|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
9-535 |
0e+00 |
|
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: 1068.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 9 GDRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGD 88
Cdd:cd03335 1 GERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 89 GTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIVNTDELGRDCLINAAKTSMSSKIIGINGDFF 168
Cdd:cd03335 81 GTTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEHLSISVDNLGKESLINVAKTSMSSKIIGADSDFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 169 ANMVVDAVLAIKYTDTRGQPRYPVNSVNILKAHGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKL 248
Cdd:cd03335 161 ANMVVDAILAVKTTNEKGKTKYPIKAVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 249 GVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATIL 328
Cdd:cd03335 241 GVQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 329 STLANLEGEETFEAAMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSV 408
Cdd:cd03335 321 STLANLEGEETFDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 409 VPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGL 488
Cdd:cd03335 401 VPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKPDKKHLKWYGL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 383872999 489 DLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHP 535
Cdd:cd03335 481 DLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIKLNP 527
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
5-540 |
0e+00 |
|
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: 1009.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 5 LSVFGDRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDK 84
Cdd:TIGR02340 1 LFLGGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 85 EVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIVNTDELGRDCLINAAKTSMSSKIIGIN 164
Cdd:TIGR02340 81 EVGDGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKENLSVSVDELGREALINVAKTSMSSKIIGLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 165 GDFFANMVVDAVLAIKYTDTRGQPRYPVNSVNILKAHGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQKT 244
Cdd:TIGR02340 161 SDFFSNIVVDAVLAVKTTNENGETKYPIKAINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 245 KMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASG 324
Cdd:TIGR02340 241 KMALGVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 325 ATILSTLANLEGEETFEAAMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLE 404
Cdd:TIGR02340 321 ATLVSTLADLEGEETFEASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 405 SKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLK 484
Cdd:TIGR02340 401 SNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAQLKPEKKHLK 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 383872999 485 WIGLDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHPESKDD 540
Cdd:TIGR02340 481 WYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIKLNPEQSKG 536
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
9-532 |
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: 570.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 9 GDRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGD 88
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 89 GTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIvNTDELGRDCLINAAKTSMSSKIIGINGDFF 168
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAV-PIDVEDREELLKVATTSLNSKLVSGGDDFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 169 ANMVVDAVLAIKytdtRGQPRYPVNSVNILKAHGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQktkmkl 248
Cdd:cd00309 160 GELVVDAVLKVG----KENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLE------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 249 gvqvvitdpekldqirqresditkeriqkilatgaNVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATIL 328
Cdd:cd00309 230 -----------------------------------YVVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 329 STLanlegeETFEAAMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSV 408
Cdd:cd00309 275 SRL------EDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 409 VPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQvnperknlKWIGL 488
Cdd:cd00309 349 VPGGGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGG--------GNAGG 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 383872999 489 DLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIK 532
Cdd:cd00309 421 DVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
28-532 |
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: 557.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 28 IANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADEL 107
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 108 VKQKIHPTSVISGYRLACKEAVRYINENLIVNTDELGRDCLINAAKTSMSSKIIGINGDFFANMVVDAVLAIKYTDTrgq 187
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDG--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 188 pRYPVNSVNILKAHGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRE 267
Cdd:pfam00118 158 -SFDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 268 SDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATILSTLANLEGEEtfeaamLGQ 347
Cdd:pfam00118 237 EEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDD------LGT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 348 AEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGGGAVEAALSIYLENYA 427
Cdd:pfam00118 311 AGKVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 428 TSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNeaqvnperKNLKWIGLDLSNGKPRDNKQAGVFEPT 507
Cdd:pfam00118 391 KSVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHA--------SGEKHAGIDVETGEIIDMKEAGVVDPL 462
|
490 500
....*....|....*....|....*
gi 383872999 508 IVKVKSLKFATEAAITILRIDDLIK 532
Cdd:pfam00118 463 KVKRQALKSATEAASTILRIDDIIK 487
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
11-531 |
1.77e-174 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 503.26 E-value: 1.77e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 11 RSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGT 90
Cdd:NF041082 12 RTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 91 TSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINEnLIVNTDELGRDCLINAAKTSMSSKIIGINGDFFAN 170
Cdd:NF041082 92 TTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDE-IAIKVDPDDKETLKKIAATAMTGKGAEAAKDKLAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 171 MVVDAVLAIkyTDTRGQPRYPVNSVNILKAHGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGV 250
Cdd:NF041082 171 LVVDAVKAV--AEKDGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 251 QVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATILST 330
Cdd:NF041082 249 KISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 331 LANLEGEEtfeaamLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVP 410
Cdd:NF041082 329 IDDLSPED------LGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 411 GGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNeaqvnperKNLKWIGLDL 490
Cdd:NF041082 403 GGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHE--------KGNKTAGLDV 474
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 383872999 491 SNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLI 531
Cdd:NF041082 475 YTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVI 515
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
11-531 |
8.93e-172 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 496.39 E-value: 8.93e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 11 RSTG-EAIRSqNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDG 89
Cdd:NF041083 12 RTKGrDAQRN-NIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 90 TTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINEnLIVNTDELGRDCLINAAKTSMSSKIIGINGDFFA 169
Cdd:NF041083 91 TTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDE-IAEKVDPDDRETLKKIAETSLTSKGVEEARDYLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 170 NMVVDAVLAIkyTDTRGQpRYPV--NSVNILKAHGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMK 247
Cdd:NF041083 170 EIAVKAVKQV--AEKRDG-KYYVdlDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 248 LGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATI 327
Cdd:NF041083 247 IDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 328 LSTLANLEGEEtfeaamLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKS 407
Cdd:NF041083 327 VTNIDDLTPED------LGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 408 VVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQvnperknlKWIG 487
Cdd:NF041083 401 IVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGK--------KWAG 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 383872999 488 LDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLI 531
Cdd:NF041083 473 INVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVI 516
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
11-532 |
5.71e-170 |
|
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: 491.78 E-value: 5.71e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 11 RSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGT 90
Cdd:cd03343 10 RTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 91 TSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYInENLIVNTDELGRDCLINAAKTSMSSKIIGINGDFFAN 170
Cdd:cd03343 90 TTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELL-DEIAIKVDPDDKDTLRKIAKTSLTGKGAEAAKDKLAD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 171 MVVDAVLAIKyTDTRGQPRYPVNSVNILKAHGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGV 250
Cdd:cd03343 169 LVVDAVLQVA-EKRDGKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 251 QVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATILST 330
Cdd:cd03343 248 KIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTN 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 331 LANLEGEEtfeaamLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVP 410
Cdd:cd03343 328 IDDLTPED------LGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 411 GGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNeaqvnperKNLKWIGLDL 490
Cdd:cd03343 402 GGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHE--------KGNKNAGLDV 473
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 383872999 491 SNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIK 532
Cdd:cd03343 474 YTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIA 515
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
11-531 |
6.40e-161 |
|
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: 468.78 E-value: 6.40e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 11 RSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGT 90
Cdd:TIGR02339 11 RTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 91 TSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYInENLIVNTDELGRDCLINAAKTSMSSK-IIGINGDFFA 169
Cdd:TIGR02339 91 TTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEII-DEIATKISPEDRDLLKKIAYTSLTSKaSAEVAKDKLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 170 NMVVDAVLAIKYTDTRGQPRYPVNSVNILKAHGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLG 249
Cdd:TIGR02339 170 DLVVEAVKQVAELRGDGKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAPLEVEKTEID 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 250 VQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATILS 329
Cdd:TIGR02339 250 AKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 330 TLANLEGEEtfeaamLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVV 409
Cdd:TIGR02339 330 SIDEITESD------LGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 410 PGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNeaqvnperKNLKWIGLD 489
Cdd:TIGR02339 404 AGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHE--------KGNKNAGIN 475
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 383872999 490 LSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLI 531
Cdd:TIGR02339 476 VFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVI 517
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
10-537 |
1.61e-145 |
|
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: 429.40 E-value: 1.61e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 10 DRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDG 89
Cdd:cd03340 10 DTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 90 TTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINE---NLIVNTDELGRDCLINAAKTSMSSKIIGINGD 166
Cdd:cd03340 90 TTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEiavNIDKEDKEEQRELLEKCAATALNSKLIASEKE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 167 FFANMVVDAVLAIKYTDtrgqpryPVNSVNILKAHGRSQMESMLISG--------YAlncvvGSQGMPKRIVNAKIACLD 238
Cdd:cd03340 170 FFAKMVVDAVLSLDDDL-------DLDMIGIKKVPGGSLEDSQLVNGvafkktfsYA-----GFEQQPKKFKNPKILLLN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 239 FSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKR 318
Cdd:cd03340 238 VELELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 319 IAKASGATILSTLANLEGEetfeaaMLGQAEEVVQERICDDELILIKN-TKARTsASIILRGANDFMCDEMERSLHDALC 397
Cdd:cd03340 318 VAQATGGSIQTTVSNITDD------VLGTCGLFEERQVGGERYNIFTGcPKAKT-CTIILRGGAEQFIEEAERSLHDAIM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 398 VVKRVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVn 477
Cdd:cd03340 391 IVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGG- 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 478 perknlKWIGLDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLhPES 537
Cdd:cd03340 470 ------KWYGVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLILSVDETIKN-PKS 522
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
10-533 |
2.01e-124 |
|
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: 375.25 E-value: 2.01e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 10 DRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDG 89
Cdd:TIGR02345 12 DTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 90 TTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIVNTDELG--RDCLINAAKTSMSSKIIGINGDF 167
Cdd:TIGR02345 92 TTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKGeqRELLEKCAATALSSKLISHNKEF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 168 FANMVVDAVLAIKYTDTRgqprypVNSVNILKAHGRSQMESMLISGYALN---CVVGSQGMPKRIVNAKIACLDFSLQKT 244
Cdd:TIGR02345 172 FSKMIVDAVLSLDRDDLD------LKLIGIKKVQGGALEDSQLVNGVAFKktfSYAGFEQQPKKFANPKILLLNVELELK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 245 KMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASG 324
Cdd:TIGR02345 246 AEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 325 ATILSTLANLEGEetfeaaMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLE 404
Cdd:TIGR02345 326 GSIQSTTSDLEAD------VLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 405 SKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNeaqvnperKNLK 484
Cdd:TIGR02345 400 NKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHA--------KGGK 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 383872999 485 WIGLDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKL 533
Cdd:TIGR02345 472 WYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITN 520
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
14-535 |
3.31e-121 |
|
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: 367.04 E-value: 3.31e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 14 GEAIRSQNVMAAASIANIVKSSLGPVGLDKML--VDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTT 91
Cdd:cd03336 11 GETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDGTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 92 SVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIVNTD--ELGRDCLINAAKTSMSSKIIGINGDFFA 169
Cdd:cd03336 91 SVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSdeEAFREDLLNIARTTLSSKILTQDKEHFA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 170 NMVVDAVLAIKytdtrgqPRYPVNSVNILKAHGRSQMESMLISGYALNCVVGSqGMPKRIVNAKIACLDFSLQKTKMKL- 248
Cdd:cd03336 171 ELAVDAVLRLK-------GSGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGV-NQPKRIENAKILIANTPMDTDKIKIf 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 249 GVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATIL 328
Cdd:cd03336 243 GAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTGGEIA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 329 STLANLegeetfEAAMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSV 408
Cdd:cd03336 323 STFDHP------ELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 409 VPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNeaqvnperKNLKWIGL 488
Cdd:cd03336 397 VLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHY--------NGNTTAGL 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 383872999 489 DLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHP 535
Cdd:cd03336 469 DMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKCAP 515
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
14-535 |
4.87e-121 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 367.05 E-value: 4.87e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 14 GEAIRSQNVMAAASIANIVKSSLGPVGLDKMLV-----DDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGD 88
Cdd:PTZ00212 20 GETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 89 GTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIVNT--DELGRDCLINAAKTSMSSKIIGINGD 166
Cdd:PTZ00212 100 GTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGsdEEKFKEDLLNIARTTLSSKLLTVEKD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 167 FFANMVVDAVLAIKYTDTrgqprypVNSVNILKAHGRSQMESMLISGYALNCVVGSqGMPKRIVNAKIACLDFSLQKTKM 246
Cdd:PTZ00212 180 HFAKLAVDAVLRLKGSGN-------LDYIQIIKKPGGTLRDSYLEDGFILEKKIGV-GQPKRLENCKILVANTPMDTDKI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 247 KL-GVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGA 325
Cdd:PTZ00212 252 KIyGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 326 TILSTLanlegeETFEAAMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLES 405
Cdd:PTZ00212 332 EIVSTF------DTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 406 KSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNperknlkw 485
Cdd:PTZ00212 406 TRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKT-------- 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 383872999 486 IGLDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHP 535
Cdd:PTZ00212 478 AGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRCAP 527
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
10-531 |
8.46e-121 |
|
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: 365.84 E-value: 8.46e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 10 DRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDG 89
Cdd:cd03338 2 DKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 90 TTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINEnLIVNTDELGRDCLINAAKTSMSSKIIGINGDFFA 169
Cdd:cd03338 82 TTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDS-MSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 170 NMVVDAVLAIkyTDTRGQPRYPVNSVNILKAHGRSQMESMLISGYALNC-VVGSQGMPKRIVNAKIACLDFSLQKTKMKL 248
Cdd:cd03338 161 PIAVDAVLKV--IDPATATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQkASKKAGGPTRIEKAKIGLIQFCLSPPKTDM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 249 GVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGI-----DDMCLKYFVEAGAMAVRRVLKRDLKRIAKAS 323
Cdd:cd03338 239 DNNIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 324 GATilsTLANLEGeetFEAAMLGQAEEVVQERICDDELILIKNTK-ARTSASIILRGANDFMCDEMERSLHDALCVVKRV 402
Cdd:cd03338 319 GCK---PVASIDH---FTEDKLGSADLVEEVSLGDGKIVKITGVKnPGKTVTILVRGSNKLVLDEAERSLHDALCVIRCL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 403 LESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHneAQVNperkn 482
Cdd:cd03338 393 VKKRALIPGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRH--AQGE----- 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 383872999 483 lKWIGLDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLI 531
Cdd:cd03338 466 -KNAGINVRKGAITNILEENVVQPLLVSTSAITLATETVRMILKIDDIV 513
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
11-532 |
1.08e-116 |
|
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: 355.45 E-value: 1.08e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 11 RSTG-EAIRSqNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDG 89
Cdd:cd03339 18 RLKGlEAHKS-HILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 90 TTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINE-NLIVNTDELGRDCLINAAKTSMSSKIIGINGDFF 168
Cdd:cd03339 97 TTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEiADKIEFSPDNKEPLIQTAMTSLGSKIVSRCHRQF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 169 ANMVVDAVLAIKYTDtrgqpRYPVN--SVNILKAHGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKM 246
Cdd:cd03339 177 AEIAVDAVLSVADLE-----RKDVNfeLIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIAILTCPFEPPKP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 247 KLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGAT 326
Cdd:cd03339 252 KTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 327 ILSTLANLEGEEtfeaamLGQAeEVVQER---ICDDELILI---KNTKARTsasIILRGANDFMCDEMERSLHDALCVVK 400
Cdd:cd03339 332 IVPRFEDLSPEK------LGKA-GLVREIsfgTTKDKMLVIegcPNSKAVT---IFIRGGNKMIIEEAKRSLHDALCVVR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 401 RVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAfhneAQVNPER 480
Cdd:cd03339 402 NLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKA----RQVKEKN 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 383872999 481 KNLkwiGLDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIK 532
Cdd:cd03339 478 PHL---GIDCLGRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
15-532 |
9.89e-111 |
|
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: 340.63 E-value: 9.89e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 15 EAIRSqNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVV 94
Cdd:TIGR02343 27 EAKKS-NIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 95 IIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINE-NLIVNTDELGRDCLINAAKTSMSSKIIGINGDFFANMVV 173
Cdd:TIGR02343 106 VLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEiSDEISADNNNREPLIQAAKTSLGSKIVSKCHRRFAEIAV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 174 DAVLAIKYTDtrgqpRYPVNS--VNILKAHGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQ 251
Cdd:TIGR02343 186 DAVLNVADME-----RRDVDFdlIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAILTCPFEPPKPKTKHK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 252 VVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATILSTL 331
Cdd:TIGR02343 261 LDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPRF 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 332 ANLEGEEtfeaamLGQAEEVVQERI--CDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVV 409
Cdd:TIGR02343 341 QELSKDK------LGKAGLVREISFgtTKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 410 PGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEaQVNPErknlkwIGLD 489
Cdd:TIGR02343 415 YGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLK-EKNPN------LGVD 487
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 383872999 490 LSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIK 532
Cdd:TIGR02343 488 CLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVIS 530
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
14-541 |
3.30e-109 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 335.12 E-value: 3.30e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 14 GEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKVLCELADLQDKEVGDG 89
Cdd:COG0459 8 GEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 90 TTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLI-VNTDELgrdcLINAAKTSMSSKiigingDFF 168
Cdd:COG0459 88 TTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKpVDDKEE----LAQVATISANGD------EEI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 169 ANMVVDAVLAIkytdtrGQprypvNSVNILKAHGRSQMESMLISGYALN-------CVVGSQGMPKRIVNAKIAcldfsl 241
Cdd:COG0459 158 GELIAEAMEKV------GK-----DGVITVEEGKGLETELEVVEGMQFDkgylspyFVTDPEKMPAELENAYIL------ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 242 qktkmklgvqvvITDpEKLDQIRQResditKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVL--------- 312
Cdd:COG0459 221 ------------LTD-KKISSIQDL-----LPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVavkapgfgd 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 313 --KRDLKRIAKASGATILSTLANLEGEETfEAAMLGQAEEVVQEricDDELILIKNTKARTSASIILRGANDFMCDEMER 390
Cdd:COG0459 283 rrKAMLEDIAILTGGRVISEDLGLKLEDV-TLDDLGRAKRVEVD---KDNTTIVEGAGNPKAIVILVGAATEVEVKERKR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 391 SLHDALCVVKRVLESKsVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAf 470
Cdd:COG0459 359 RVEDALHATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRA- 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383872999 471 hneaqvnperKNLKWIGLDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHPESKDDK 541
Cdd:COG0459 437 ----------AKDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
8-531 |
3.85e-108 |
|
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: 333.29 E-value: 3.85e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 8 FGDRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVG 87
Cdd:TIGR02342 1 FQDKDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 88 DGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINEnLIVNTDELGRDCLINAAKTSMSSKIIGINGDF 167
Cdd:TIGR02342 81 DGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDE-MSIPVDLSDREQLLKSATTSLSSKVVSQYSSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 168 FANMVVDAVLAIkyTDTRGQPRYPVNSVNILKAHGRSQMESMLISGYAL-NCVVGSQGMPKRIVNAKIACLDFSLQKTKM 246
Cdd:TIGR02342 160 LAPLAVDAVLKV--IDPENAKNVDLNDIKVVKKLGGTIDDTELIEGLVFtQKASKSAGGPTRIEKAKIGLIQFQISPPKT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 247 KLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGI-----DDMCLKYFVEAGAMAVRRVLKRDLKRIAK 321
Cdd:TIGR02342 238 DMENQIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 322 ASGATILSTLanlegeETFEAAMLGQAEEVvqERICDDELILIKNT---KARTSASIILRGANDFMCDEMERSLHDALCV 398
Cdd:TIGR02342 318 TIGCKPIASI------DHFTADKLGSAELV--EEVDSDGGKIIKITgiqNAGKTVTVVVRGSNKLVIDEAERSLHDALCV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 399 VKRVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQvnp 478
Cdd:TIGR02342 390 IRCLVKKRGLIAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGE--- 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 383872999 479 erknlKWIGLDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLI 531
Cdd:TIGR02342 467 -----KTAGISVRKGGITNMLEEHVLQPLLVTTSAITLASETVRSILKIDDIV 514
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
11-531 |
4.05e-104 |
|
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: 321.55 E-value: 4.05e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 11 RSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGT 90
Cdd:cd03337 11 RESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 91 TSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYInENLIVNTDELGRDCLINAAKTSMSSKIIGINGDFFAN 170
Cdd:cd03337 91 TSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKIL-EEISIPVDVNDRAQMLKIIKSCIGTKFVSRWSDLMCN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 171 MVVDAVLAIKYTDtrGQPRYPV---NSVNILKAHGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQktkmk 247
Cdd:cd03337 170 LALDAVKTVAVEE--NGRKKEIdikRYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPLE----- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 248 lgvQVVITdpEKldqirqresditkeriqkilatganvilttgGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATI 327
Cdd:cd03337 243 ---YLVIT--EK-------------------------------GVSDLAQHYLVKAGITALRRVRKTDNNRIARACGATI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 328 LSTLANLEGEETFEAAMLgqaEEVvqeRICDDE----LILIKNTKArtsASIILRGANDFMCDEMERSLHDALCVVKRVL 403
Cdd:cd03337 287 VNRPEELTESDVGTGAGL---FEV---KKIGDEyftfITECKDPKA---CTILLRGASKDVLNEVERNLQDAMAVARNII 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 404 ESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQvnperkNL 483
Cdd:cd03337 358 LNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGE------NS 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 383872999 484 KWiGLDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLI 531
Cdd:cd03337 432 TW-GIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
5-531 |
2.55e-103 |
|
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: 320.92 E-value: 2.55e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 5 LSVFGDRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDK 84
Cdd:TIGR02344 5 LNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 85 EVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINE-NLIVNTDElgRDCLINAAKTSMSSKIIGI 163
Cdd:TIGR02344 85 EVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEiSIPVDVND--DAAMLKLIQSCIGTKFVSR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 164 NGDFFANMVVDAVLAIKYTdtrGQPRYPVN---SVNILKAHGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFS 240
Cdd:TIGR02344 163 WSDLMCDLALDAVRTVQRD---ENGRKEIDikrYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 241 LQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIA 320
Cdd:TIGR02344 240 LEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 321 KASGATILSTLANLEGEETFEAAMLGQAeevvqERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVK 400
Cdd:TIGR02344 320 RACGATIVNRPEELRESDVGTGCGLFEV-----KKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVAR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 401 RVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAqvnper 480
Cdd:TIGR02344 395 NVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQE------ 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 383872999 481 kNLKWIGLDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLI 531
Cdd:TIGR02344 469 -NNCTWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
9-538 |
1.19e-98 |
|
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: 308.71 E-value: 1.19e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 9 GDRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDD--IGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEV 86
Cdd:TIGR02341 7 ADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSssDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 87 GDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIVNTDELG--RDCLINAAKTSMSSKIIGIN 164
Cdd:TIGR02341 87 GDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVkfRQDLMNIARTTLSSKILSQH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 165 GDFFANMVVDAVLAIKYTDTrgqprypVNSVNILKAHGRSQMESMLISGYALNCVVGSQgMPKRIVNAKIACLDFSLQKT 244
Cdd:TIGR02341 167 KDHFAQLAVDAVLRLKGSGN-------LEAIQIIKKLGGSLADSYLDEGFLLDKKIGVN-QPKRIENAKILIANTGMDTD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 245 KMKL-GVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKAS 323
Cdd:TIGR02341 239 KVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 324 GATILSTLanlegeETFEAAMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVL 403
Cdd:TIGR02341 319 GGEIVSTF------DHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 404 ESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNperknl 483
Cdd:TIGR02341 393 KESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTT------ 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 383872999 484 kwIGLDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHPESK 538
Cdd:TIGR02341 467 --MGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPRKR 519
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
21-531 |
3.30e-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: 303.37 E-value: 3.30e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 21 NVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAEL 100
Cdd:cd03341 13 NIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 101 LKNADELVKQKIHPTSVISGYRLACKEAVRyINENLIVNTDELGRDC--LINAAKTSMSSKIIGiNGDFFANMVVDAVLA 178
Cdd:cd03341 93 LEKAEELLRMGLHPSEIIEGYEKALKKALE-ILEELVVYKIEDLRNKeeVSKALKTAIASKQYG-NEDFLSPLVAEACIS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 179 IKYTDTRgqpRYPVNSVNILKAHGRSQMESMLISGYALNcvVGSQGMPKRIVNAKIAcldfslqktkmklgvqvVITDPe 258
Cdd:cd03341 171 VLPENIG---NFNVDNIRVVKILGGSLEDSKVVRGMVFK--REPEGSVKRVKKAKVA-----------------VFSCP- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 259 kldqirqresditkeriqkiLATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATILSTLANLEGEE 338
Cdd:cd03341 228 --------------------FDIGVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 339 tfeaamLGQAEEVVQERICDDELILIKNTKARTS-ASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGGGAVEA 417
Cdd:cd03341 288 ------IGYCDSVYVEEIGDTKVVVFRQNKEDSKiATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 418 ALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNperknlkwIGLDLSNGKP-- 495
Cdd:cd03341 362 ELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKS--------AGVDIESGDEgt 433
|
490 500 510
....*....|....*....|....*....|....*.
gi 383872999 496 RDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLI 531
Cdd:cd03341 434 KDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
20-535 |
8.61e-95 |
|
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: 299.32 E-value: 8.61e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 20 QNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAE 99
Cdd:TIGR02346 22 KNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 100 LLKNADELVKQKIHPTSVISGYRLACKEAVRYINEnLIVNT--DELGRDCLINAAKTSMSSKIIGiNGDFFANMVVDAVL 177
Cdd:TIGR02346 102 LLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEE-LVVWEvkDLRDKDELIKALKASISSKQYG-NEDFLAQLVAQACS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 178 AIKYTDtrgQPRYPVNSVNILKAHGRSQMESMLISGYALNcvVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDP 257
Cdd:TIGR02346 180 TVLPKN---PQNFNVDNIRVCKILGGSLSNSEVLKGMVFN--REAEGSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 258 EKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATILSTLANLEGE 337
Cdd:TIGR02346 255 EELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 338 EtfeaamLGQAEEVVQERICDDELILIKNTKARTS-ASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGGGAVE 416
Cdd:TIGR02346 335 E------IGYVDSVYVSEIGGDKVTVFKQENGDSKiSTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 417 AALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNeaqvnperKNLKWIGLDLSNGKPR 496
Cdd:TIGR02346 409 IELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHK--------KGNKSKGIDIEAESDG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 383872999 497 --DNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHP 535
Cdd:TIGR02346 481 vkDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKP 521
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
15-532 |
2.73e-87 |
|
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: 279.70 E-value: 2.73e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 15 EAIRSQ-----NVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDG 89
Cdd:TIGR02347 10 ESLRRDaalmmNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 90 TTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIVNTDELGRDCLINAAKTSMSSKIIGINGDFFA 169
Cdd:TIGR02347 90 TTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEVDREFLLNVARTSLRTKLPADLADQLT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 170 NMVVDAVLAIKytdtRGQPRYPVNSVNILKAHGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLG 249
Cdd:TIGR02347 170 EIVVDAVLAIK----KDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 250 VQVVITDPEKLDQIRQRESDITKERIQKIL-------ATGAN---VILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRI 319
Cdd:TIGR02347 246 SGFFYSSAEQREKLVKAERKFVDDRVKKIIelkkkvcGKSPDkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 320 AKASGATILSTLANLEGEEtfeaamLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVV 399
Cdd:TIGR02347 326 TLACGGEALNSVEDLTPEC------LGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 400 KRVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQvnpe 479
Cdd:TIGR02347 400 KNAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGG---- 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 383872999 480 rknlKWIGLDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIK 532
Cdd:TIGR02347 476 ----EVVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMR 524
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
21-532 |
1.01e-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: 271.44 E-value: 1.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 21 NVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAEL 100
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 101 LKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIVNTDELGRDCLINAAKTSMSSKIIGINGDFFANMVVDAVLAIK 180
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 181 ytdtrgQPRYPV--NSVNILKAHGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKmklgvqvvitdpe 258
Cdd:cd03342 177 ------KPDEPIdlHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEK------------- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 259 kldqirqreSDITKERIQKilatganVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATILSTLANLEGEE 338
Cdd:cd03342 238 ---------TEVNSGFFYS-------VVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPEC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 339 tfeaamLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGGGAVEAA 418
Cdd:cd03342 302 ------LGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 419 LSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPerknlkwiGLDLSNGKPRDN 498
Cdd:cd03342 376 LYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVG--------GVDLDTGEPMDP 447
|
490 500 510
....*....|....*....|....*....|....
gi 383872999 499 KQAGVFEPTIVKVKSLKFATEAAITILRIDDLIK 532
Cdd:cd03342 448 ESEGIWDNYSVKRQILHSATVIASQLLLVDEIIR 481
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
145-405 |
1.35e-66 |
|
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: 215.02 E-value: 1.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 145 RDCLINAAKTSMSSKIIGiNGDFFANMVVDAVLAIKYTDtrgqPRYPVNSVNILKAHGRSQMESMLISGYALNCVVGSQG 224
Cdd:cd03333 1 RELLLQVATTSLNSKLSS-WDDFLGKLVVDAVLKVGPDN----RMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 225 MPKRIVNAKIACLDFSLQktkmklgvqvvitdpekldqirqresditkeriqkilatgaNVILTTGGIDDMCLKYFVEAG 304
Cdd:cd03333 76 MPKRLENAKILLLDCPLE-----------------------------------------YVVIAEKGIDDLALHYLAKAG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 305 AMAVRRVLKRDLKRIAKASGATILSTLanlegeETFEAAMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFM 384
Cdd:cd03333 115 IMAVRRVKKEDLERIARATGATIVSSL------EDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVE 188
|
250 260
....*....|....*....|.
gi 383872999 385 CDEMERSLHDALCVVKRVLES 405
Cdd:cd03333 189 LDEVKRSLHDALCAVRAAVEE 209
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
183-424 |
6.09e-13 |
|
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: 69.17 E-value: 6.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 183 DTR-GQPRYPVNSVNILKAHGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLqktkmklGVQVVITDPEKLD 261
Cdd:cd03334 37 DVRaGDDMDIRQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPL-------EYQRVENKLLSLD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 262 QIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATILSTLANLegeetFE 341
Cdd:cd03334 110 PVILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDL-----LT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 342 AAMLGQAEEVVQERICDDE-----LILIKNTKARTSASIILRGANdfmcdemerslHDALCVVKRVLESksvvpgggAVE 416
Cdd:cd03334 185 SPKLGTCESFRVRTYVEEHgrsktLMFFEGCPKELGCTILLRGGD-----------LEELKKVKRVVEF--------MVF 245
|
....*...
gi 383872999 417 AALSIYLE 424
Cdd:cd03334 246 AAYHLKLE 253
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
28-135 |
1.75e-08 |
|
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: 57.08 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 28 IANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKVLCELADLQDKEVGDGTTSVVIIAAELLKN 103
Cdd:cd03344 20 LADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLARAIIKE 99
|
90 100 110
....*....|....*....|....*....|..
gi 383872999 104 ADELVKQKIHPTSVISGYRLACKEAVRYINEN 135
Cdd:cd03344 100 GLKAVAAGANPMDLKRGIEKAVEAVVEELKKL 131
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
28-135 |
5.45e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 55.49 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 28 IANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKVLCELADLQDKEVGDGTTSVVIIAAELLKN 103
Cdd:PRK12850 23 LANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110
....*....|....*....|....*....|..
gi 383872999 104 ADELVKQKIHPTSVISGYRLACKEAVRYINEN 135
Cdd:PRK12850 103 GAKLVAAGMNPMDLKRGIDLAVAAVVDELKKI 134
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
28-135 |
4.18e-07 |
|
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: 52.68 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 28 IANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKVLCELADLQDKEVGDGTTSVVIIAAELLKN 103
Cdd:TIGR02348 21 LADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVASKTNDVAGDGTTTATVLAQAIVKE 100
|
90 100 110
....*....|....*....|....*....|..
gi 383872999 104 ADELVKQKIHPTSVISGYRLACKEAVRYINEN 135
Cdd:TIGR02348 101 GLKNVAAGANPIELKRGIEKAVEAVVEELKKL 132
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
15-130 |
1.79e-06 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 50.51 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 15 EAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKVLCELADLQDKEVGDGT 90
Cdd:PRK12851 10 VEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGT 89
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 383872999 91 TSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVR 130
Cdd:PRK12851 90 TTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVE 129
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
28-155 |
3.45e-06 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 49.91 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 28 IANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPA----AKVLCELADLQDKEVGDGTTSVVIIAAELLKN 103
Cdd:PTZ00114 34 LADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKAGDGTTTATILARAIFRE 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 383872999 104 ADELVKQKIHPTSVISGYRLACKEAVRYINENLI-VNTDELgrdcLINAAKTS 155
Cdd:PTZ00114 114 GCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRpVKTKED----ILNVATIS 162
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
29-97 |
5.47e-06 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 49.03 E-value: 5.47e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383872999 29 ANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKVLCELAdLQDKEV-GDGTTSVVIIA 97
Cdd:PRK12849 23 ADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVA-SKTNDVaGDGTTTATVLA 95
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
28-120 |
2.59e-05 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 46.84 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 28 IANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKVLCELADLQDKEVGDGTTSVVIIAAELLKN 103
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAE 157
|
90
....*....|....*..
gi 383872999 104 ADELVKQKIHPTSVISG 120
Cdd:PLN03167 158 GVKVVAAGANPVQITRG 174
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
28-103 |
1.87e-04 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 44.34 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 28 IANIVKSSLGP----VGLDKmlvdDIGDVTITNDGATILKLLEVEHP----AAKVLCELADLQDKEVGDGTTSVVIIAA- 98
Cdd:PRK00013 22 LADAVKVTLGPkgrnVVLEK----SFGAPTITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLAQa 97
|
....*...
gi 383872999 99 ---ELLKN 103
Cdd:PRK00013 98 ivrEGLKN 105
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
18-525 |
4.04e-03 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 40.09 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 18 RSQNVMAAAsianiVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKV---LCELADLQDKEV-GDGTTSV 93
Cdd:CHL00093 17 RGMDILAEA-----VSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTgvaLIRQAASKTNDVaGDGTTTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 94 VIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENL--IVNTDELGRDCLINAAKTSMSSKIIginGDFFANM 171
Cdd:CHL00093 92 TVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYArpVEDIQAITQVASISAGNDEEVGSMI---ADAIEKV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 172 VVDAVLAIKytdtRGQprypvNSVNILKAHGRSQMESMLISGYAlncVVGSQGMPKRIVNAKIACLDfslqkTKMKLGVQ 251
Cdd:CHL00093 169 GREGVISLE----EGK-----STVTELEITEGMRFEKGFISPYF---VTDTERMEVVQENPYILLTD-----KKITLVQQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 252 VVITDPEKLDQIRqRESDITKERIQK-ILATgaNVILTTGGIDDMCLkyfVEAGAMAVRRvlKRDLKRIAKASGATILST 330
Cdd:CHL00093 232 DLLPILEQVTKTK-RPLLIIAEDVEKeALAT--LVLNKLRGIVNVVA---VRAPGFGDRR--KAMLEDIAILTGGQVITE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 331 LANLEgEETFEAAMLGQAEEVVQER-----ICDDELILIKN-------------------------TKARTSASIILRGA 380
Cdd:CHL00093 304 DAGLS-LETIQLDLLGQARRIIVTKdsttiIADGNEEQVKArceqlrkqieiadssyekeklqerlAKLSGGVAVIKVGA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872999 381 --NDFMCDEMERsLHDALCVVKRVLEsKSVVPGGGAVEAALSIYLENYA-TSMGSREQLAIAEFARSLLVIPNTLAVNAA 457
Cdd:CHL00093 383 atETEMKDKKLR-LEDAINATKAAVE-EGIVPGGGATLVHLSENLKTWAkNNLKEDELIGALIVARAILAPLKRIAENAG 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 383872999 458 QDSTDLVAKLRAFHNEaqvnperknlkwIGLDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITIL 525
Cdd:CHL00093 461 KNGSVIIEKVQEQDFE------------IGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMIL 516
|
|
| |
