 TVADMERrdvdfelIKVEgKVGGRLEDTKLIKGVIVDKDFSHPQ-------MPKKVVDAKIAIltcpfeppkpkTKHKLD 229
Cdd:COG0459 167 KVGKDGV-------ITVE-EGKGLETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILL-----------TDKKIS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 230 VMsvedykalqkyekEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVR---WVGGP--------EIELIAIA 298
Cdd:COG0459 228 SI-------------QDLLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLrvvAVKAPgfgdrrkaMLEDIAIL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 299 TGGRIV-----PRFSELTSEKLGFAGVVQEisfgtTKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRN 373
Cdd:COG0459 295 TGGRVIsedlgLKLEDVTLDDLGRAKRVEV-----DKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALHATRA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 374 LIRDnRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRArqvkESNPALGI 453
Cdd:COG0459 370 AVEE-GIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRA----AKDKGFGF 444
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1130413408 454 DCLHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDDI 495
Cdd:COG0459 445 DAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAV 486
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
2-495 |
2.50e-115 |
|
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: 350.19 E-value: 2.50e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 2 AAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 81
Cdd:TIGR02344 24 AAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILAGEMLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 82 AEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdkVLVDINNPEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVLTVA-- 159
Cdd:TIGR02344 104 AEPFLEQNIHPTVIIRAYRKALDDALSVLEEIS--IPVDVNDDAAMLKLIQSCIGTKFVSRWSDLMCDLALDAVRTVQrd 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 160 DMERRDVDFE-LIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEPPKPKTKHKLDVMSVEDYKA 238
Cdd:TIGR02344 182 ENGRKEIDIKrYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLEYKKGESQTNIEITKEEDWNR 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 239 LQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTSEKLGF- 317
Cdd:TIGR02344 262 ILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACGATIVNRPEELRESDVGTg 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 318 AGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQ 397
Cdd:TIGR02344 342 CGLFEVKKIG--DEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKLVPGGGATEMAVSVALTE 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 398 EADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPALGIDCLHKGSNDMQYQHVIETLIGKKQ 477
Cdd:TIGR02344 420 KSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTWGIDGETGKIVDMKEKGIWEPLAVKLQ 499
|
490
....*....|....*...
gi 1130413408 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 |
9.27e-109 |
|
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: 333.14 E-value: 9.27e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 1 MAAKAVANTMRTSLGPNGLDKMM--VDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGAL 78
Cdd:cd03336 20 VGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDGTTSVTVLAAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 79 LEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVLVDINN-PEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVLT 157
Cdd:cd03336 100 LREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEAfREDLLNIARTTLSSKILTQDKEHFAELAVDAVLR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 158 VADmerrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKKVVDAKIAILTCPFEPPKPKT-KHKLDVMSVEDY 236
Cdd:cd03336 180 LKG----SGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTPMDTDKIKIfGAKVRVDSTAKV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 237 KALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTSEKLG 316
Cdd:cd03336 255 AEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTGGEIASTFDHPELVKLG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 317 FAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVS 396
Cdd:cd03336 335 TCKLIEEIMIG--EDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRVVLGGGCSEMLMAKAVE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 397 QEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPAlGIDCLHKGSNDMQYQHVIETLIGKK 476
Cdd:cd03336 413 ELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTA-GLDMRKGTVGDMKELGITESFKVKR 491
|
490 500
....*....|....*....|.
gi 1130413408 477 QQISLATQMVRMILKIDDIRK 497
Cdd:cd03336 492 QVLLSASEAAEMILRVDDIIK 512
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-495 |
8.58e-107 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 328.53 E-value: 8.58e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 1 MAAKAVANTMRTSLGPNGLDKMMV-----DKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLA 75
Cdd:PTZ00212 29 VGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGDGTTSVVVLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 76 GALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVLVDINN-PEPLIQTAKTTLGSKVINSCHRQMAEIAVNA 154
Cdd:PTZ00212 109 GELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEKfKEDLLNIARTTLSSKLLTVEKDHFAKLAVDA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 155 VLTVadmeRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKKVVDAKIAILTCPFEPPKPK---TKHKLDvm 231
Cdd:PTZ00212 189 VLRL----KGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVGQ-PKRLENCKILVANTPMDTDKIKiygAKVKVD-- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 232 SVEDYKALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELT 311
Cdd:PTZ00212 262 SMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 312 SEKLGFAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISC 391
Cdd:PTZ00212 342 KVKLGHCDLIEEIMIG--EDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKDTRVVLGGGCSEMLM 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 392 ALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPAlGIDCLHKGSNDMQYQHVIET 471
Cdd:PTZ00212 420 ANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTA-GIDMEKGTVGDMKELGITES 498
|
490 500
....*....|....*....|....
gi 1130413408 472 LIGKKQQISLATQMVRMILKIDDI 495
Cdd:PTZ00212 499 YKVKLSQLCSATEAAEMILRVDDI 522
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
2-493 |
1.27e-105 |
|
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: 325.01 E-value: 1.27e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 2 AAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 81
Cdd:cd03340 24 ACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLKE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 82 AEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdkvlVDINNPEP------LIQTAKTTLGSKVINSCHRQMAEIAVNAV 155
Cdd:cd03340 104 AKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIA----VNIDKEDKeeqrelLEKCAATALNSKLIASEKEFFAKMVVDAV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 156 LTVADmerrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFS---HPQMPKKVVDAKIAILTCPFEPPKPKTKHKLDVMS 232
Cdd:cd03340 180 LSLDD----DLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSyagFEQQPKKFKNPKILLLNVELELKAEKDNAEVRVED 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 233 VEDYKALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTS 312
Cdd:cd03340 256 PEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQTTVSNITD 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 313 EKLGFAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCA 392
Cdd:cd03340 336 DVLGTCGLFEERQVG--GERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAIEMELS 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 393 LAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPALGIDCLHKGSNDMQYQHVIETL 472
Cdd:cd03340 414 KYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKWYGVDINNEGIADNFEAFVWEPS 493
|
490 500
....*....|....*....|.
gi 1130413408 473 IGKKQQISLATQMVRMILKID 493
Cdd:cd03340 494 LVKINALTAATEAACLILSVD 514
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
1-497 |
1.43e-104 |
|
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: 322.70 E-value: 1.43e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:cd03335 15 TAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAELLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 81 EAEQLLDRGIHPIRIADGYEQAARIAIQHldkISDKVLVDINN--PEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVLTV 158
Cdd:cd03335 95 RANELVKQKIHPTTIISGYRLACKEAVKY---IKEHLSISVDNlgKESLINVAKTSMSSKIIGADSDFFANMVVDAILAV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 159 ADM-ERRDV-----DFELIKVEGKvggRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEppkpKTKHKLDV-M 231
Cdd:cd03335 172 KTTnEKGKTkypikAVNILKAHGK---SAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQ----KTKMKLGVqV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 232 SVEDYKALQKYEKEKFE---EMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFS 308
Cdd:cd03335 245 VVTDPEKLEKIRQRESDitkERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVSTLA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 309 ELTSE------KLGFAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVY 382
Cdd:cd03335 325 NLEGEetfdpsYLGEAEEVVQERIG--DDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 383 GGGAAEisCALAVSQE--ADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRAR----QVKESNPAL---GI 453
Cdd:cd03335 403 GGGAVE--TALSIYLEnfATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYhaaaQVKPDKKHLkwyGL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1130413408 454 DcLHKGS--NDMQYQhVIETLIGKKQQISLATQMVRMILKIDDIRK 497
Cdd:cd03335 481 D-LINGKvrDNLEAG-VLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
1-503 |
2.52e-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: 317.05 E-value: 2.52e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 1 MAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:TIGR02340 19 TAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVIIAAELLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 81 EAEQLLDRGIHPIRIADGYEQAARIAIQHldkISDKVLVDINN--PEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVLTV 158
Cdd:TIGR02340 99 RADELVKNKIHPTSVISGYRLACKEAVKY---IKENLSVSVDElgREALINVAKTSMSSKIIGLDSDFFSNIVVDAVLAV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 159 ADM-ERRDVDF--ELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEppkpKTKHKLDV-MSVE 234
Cdd:TIGR02340 176 KTTnENGETKYpiKAINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQ----KAKMALGVqIVVD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 235 DYKALQKYEKEKFE---EMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELT 311
Cdd:TIGR02340 252 DPEKLEQIRQREADitkERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVSTLADLE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 312 SE------KLGFAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGG 385
Cdd:TIGR02340 332 GEetfeasYLGFADEVVQERIA--DDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 386 AAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQ-------VKESNPALGIDCLHK 458
Cdd:TIGR02340 410 AVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHaaaqlkpEKKHLKWYGLDLVNG 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1130413408 459 GSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDD-IRKPGESEE 503
Cdd:TIGR02340 490 KIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDlIKLNPEQSK 535
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
2-499 |
3.98e-101 |
|
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: 313.62 E-value: 3.98e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 2 AAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 81
Cdd:TIGR02345 26 ACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGELLKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 82 AEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKV-LVDINNPEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVLTvad 160
Cdd:TIGR02345 106 AKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIdEEKGEQRELLEKCAATALSSKLISHNKEFFSKMIVDAVLS--- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 161 MERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFS---HPQMPKKVVDAKIAILTCPFEPPKPKTKHKLDVMSVEDYK 237
Cdd:TIGR02345 183 LDRDDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSyagFEQQPKKFANPKILLLNVELELKAEKDNAEIRVEDVEDYQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 238 ALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTSEKLGF 317
Cdd:TIGR02345 263 AIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTTSDLEADVLGT 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 318 AGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQ 397
Cdd:TIGR02345 343 CALFEERQIG--SERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIEMELSKCLRD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 398 EADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPAlGIDCLHKGSNDMQYQHVIETLIGKKQ 477
Cdd:TIGR02345 421 YSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWY-GVDINTEDIGDNFEAFVWEPALVKIN 499
|
490 500
....*....|....*....|...
gi 1130413408 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 |
2.86e-97 |
|
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: 301.83 E-value: 2.86e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 2 AAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 81
Cdd:cd03341 16 ACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGELLEK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 82 AEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVLVDINNPEPLIQTAKTTLGSKVI-NSCHrqMAEIAVNAVLTVAD 160
Cdd:cd03341 96 AEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLRNKEEVSKALKTAIASKQYgNEDF--LSPLVAEACISVLP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 161 MERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDfSHPQMpKKVVDAKIAILTCPFeppkpktkhkldvmsvedykalq 240
Cdd:cd03341 174 ENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKRE-PEGSV-KRVKKAKVAVFSCPF----------------------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 241 kyekekfeemikqikETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTSEKLGFAGV 320
Cdd:cd03341 229 ---------------DIGVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEEIGYCDS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 321 VQEISFGTTkdKMLVIEKCKNSRAV-TIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEA 399
Cdd:cd03341 294 VYVEEIGDT--KVVVFRQNKEDSKIaTIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAKKLKEYG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 400 DKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPA-LGIDCLHKGSNDMQYQHVIETLIGKKQQ 478
Cdd:cd03341 372 EKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAgVDIESGDEGTKDAKEAGIFDHLATKKWA 451
|
490
....*....|....*..
gi 1130413408 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 |
3.03e-96 |
|
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: 301.25 E-value: 3.03e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 2 AAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 81
Cdd:TIGR02346 26 ACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGELLNK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 82 AEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVLVDINNPEPLIQTAKTTLGSKVINScHRQMAEIAVNAVLTVADM 161
Cdd:TIGR02346 106 AEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDLRDKDELIKALKASISSKQYGN-EDFLAQLVAQACSTVLPK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 162 ERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFShpQMPKKVVDAKIAILTCPFEPPKPKTKHKLDVMSVEDYKALQK 241
Cdd:TIGR02346 185 NPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNREAE--GSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNAEELLNYSK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 242 YEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTSEKLGFAGVV 321
Cdd:TIGR02346 263 GEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPEEIGYVDSV 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 322 QEISFGTtkDKMLVIE-KCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEAD 400
Cdd:TIGR02346 343 YVSEIGG--DKVTVFKqENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELASRLTKYGE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 401 KCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQvKESNPALGID--CLHKGSNDMQYQHVIETLIGKKQQ 478
Cdd:TIGR02346 421 KLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAH-KKGNKSKGIDieAESDGVKDASEAGIYDMLATKKWA 499
|
490
....*....|....*..
gi 1130413408 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 |
1.83e-90 |
|
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: 285.99 E-value: 1.83e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 1 MAAKAVANTMRTSLGPNGLDKMMV--DKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGAL 78
Cdd:TIGR02341 21 VGAIAIGDLVKSTLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEVGDGTTSVTVLAAEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 79 LEEAEQLLDRGIHPIRIADGYEQAARIAIQHL-----DKISDKVLVDinnpEPLIQTAKTTLGSKVINSCHRQMAEIAVN 153
Cdd:TIGR02341 101 LREAEKLINQKIHPQTIIAGYREATKAARDALlksavDNGSDEVKFR----QDLMNIARTTLSSKILSQHKDHFAQLAVD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 154 AVLTVadmeRRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQmPKKVVDAKIAILTCPFEPPKPKT-KHKLDVMS 232
Cdd:TIGR02341 177 AVLRL----KGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTDKVKIfGSRVRVDS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 233 VEDYKALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTS 312
Cdd:TIGR02341 252 TAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIVSTFDHPEL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 313 EKLGFAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCA 392
Cdd:TIGR02341 332 VKLGSCDLIEEIMIG--EDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGGGCSEMLMS 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 393 LAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRArQVKESNPALGIDCLHKGSNDMQYQHVIETL 472
Cdd:TIGR02341 410 KAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRA-AHYNGNTTMGLDMNEGTIADMRQLGITESY 488
|
490 500
....*....|....*....|....*
gi 1130413408 473 IGKKQQISLATQMVRMILKIDDIRK 497
Cdd:TIGR02341 489 KVKRAVVSSAAEAAEVILRVDNIIK 513
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
2-501 |
9.64e-85 |
|
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: 271.22 E-value: 9.64e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 2 AAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 81
Cdd:TIGR02347 24 AARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 82 AEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVlVDINNPEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVLTVADM 161
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFLDKFKVKK-EDEVDREFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIKKD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 162 ErRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEPPKPKTKHKLDVMSVEDYKALQK 241
Cdd:TIGR02347 183 G-EDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQREKLVK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 242 YEKEKFEEMIKQIKE-------TGAN---LAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELT 311
Cdd:TIGR02347 262 AERKFVDDRVKKIIElkkkvcgKSPDkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEALNSVEDLT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 312 SEKLGFAGVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISC 391
Cdd:TIGR02347 342 PECLGWAGLVYETTIG--EEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAGAFEIAA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 392 ALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRArQVKESNPALGIDCLHKGSNDMQYQHVIET 471
Cdd:TIGR02347 420 YRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLED-EHDEGGEVVGVDLNTGEPIDPEIKGIWDN 498
|
490 500 510
....*....|....*....|....*....|
gi 1130413408 472 LIGKKQQISLATQMVRMILKIDDIRKPGES 501
Cdd:TIGR02347 499 YRVKKQLIQSATVIASQLLLVDEVMRAGRS 528
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
2-499 |
3.11e-83 |
|
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: 266.05 E-value: 3.11e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 2 AAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 81
Cdd:cd03342 20 AAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGELLKQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 82 AEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVLVDiNNPEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVLTVadm 161
Cdd:cd03342 100 AERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEID-TDRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAI--- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 162 ERRDVDFELIKVE-GKVGGRLE-DTKLIKGVIVDKDFSHPQMPKKVVDAkiAILTCPfeppkpktkhkldvMSVEdykal 239
Cdd:cd03342 176 YKPDEPIDLHMVEiMQMQHKSDsDTKLIRGLVLDHGARHPDMPKRVENA--YILTCN--------------VSLE----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 240 qkYEK-EKFEEMIkqiketgANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTSEKLGFA 318
Cdd:cd03342 235 --YEKtEVNSGFF-------YSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPECLGYA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 319 GVVQEISFGttKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQE 398
Cdd:cd03342 306 GLVYERTLG--EEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHLKEF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 399 ADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRaRQVKESNPALGIDCLHKGSNDMQYQHVIETLIGKKQQ 478
Cdd:cd03342 384 KKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQ-DEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQI 462
|
490 500
....*....|....*....|.
gi 1130413408 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 |
2.00e-75 |
|
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: 236.21 E-value: 2.00e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 125 EPLIQTAKTTLGSKvINSCHRQMAEIAVNAVLTVADMERrDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKK 204
Cdd:cd03333 2 ELLLQVATTSLNSK-LSSWDDFLGKLVVDAVLKVGPDNR-MDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 205 VVDAKIAILTCPFEPpkpktkhkldvmsvedykalqkyekekfeemikqiketganLAICQWGFDDEANHLLLQNGLPAV 284
Cdd:cd03333 80 LENAKILLLDCPLEY-----------------------------------------VVIAEKGIDDLALHYLAKAGIMAV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 285 RWVGGPEIELIAIATGGRIVPRFSELTSEKLGFAGVVQEISFGTtkDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSL 364
Cdd:cd03333 119 RRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGE--EKLTFIEGCKGGKAATILLRGATEVELDEVKRSL 196
|
250
....*....|...
gi 1130413408 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 |
3.28e-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: 78.42 E-value: 3.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 149 EIAVNAVLTVADMERRDVDF-------ELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEPPK 221
Cdd:cd03334 21 DILLPLVWKAASNVKPDVRAgddmdirQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 222 PKTKhkldVMSVEDYKAlqkYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGG 301
Cdd:cd03334 101 VENK----LLSLDPVIL---QEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1130413408 302 RIVPRFSEL-TSEKLGFAGVVQEISF----GTTKDKMLvIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLI 375
Cdd:cd03334 174 DIISSMDDLlTSPKLGTCESFRVRTYveehGRSKTLMF-FEGCPKELGCTILLRGGDLEELKKVKRVVEFMVFAAYHLK 251
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
3-463 |
1.36e-13 |
|
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: 72.87 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 3 AKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATI---LSMMD-VDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGAL 78
Cdd:cd03344 17 VNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVakeIELEDpFENMGAQLVKEVASKTNDVAGDGTTTATVLARAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 79 LEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdkvlVDINNPEPLIQTAKT------TLGSKVINSchrqMAEIAV 152
Cdd:cd03344 97 IKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLS----KPVKTKEEIAQVATIsangdeEIGELIAEA----MEKVGK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 153 NAVLTVADmerrdvdfelikvegkvGGRLEDT-KLIKGVIVDKDFSHPQM-----PKKVV--DAKIAIltcpfeppkpkT 224
Cdd:cd03344 169 DGVITVEE-----------------GKTLETElEVVEGMQFDRGYLSPYFvtdpeKMEVEleNPYILL-----------T 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 225 KHKLDvmSVED-YKALQkyekekfeemikQIKETGANLAICQWGFDDEANHLL----LQNGLPAVRwVGGPE-------- 291
Cdd:cd03344 221 DKKIS--SIQElLPILE------------LVAKAGRPLLIIAEDVEGEALATLvvnkLRGGLKVCA-VKAPGfgdrrkam 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 292 IELIAIATGGRIVP-----RFSELTSEKLGFAGVVQeisfgTTKDKMLVIEKCKNSRAV--------------------- 345
Cdd:cd03344 286 LEDIAILTGGTVISeelglKLEDVTLEDLGRAKKVV-----VTKDDTTIIGGAGDKAAIkariaqirkqieettsdydke 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 346 --------------TIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNrVVYGGGAAEISCALAVSQEADKCPtLEQYAMR 411
Cdd:cd03344 361 klqerlaklsggvaVIKVGGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPALDKLKALNG-DEKLGIE 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1130413408 412 AFADALEVIPMALSENSGMNPiqtmtEVRARQVKESNPALGIDCLHKGSNDM 463
Cdd:cd03344 439 IVRRALEAPLRQIAENAGVDG-----SVVVEKVLESPDGFGYDAATGEYVDM 485
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
4-175 |
3.58e-12 |
|
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES cytosolic chaperonin. It is found in bacteria, organelles derived from bacteria, and occasionally in the Archaea. The bacterial GroEL/GroES group I chaperonin is replaced a group II chaperonin, usually called the thermosome in the Archaeota and CCT (chaperone-containing TCP) in the Eukaryota. GroEL, thermosome subunits, and CCT subunits all fall under the scope of pfam00118. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274089 Cd Length: 524 Bit Score: 68.47 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 4 KAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALL 79
Cdd:TIGR02348 19 DKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFenmgAQLVKEVASKTNDVAGDGTTTATVLAQAIV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 80 EEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISdkvlVDINNPEPLIQTAKTTLGS--KVINSCHRQMAEIAVNAVLT 157
Cdd:TIGR02348 99 KEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLS----KPVKGKKEIAQVATISANNdeEIGSLIAEAMEKVGKDGVIT 174
|
170
....*....|....*...
gi 1130413408 158 VAdmERRDVDFELIKVEG 175
Cdd:TIGR02348 175 VE--ESKSLETELEVVEG 190
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
5-117 |
2.41e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 62.81 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 5 AVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKL---MV-ELSKSQDDEIGDGTTGVVVLAGALLE 80
Cdd:PRK12850 22 ILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMgaqMVkEVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110
....*....|....*....|....*....|....*..
gi 1130413408 81 EAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKV 117
Cdd:PRK12850 102 EGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKV 138
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
6-138 |
3.04e-10 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 62.63 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 6 VANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 81
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVenigAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAE 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1130413408 82 AEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKV----LVDI------NNPE--PLIQTAKTTLGSK 138
Cdd:PLN03167 158 GVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVedseLADVaavsagNNYEvgNMIAEAMSKVGRK 226
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
4-431 |
6.62e-10 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 61.47 E-value: 6.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 4 KAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATIL-------SMMDVDhqiAKLMVELSKSQDDEIGDGTTGVVVLAG 76
Cdd:PTZ00114 32 ERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAkaiefsdRFENVG---AQLIRQVASKTNDKAGDGTTTATILAR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 77 ALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVlvdiNNPEPLIQTAK-TTLGSKVINSCHRQ-MAEIAVNA 154
Cdd:PTZ00114 109 AIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPV----KTKEDILNVATiSANGDVEIGSLIADaMDKVGKDG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 155 VLTVADmerrdvdfelikvegkvGGRLEDT-KLIKGVIVDKDFSHPQMpkkVVDAK--IAILTCPFeppkpktkhkldvM 231
Cdd:PTZ00114 185 TITVED-----------------GKTLEDElEVVEGMSFDRGYISPYF---VTNEKtqKVELENPL-------------I 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 232 SVEDYKALQkyekekfeemIKQI-------KETGANLAICQWGFDDEA------NHllLQNGLP--AVRWVGGPE----- 291
Cdd:PTZ00114 232 LVTDKKISS----------IQSIlpilehaVKNKRPLLIIAEDVEGEAlqtliiNK--LRGGLKvcAVKAPGFGDnrkdi 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 292 IELIAIATGGRIVPR------FSELTSEKLGFAGVVQ-----EISFGTTKDKMLVIEKCKNSRA---------------- 344
Cdd:PTZ00114 300 LQDIAVLTGATVVSEdnvglkLDDFDPSMLGSAKKVTvtkdeTVILTGGGDKAEIKERVELLRSqierttseydkeklke 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 345 ---------VTIFIRGGNKMIIEEAKRSLHDALCVIRNLIrDNRVVYGGGAAEI--SCALAVSQEADKCPTLEQYAMRAF 413
Cdd:PTZ00114 380 rlaklsggvAVIKVGGASEVEVNEKKDRIEDALNATRAAV-EEGIVPGGGVALLraSKLLDKLEEDNELTPDQRTGVKIV 458
|
490
....*....|....*...
gi 1130413408 414 ADALEVIPMALSENSGMN 431
Cdd:PTZ00114 459 RNALRLPTKQIAENAGVE 476
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
3-117 |
1.32e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 60.53 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 3 AKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGAL 78
Cdd:PRK12851 20 VNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFenmgAQMVREVASKTNDVAGDGTTTATVLAQAI 99
|
90 100 110
....*....|....*....|....*....|....*....
gi 1130413408 79 LEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKV 117
Cdd:PRK12851 100 VREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPV 138
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
6-175 |
2.39e-09 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 59.66 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 6 VANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 81
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFenmgAQMVREVASKSADAAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 82 AEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVLVdiNNPEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVLTVAdm 161
Cdd:PRK14104 103 GAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTS--NDEIAQVGTISANGDAEIGKFLADAMKKVGNEGVITVE-- 178
|
170
....*....|....
gi 1130413408 162 ERRDVDFELIKVEG 175
Cdd:PRK14104 179 EAKSLETELDVVEG 192
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
5-175 |
4.62e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 58.66 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 5 AVANTMRTSLGPNGLDkMMVDKD-GDVTITNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALL 79
Cdd:PRK12849 21 KLADAVKVTLGPKGRN-VVIDKSfGAPTITKDGVSIAKEIELEDPFenlgAQLVKEVASKTNDVAGDGTTTATVLAQALV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 80 EEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVlvdiNNPEPLIQTAKT------TLGSKVinscHRQMAEIAVN 153
Cdd:PRK12849 100 QEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPV----SGSEEIAQVATIsangdeEIGELI----AEAMEKVGKD 171
|
170 180
....*....|....*....|..
gi 1130413408 154 AVLTVAdmERRDVDFELIKVEG 175
Cdd:PRK12849 172 GVITVE--ESKTLETELEVTEG 191
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
5-117 |
5.92e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 58.21 E-value: 5.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 5 AVANTMRTSLGPNG----LDKmmvdKDGDVTITNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAG 76
Cdd:PRK00013 21 KLADAVKVTLGPKGrnvvLEK----SFGAPTITKDGVTVAKEIELEDPFenmgAQLVKEVASKTNDVAGDGTTTATVLAQ 96
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1130413408 77 ALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKV 117
Cdd:PRK00013 97 AIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPV 137
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
6-117 |
5.78e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 55.24 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 6 VANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQI----AKLMVELSKSQDDEIGDGTTGVVVLAGALLEE 81
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFenmgAQMVREVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110
....*....|....*....|....*....|....*.
gi 1130413408 82 AEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKV 117
Cdd:PRK12852 103 GAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPV 138
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
3-115 |
1.61e-06 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 50.49 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130413408 3 AKAVANTmrtsLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVEL-----SKSqDDEIGDGTTGVVVLAGA 77
Cdd:CHL00093 23 AEAVSVT----LGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALirqaaSKT-NDVAGDGTTTATVLAYA 97
|
90 100 110
....*....|....*....|....*....|....*...
gi 1130413408 78 LLEEAEQLLDRGIHPIRIADGYEQAARIAIQhldKISD 115
Cdd:CHL00093 98 IVKQGMKNVAAGANPISLKRGIEKATQYVVS---QIAE 132
|
|
| |
