|
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: 1062.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 9 GDRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGD 88
Cdd:cd03335 1 GERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 89 GTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIINTDELGRDCLINAAKTSMSSKIIGINGDFF 168
Cdd:cd03335 81 GTTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEHLSISVDNLGKESLINVAKTSMSSKIIGADSDFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 169 ANMVVDAVLAVKYTDIRGQPRYPVNSVNILKAHGRSQIESMLINGYALNCVVGSQGMLKRIVNAKIACLDFSLQKTKMKL 248
Cdd:cd03335 161 ANMVVDAILAVKTTNEKGKTKYPIKAVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 249 GVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGASIL 328
Cdd:cd03335 241 GVQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 329 STLANLEGEETFEATMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSV 408
Cdd:cd03335 321 STLANLEGEETFDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 409 VPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGL 488
Cdd:cd03335 401 VPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKPDKKHLKWYGL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 6981642 489 DLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHP 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: 1003.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 5 LSVFGDRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDK 84
Cdd:TIGR02340 1 LFLGGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 85 EVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIINTDELGRDCLINAAKTSMSSKIIGIN 164
Cdd:TIGR02340 81 EVGDGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKENLSVSVDELGREALINVAKTSMSSKIIGLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 165 GDFFANMVVDAVLAVKYTDIRGQPRYPVNSVNILKAHGRSQIESMLINGYALNCVVGSQGMLKRIVNAKIACLDFSLQKT 244
Cdd:TIGR02340 161 SDFFSNIVVDAVLAVKTTNENGETKYPIKAINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 245 KMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASG 324
Cdd:TIGR02340 241 KMALGVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 325 ASILSTLANLEGEETFEATMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLE 404
Cdd:TIGR02340 321 ATLVSTLADLEGEETFEASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 405 SKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLK 484
Cdd:TIGR02340 401 SNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAQLKPEKKHLK 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981642 485 WIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHPESKDD 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: 564.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 9 GDRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGD 88
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 89 GTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLiINTDELGRDCLINAAKTSMSSKIIGINGDFF 168
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIA-VPIDVEDREELLKVATTSLNSKLVSGGDDFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 169 ANMVVDAVLAVKytdiRGQPRYPVNSVNILKAHGRSQIESMLINGYALNCVVGSQGMLKRIVNAKIACLDFSLQktkmkl 248
Cdd:cd00309 160 GELVVDAVLKVG----KENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLE------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 249 gvqvvitdpekldqirqresditkeriqkilatgaNVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGASIL 328
Cdd:cd00309 230 -----------------------------------YVVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 329 STLanlegeETFEATMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSV 408
Cdd:cd00309 275 SRL------EDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 409 VPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQvnperknlKWIGL 488
Cdd:cd00309 349 VPGGGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGG--------GNAGG 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 6981642 489 DLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIK 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: 549.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 28 IANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADEL 107
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 108 VKQKIHPTSVISGYRLACKEAVRYINENLIINTDELGRDCLINAAKTSMSSKIIGINGDFFANMVVDAVLAVKYTDirgq 187
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKND---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 188 PRYPVNSVNILKAHGRSQIESMLINGYALNCVVGSQGMLKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRE 267
Cdd:pfam00118 157 GSFDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 268 SDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGASILSTLANLEGEEtfeatmLGQ 347
Cdd:pfam00118 237 EEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDD------LGT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 348 AEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGGGAVEAALSIYLENYA 427
Cdd:pfam00118 311 AGKVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 428 TSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNeaqvnperKNLKWIGLDLVHGKPRDNKQAGVFEPT 507
Cdd:pfam00118 391 KSVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHA--------SGEKHAGIDVETGEIIDMKEAGVVDPL 462
|
490 500
....*....|....*....|....*
gi 6981642 508 IVKVKSLKFATEAAITILRIDDLIK 532
Cdd:pfam00118 463 KVKRQALKSATEAASTILRIDDIIK 487
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
11-531 |
8.09e-172 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 496.33 E-value: 8.09e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 11 RSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGT 90
Cdd:NF041082 12 RTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 91 TSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINEnLIINTDELGRDCLINAAKTSMSSKIIGINGDFFAN 170
Cdd:NF041082 92 TTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDE-IAIKVDPDDKETLKKIAATAMTGKGAEAAKDKLAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 171 MVVDAVLAVkyTDIRGQPRYPVNSVNILKAHGRSQIESMLINGYALNCVVGSQGMLKRIVNAKIACLDFSLQKTKMKLGV 250
Cdd:NF041082 171 LVVDAVKAV--AEKDGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 251 QVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGASILST 330
Cdd:NF041082 249 KISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 331 LANLEGEEtfeatmLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVP 410
Cdd:NF041082 329 IDDLSPED------LGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 411 GGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNeaqvnperKNLKWIGLDL 490
Cdd:NF041082 403 GGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHE--------KGNKTAGLDV 474
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 6981642 491 VHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLI 531
Cdd:NF041082 475 YTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVI 515
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
11-531 |
1.63e-169 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 490.62 E-value: 1.63e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 11 RSTG-EAIRSqNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDG 89
Cdd:NF041083 12 RTKGrDAQRN-NIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 90 TTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINEnLIINTDELGRDCLINAAKTSMSSKIIGINGDFFA 169
Cdd:NF041083 91 TTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDE-IAEKVDPDDRETLKKIAETSLTSKGVEEARDYLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 170 NMVVDAVLAVkyTDIRGQpRYPV--NSVNILKAHGRSQIESMLINGYALNCVVGSQGMLKRIVNAKIACLDFSLQKTKMK 247
Cdd:NF041083 170 EIAVKAVKQV--AEKRDG-KYYVdlDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 248 LGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGASI 327
Cdd:NF041083 247 IDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 328 LSTLANLEGEEtfeatmLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKS 407
Cdd:NF041083 327 VTNIDDLTPED------LGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 408 VVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQvnperknlKWIG 487
Cdd:NF041083 401 IVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGK--------KWAG 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 6981642 488 LDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLI 531
Cdd:NF041083 473 INVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVI 516
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
11-532 |
2.19e-167 |
|
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: 484.84 E-value: 2.19e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 11 RSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGT 90
Cdd:cd03343 10 RTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 91 TSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYInENLIINTDELGRDCLINAAKTSMSSKIIGINGDFFAN 170
Cdd:cd03343 90 TTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELL-DEIAIKVDPDDKDTLRKIAKTSLTGKGAEAAKDKLAD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 171 MVVDAVLAVKYTDiRGQPRYPVNSVNILKAHGRSQIESMLINGYALNCVVGSQGMLKRIVNAKIACLDFSLQKTKMKLGV 250
Cdd:cd03343 169 LVVDAVLQVAEKR-DGKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 251 QVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGASILST 330
Cdd:cd03343 248 KIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTN 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 331 LANLEGEEtfeatmLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVP 410
Cdd:cd03343 328 IDDLTPED------LGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 411 GGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNeaqvnperKNLKWIGLDL 490
Cdd:cd03343 402 GGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHE--------KGNKNAGLDV 473
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 6981642 491 VHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIK 532
Cdd:cd03343 474 YTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIA 515
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
11-531 |
2.09e-159 |
|
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: 464.93 E-value: 2.09e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 11 RSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGT 90
Cdd:TIGR02339 11 RTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 91 TSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYInENLIINTDELGRDCLINAAKTSMSSK-IIGINGDFFA 169
Cdd:TIGR02339 91 TTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEII-DEIATKISPEDRDLLKKIAYTSLTSKaSAEVAKDKLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 170 NMVVDAVLAVKYTDIRGQPRYPVNSVNILKAHGRSQIESMLINGYALNCVVGSQGMLKRIVNAKIACLDFSLQKTKMKLG 249
Cdd:TIGR02339 170 DLVVEAVKQVAELRGDGKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAPLEVEKTEID 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 250 VQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGASILS 329
Cdd:TIGR02339 250 AKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 330 TLANLEGEEtfeatmLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVV 409
Cdd:TIGR02339 330 SIDEITESD------LGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 410 PGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNeaqvnperKNLKWIGLD 489
Cdd:TIGR02339 404 AGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHE--------KGNKNAGIN 475
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 6981642 490 LVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLI 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 |
1.62e-142 |
|
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: 421.70 E-value: 1.62e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 10 DRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDG 89
Cdd:cd03340 10 DTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 90 TTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINE---NLIINTDELGRDCLINAAKTSMSSKIIGINGD 166
Cdd:cd03340 90 TTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEiavNIDKEDKEEQRELLEKCAATALNSKLIASEKE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 167 FFANMVVDAVLAVKYTDirgqpryPVNSVNILKAHGRSQIESMLINGYALN---CVVGSQGMLKRIVNAKIACLDFSLQK 243
Cdd:cd03340 170 FFAKMVVDAVLSLDDDL-------DLDMIGIKKVPGGSLEDSQLVNGVAFKktfSYAGFEQQPKKFKNPKILLLNVELEL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 244 TKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKAS 323
Cdd:cd03340 243 KAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQAT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 324 GASILSTLANLEGEetfeatMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVL 403
Cdd:cd03340 323 GGSIQTTVSNITDD------VLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 404 ESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVnperknl 483
Cdd:cd03340 397 KNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGG------- 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 6981642 484 KWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLhPES 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 |
1.39e-122 |
|
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: 370.63 E-value: 1.39e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 10 DRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDG 89
Cdd:TIGR02345 12 DTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 90 TTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIINTDELG--RDCLINAAKTSMSSKIIGINGDF 167
Cdd:TIGR02345 92 TTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKGeqRELLEKCAATALSSKLISHNKEF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 168 FANMVVDAVLAVKYTDIRgqprypVNSVNILKAHGRSQIESMLINGYALN---CVVGSQGMLKRIVNAKIACLDFSLQKT 244
Cdd:TIGR02345 172 FSKMIVDAVLSLDRDDLD------LKLIGIKKVQGGALEDSQLVNGVAFKktfSYAGFEQQPKKFANPKILLLNVELELK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 245 KMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASG 324
Cdd:TIGR02345 246 AEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 325 ASILSTLANLEGEetfeatMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLE 404
Cdd:TIGR02345 326 GSIQSTTSDLEAD------VLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 405 SKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNeaqvnperKNLK 484
Cdd:TIGR02345 400 NKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHA--------KGGK 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 6981642 485 WIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKL 533
Cdd:TIGR02345 472 WYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITN 520
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
10-531 |
1.17e-120 |
|
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: 365.46 E-value: 1.17e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 10 DRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDG 89
Cdd:cd03338 2 DKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 90 TTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINEnLIINTDELGRDCLINAAKTSMSSKIIGINGDFFA 169
Cdd:cd03338 82 TTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDS-MSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 170 NMVVDAVLAVkyTDIRGQPRYPVNSVNILKAHGRSQIESMLINGYALNC-VVGSQGMLKRIVNAKIACLDFSLQKTKMKL 248
Cdd:cd03338 161 PIAVDAVLKV--IDPATATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQkASKKAGGPTRIEKAKIGLIQFCLSPPKTDM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 249 GVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGI-----DDMCLKYFVEAGAMAVRRVLKRDLKRIAKAS 323
Cdd:cd03338 239 DNNIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 324 GAsilSTLANLEGeetFEATMLGQAEEVVQERICDDELILIKNTK-ARTSASIILRGANDFMCDEMERSLHDALCVVKRV 402
Cdd:cd03338 319 GC---KPVASIDH---FTEDKLGSADLVEEVSLGDGKIVKITGVKnPGKTVTILVRGSNKLVLDEAERSLHDALCVIRCL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 403 LESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHneAQVNperkn 482
Cdd:cd03338 393 VKKRALIPGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRH--AQGE----- 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 6981642 483 lKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLI 531
Cdd:cd03338 466 -KNAGINVRKGAITNILEENVVQPLLVSTSAITLATETVRMILKIDDIV 513
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
14-535 |
3.10e-119 |
|
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: 361.65 E-value: 3.10e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 14 GEAIRSQNVMAAASIANIVKSSLGPVGLDKML--VDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTT 91
Cdd:cd03336 11 GETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDGTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 92 SVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIINTD--ELGRDCLINAAKTSMSSKIIGINGDFFA 169
Cdd:cd03336 91 SVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSdeEAFREDLLNIARTTLSSKILTQDKEHFA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 170 NMVVDAVLAVK-YTDIrgqprypvNSVNILKAHGRSQIESMLINGYALNCVVGSqGMLKRIVNAKIACLDFSLQKTKMKL 248
Cdd:cd03336 171 ELAVDAVLRLKgSGNL--------DAIQIIKKLGGSLKDSYLDEGFLLDKKIGV-NQPKRIENAKILIANTPMDTDKIKI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 249 -GVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGASI 327
Cdd:cd03336 242 fGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTGGEI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 328 LSTLANLegeetfEATMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKS 407
Cdd:cd03336 322 ASTFDHP------ELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 408 VVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNeaqvnperKNLKWIG 487
Cdd:cd03336 396 VVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHY--------NGNTTAG 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 6981642 488 LDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHP 535
Cdd:cd03336 468 LDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKCAP 515
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
14-535 |
4.69e-119 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 362.04 E-value: 4.69e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 14 GEAIRSQNVMAAASIANIVKSSLGPVGLDKMLV-----DDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGD 88
Cdd:PTZ00212 20 GETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 89 GTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIINT--DELGRDCLINAAKTSMSSKIIGINGD 166
Cdd:PTZ00212 100 GTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGsdEEKFKEDLLNIARTTLSSKLLTVEKD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 167 FFANMVVDAVLavkytDIRGQPRypVNSVNILKAHGRSQIESMLINGYALNCVVGSqGMLKRIVNAKIACLDFSLQKTKM 246
Cdd:PTZ00212 180 HFAKLAVDAVL-----RLKGSGN--LDYIQIIKKPGGTLRDSYLEDGFILEKKIGV-GQPKRLENCKILVANTPMDTDKI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 247 KL-GVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGA 325
Cdd:PTZ00212 252 KIyGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 326 SILSTLanlegeETFEATMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLES 405
Cdd:PTZ00212 332 EIVSTF------DTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 406 KSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNperknlkw 485
Cdd:PTZ00212 406 TRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKT-------- 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 6981642 486 IGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHP 535
Cdd:PTZ00212 478 AGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRCAP 527
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
11-532 |
2.01e-117 |
|
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: 357.38 E-value: 2.01e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 11 RSTG-EAIRSqNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDG 89
Cdd:cd03339 18 RLKGlEAHKS-HILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 90 TTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINE-NLIINTDELGRDCLINAAKTSMSSKIIGINGDFF 168
Cdd:cd03339 97 TTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEiADKIEFSPDNKEPLIQTAMTSLGSKIVSRCHRQF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 169 ANMVVDAVLAVKYTDirgqpRYPVN--SVNILKAHGRSQIESMLINGYALNCVVGSQGMLKRIVNAKIACLDFSLQKTKM 246
Cdd:cd03339 177 AEIAVDAVLSVADLE-----RKDVNfeLIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIAILTCPFEPPKP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 247 KLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGAS 326
Cdd:cd03339 252 KTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 327 ILSTLANLEGEEtfeatmLGQAeEVVQER---ICDDELILI---KNTKARTsasIILRGANDFMCDEMERSLHDALCVVK 400
Cdd:cd03339 332 IVPRFEDLSPEK------LGKA-GLVREIsfgTTKDKMLVIegcPNSKAVT---IFIRGGNKMIIEEAKRSLHDALCVVR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 401 RVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAfhneAQVNPER 480
Cdd:cd03339 402 NLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKA----RQVKEKN 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 6981642 481 KNLkwiGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIK 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 |
8.10e-112 |
|
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: 343.32 E-value: 8.10e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 15 EAIRSqNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVV 94
Cdd:TIGR02343 27 EAKKS-NIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 95 IIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINE-NLIINTDELGRDCLINAAKTSMSSKIIGINGDFFANMVV 173
Cdd:TIGR02343 106 VLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEiSDEISADNNNREPLIQAAKTSLGSKIVSKCHRRFAEIAV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 174 DAVLAVKYTDirgqpRYPVNS--VNILKAHGRSQIESMLINGYALNCVVGSQGMLKRIVNAKIACLDFSLQKTKMKLGVQ 251
Cdd:TIGR02343 186 DAVLNVADME-----RRDVDFdlIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAILTCPFEPPKPKTKHK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 252 VVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGASILSTL 331
Cdd:TIGR02343 261 LDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPRF 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 332 ANLEGEEtfeatmLGQAEEVVQERI--CDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVV 409
Cdd:TIGR02343 341 QELSKDK------LGKAGLVREISFgtTKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 410 PGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEaQVNPErknlkwIGLD 489
Cdd:TIGR02343 415 YGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLK-EKNPN------LGVD 487
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 6981642 490 LVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIK 532
Cdd:TIGR02343 488 CLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVIS 530
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
8-531 |
6.68e-107 |
|
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: 330.21 E-value: 6.68e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 8 FGDRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVG 87
Cdd:TIGR02342 1 FQDKDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 88 DGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINEnLIINTDELGRDCLINAAKTSMSSKIIGINGDF 167
Cdd:TIGR02342 81 DGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDE-MSIPVDLSDREQLLKSATTSLSSKVVSQYSSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 168 FANMVVDAVLAVkyTDIRGQPRYPVNSVNILKAHGRSQIESMLINGYAL-NCVVGSQGMLKRIVNAKIACLDFSLQKTKM 246
Cdd:TIGR02342 160 LAPLAVDAVLKV--IDPENAKNVDLNDIKVVKKLGGTIDDTELIEGLVFtQKASKSAGGPTRIEKAKIGLIQFQISPPKT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 247 KLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGI-----DDMCLKYFVEAGAMAVRRVLKRDLKRIAK 321
Cdd:TIGR02342 238 DMENQIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 322 ASGASILSTLanlegeETFEATMLGQAEEVvqERICDDELILIKNT---KARTSASIILRGANDFMCDEMERSLHDALCV 398
Cdd:TIGR02342 318 TIGCKPIASI------DHFTADKLGSAELV--EEVDSDGGKIIKITgiqNAGKTVTVVVRGSNKLVIDEAERSLHDALCV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 399 VKRVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQvnp 478
Cdd:TIGR02342 390 IRCLVKKRGLIAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGE--- 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 6981642 479 erknlKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLI 531
Cdd:TIGR02342 467 -----KTAGISVRKGGITNMLEEHVLQPLLVTTSAITLASETVRSILKIDDIV 514
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
14-541 |
9.10e-107 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 328.96 E-value: 9.10e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 14 GEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKVLCELADLQDKEVGDG 89
Cdd:COG0459 8 GEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 90 TTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLI-INTDELgrdcLINAAKTSMSSKiigingDFF 168
Cdd:COG0459 88 TTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKpVDDKEE----LAQVATISANGD------EEI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 169 ANMVVDAVLAVkytdirGQprypvNSVNILKAHGRSQIESMLINGYALN-------CVVGSQGMLKRIVNAKIAcldfsl 241
Cdd:COG0459 158 GELIAEAMEKV------GK-----DGVITVEEGKGLETELEVVEGMQFDkgylspyFVTDPEKMPAELENAYIL------ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 242 qktkmklgvqvvITDpEKLDQIRQResditKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVL--------- 312
Cdd:COG0459 221 ------------LTD-KKISSIQDL-----LPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVavkapgfgd 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 313 --KRDLKRIAKASGASILSTLANLEGEETfEATMLGQAEEVVQEricDDELILIKNTKARTSASIILRGANDFMCDEMER 390
Cdd:COG0459 283 rrKAMLEDIAILTGGRVISEDLGLKLEDV-TLDDLGRAKRVEVD---KDNTTIVEGAGNPKAIVILVGAATEVEVKERKR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 391 SLHDALCVVKRVLESKsVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAf 470
Cdd:COG0459 359 RVEDALHATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRA- 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981642 471 hneaqvnperKNLKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHPESKDDK 541
Cdd:COG0459 437 ----------AKDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
11-531 |
3.90e-103 |
|
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: 319.24 E-value: 3.90e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 11 RSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGT 90
Cdd:cd03337 11 RESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 91 TSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYInENLIINTDELGRDCLINAAKTSMSSKIIGINGDFFAN 170
Cdd:cd03337 91 TSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKIL-EEISIPVDVNDRAQMLKIIKSCIGTKFVSRWSDLMCN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 171 MVVDAVLAV--------KYTDIRgqpRYpvnsVNILKAHGRSQIESMLINGYALNCVVGSQGMLKRIVNAKIACLDFSLQ 242
Cdd:cd03337 170 LALDAVKTVaveengrkKEIDIK---RY----AKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPLE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 243 ktkmklgvQVVITdpEKldqirqresditkeriqkilatganvilttgGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKA 322
Cdd:cd03337 243 --------YLVIT--EK-------------------------------GVSDLAQHYLVKAGITALRRVRKTDNNRIARA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 323 SGASILSTLANLEGEEtfeatmLGQAEEVVQERICDDE----LILIKNTKArtsASIILRGANDFMCDEMERSLHDALCV 398
Cdd:cd03337 282 CGATIVNRPEELTESD------VGTGAGLFEVKKIGDEyftfITECKDPKA---CTILLRGASKDVLNEVERNLQDAMAV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 399 VKRVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQvnp 478
Cdd:cd03337 353 ARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGE--- 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 6981642 479 erkNLKWiGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLI 531
Cdd:cd03337 430 ---NSTW-GIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
5-531 |
5.28e-102 |
|
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: 317.45 E-value: 5.28e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 5 LSVFGDRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDK 84
Cdd:TIGR02344 5 LNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 85 EVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINEnLIINTDELGRDCLINAAKTSMSSKIIGIN 164
Cdd:TIGR02344 85 EVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEE-ISIPVDVNDDAAMLKLIQSCIGTKFVSRW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 165 GDFFANMVVDAVLAVKYTdirGQPRYPVN---SVNILKAHGRSQIESMLINGYALNCVVGSQGMLKRIVNAKIACLDFSL 241
Cdd:TIGR02344 164 SDLMCDLALDAVRTVQRD---ENGRKEIDikrYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 242 QKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAK 321
Cdd:TIGR02344 241 EYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 322 ASGASILSTLANLEGEET------FEATMLGqaeevvqericDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDA 395
Cdd:TIGR02344 321 ACGATIVNRPEELRESDVgtgcglFEVKKIG-----------DEYFTFITECKDPKACTILLRGASKDILNEVERNLQDA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 396 LCVVKRVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAq 475
Cdd:TIGR02344 390 MAVARNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQE- 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981642 476 vnperkNLKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLI 531
Cdd:TIGR02344 469 ------NNCTWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
21-531 |
3.41e-96 |
|
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: 300.68 E-value: 3.41e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 21 NVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAEL 100
Cdd:cd03341 13 NIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 101 LKNADELVKQKIHPTSVISGYRLACKEAVRyINENLIINTDELGRDC--LINAAKTSMSSKIIGiNGDFFANMVVDAVLA 178
Cdd:cd03341 93 LEKAEELLRMGLHPSEIIEGYEKALKKALE-ILEELVVYKIEDLRNKeeVSKALKTAIASKQYG-NEDFLSPLVAEACIS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 179 VKYTDIRgqpRYPVNSVNILKAHGRSQIESMLINGYALNcvVGSQGMLKRIVNAKIAcldfslqktkmklgvqvVITDPe 258
Cdd:cd03341 171 VLPENIG---NFNVDNIRVVKILGGSLEDSKVVRGMVFK--REPEGSVKRVKKAKVA-----------------VFSCP- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 259 kldqirqresditkeriqkiLATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGASILSTLANLEGEE 338
Cdd:cd03341 228 --------------------FDIGVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 339 tfeatmLGQAEEVVQERICDDELILIKNTKARTS-ASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGGGAVEA 417
Cdd:cd03341 288 ------IGYCDSVYVEEIGDTKVVVFRQNKEDSKiATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 418 ALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNperknlkwIGLDLVHGKP-- 495
Cdd:cd03341 362 ELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKS--------AGVDIESGDEgt 433
|
490 500 510
....*....|....*....|....*....|....*.
gi 6981642 496 RDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLI 531
Cdd:cd03341 434 KDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
9-538 |
2.70e-95 |
|
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: 300.24 E-value: 2.70e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 9 GDRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDD--IGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEV 86
Cdd:TIGR02341 7 ADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSssDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 87 GDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIINTDELG--RDCLINAAKTSMSSKIIGIN 164
Cdd:TIGR02341 87 GDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVkfRQDLMNIARTTLSSKILSQH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 165 GDFFANMVVDAVLAVKYTDirgqpryPVNSVNILKAHGRSQIESMLINGYALNCVVGSQgMLKRIVNAKIACLDFSLQKT 244
Cdd:TIGR02341 167 KDHFAQLAVDAVLRLKGSG-------NLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVN-QPKRIENAKILIANTGMDTD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 245 KMKL-GVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKAS 323
Cdd:TIGR02341 239 KVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 324 GASILSTLanlegeETFEATMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVL 403
Cdd:TIGR02341 319 GGEIVSTF------DHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 404 ESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNperknl 483
Cdd:TIGR02341 393 KESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTT------ 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 6981642 484 kwIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHPESK 538
Cdd:TIGR02341 467 --MGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPRKR 519
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
20-535 |
8.70e-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: 298.94 E-value: 8.70e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 20 QNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAE 99
Cdd:TIGR02346 22 KNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 100 LLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIINTDEL-GRDCLINAAKTSMSSKIIGiNGDFFANMVVDAVLA 178
Cdd:TIGR02346 102 LLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDLrDKDELIKALKASISSKQYG-NEDFLAQLVAQACST 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 179 VKYTDIRgqpRYPVNSVNILKAHGRSQIESMLINGYALNcvVGSQGMLKRIVNAKIACLDFSLQKTKMKLGVQVVITDPE 258
Cdd:TIGR02346 181 VLPKNPQ---NFNVDNIRVCKILGGSLSNSEVLKGMVFN--REAEGSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNAE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 259 KLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGASILSTLANLEGEE 338
Cdd:TIGR02346 256 ELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 339 tfeatmLGQAEEVVQERICDDELILIKNTKARTS-ASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGGGAVEA 417
Cdd:TIGR02346 336 ------IGYVDSVYVSEIGGDKVTVFKQENGDSKiSTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEI 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 418 ALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNeaqvnperKNLKWIGLDLVHGKPR- 496
Cdd:TIGR02346 410 ELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHK--------KGNKSKGIDIEAESDGv 481
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 6981642 497 -DNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHP 535
Cdd:TIGR02346 482 kDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKP 521
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
15-532 |
5.50e-84 |
|
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274088 [Multi-domain] Cd Length: 531 Bit Score: 270.84 E-value: 5.50e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 15 EAIRSQ-----NVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDG 89
Cdd:TIGR02347 10 ESLRRDaalmmNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 90 TTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIINTDELGRDCLINAAKTSMSSKIIGINGDFFA 169
Cdd:TIGR02347 90 TTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEVDREFLLNVARTSLRTKLPADLADQLT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 170 NMVVDAVLAVKytdiRGQPRYPVNSVNILKAHGRSQIESMLINGYALNCVVGSQGMLKRIVNAKIACLDFSLQKTKMKLG 249
Cdd:TIGR02347 170 EIVVDAVLAIK----KDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 250 VQVVITDPEKLDQIRQRESDITKERIQKIL-------ATGAN---VILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRI 319
Cdd:TIGR02347 246 SGFFYSSAEQREKLVKAERKFVDDRVKKIIelkkkvcGKSPDkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 320 AKASGASILSTLANLEGEEtfeatmLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVV 399
Cdd:TIGR02347 326 TLACGGEALNSVEDLTPEC------LGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 400 KRVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQvnpe 479
Cdd:TIGR02347 400 KNAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGG---- 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 6981642 480 rknlKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIK 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 |
4.82e-82 |
|
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: 264.51 E-value: 4.82e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 21 NVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAEL 100
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 101 LKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIINTDELGRDCLINAAKTSMSSKIIGINGDFFANMVVDAVLAVK 180
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 181 ytdirgQPRYPV--NSVNILKAHGRSQIESMLINGYALNCVVGSQGMLKRIVNAKIACLDFSLQKTKmklgvqvvitdpe 258
Cdd:cd03342 177 ------KPDEPIdlHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEK------------- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 259 kldqirqreSDITKERIQKilatganVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGASILSTLANLEGEE 338
Cdd:cd03342 238 ---------TEVNSGFFYS-------VVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPEC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 339 tfeatmLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGGGAVEAA 418
Cdd:cd03342 302 ------LGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 419 LSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPerknlkwiGLDLVHGKPRDN 498
Cdd:cd03342 376 LYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVG--------GVDLDTGEPMDP 447
|
490 500 510
....*....|....*....|....*....|....
gi 6981642 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 |
2.73e-65 |
|
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: 211.56 E-value: 2.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 145 RDCLINAAKTSMSSKIIGiNGDFFANMVVDAVLAVKytdiRGQPRYPVNSVNILKAHGRSQIESMLINGYALNCVVGSQG 224
Cdd:cd03333 1 RELLLQVATTSLNSKLSS-WDDFLGKLVVDAVLKVG----PDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 225 MLKRIVNAKIACLDFSLQktkmklgvqvvitdpekldqirqresditkeriqkilatgaNVILTTGGIDDMCLKYFVEAG 304
Cdd:cd03333 76 MPKRLENAKILLLDCPLE-----------------------------------------YVVIAEKGIDDLALHYLAKAG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 305 AMAVRRVLKRDLKRIAKASGASILSTLanlegeETFEATMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFM 384
Cdd:cd03333 115 IMAVRRVKKEDLERIARATGATIVSSL------EDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVE 188
|
250 260
....*....|....*....|.
gi 6981642 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. ... |
166-424 |
1.50e-12 |
|
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: 68.02 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 166 DFFANMVVDAVLAVKyTDIR-GQPRYPVNSVNILKAHGRSQIESMLINGYALNCVVGSQGMLKRIVNAKIACLDFSLqkt 244
Cdd:cd03334 21 DILLPLVWKAASNVK-PDVRaGDDMDIRQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPL--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 245 kmklGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASG 324
Cdd:cd03334 97 ----EYQRVENKLLSLDPVILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 325 ASILSTLANLegeetFEATMLGQAEEVVQERICDDE-----LILIKNTKARTSASIILRGANdfmcdemerslHDALCVV 399
Cdd:cd03334 173 ADIISSMDDL-----LTSPKLGTCESFRVRTYVEEHgrsktLMFFEGCPKELGCTILLRGGD-----------LEELKKV 236
|
250 260
....*....|....*....|....*
gi 6981642 400 KRVLESksvvpgggAVEAALSIYLE 424
Cdd:cd03334 237 KRVVEF--------MVFAAYHLKLE 253
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
28-135 |
1.96e-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: 56.70 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 28 IANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKVLCELADLQDKEVGDGTTSVVIIAAELLKN 103
Cdd:cd03344 20 LADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLARAIIKE 99
|
90 100 110
....*....|....*....|....*....|..
gi 6981642 104 ADELVKQKIHPTSVISGYRLACKEAVRYINEN 135
Cdd:cd03344 100 GLKAVAAGANPMDLKRGIEKAVEAVVEELKKL 131
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
28-135 |
5.54e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 55.49 E-value: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 28 IANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKVLCELADLQDKEVGDGTTSVVIIAAELLKN 103
Cdd:PRK12850 23 LANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110
....*....|....*....|....*....|..
gi 6981642 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 |
4.33e-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: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 28 IANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKVLCELADLQDKEVGDGTTSVVIIAAELLKN 103
Cdd:TIGR02348 21 LADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVASKTNDVAGDGTTTATVLAQAIVKE 100
|
90 100 110
....*....|....*....|....*....|..
gi 6981642 104 ADELVKQKIHPTSVISGYRLACKEAVRYINEN 135
Cdd:TIGR02348 101 GLKNVAAGANPIELKRGIEKAVEAVVEELKKL 132
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
15-130 |
1.81e-06 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 50.51 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 15 EAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKVLCELADLQDKEVGDGT 90
Cdd:PRK12851 10 VEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGT 89
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 6981642 91 TSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVR 130
Cdd:PRK12851 90 TTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVE 129
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
28-134 |
3.54e-06 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 49.91 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 28 IANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPA----AKVLCELADLQDKEVGDGTTSVVIIAAELLKN 103
Cdd:PTZ00114 34 LADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKAGDGTTTATILARAIFRE 113
|
90 100 110
....*....|....*....|....*....|.
gi 6981642 104 ADELVKQKIHPTSVISGYRLACKEAVRYINE 134
Cdd:PTZ00114 114 GCKAVAAGLNPMDLKRGIDLAVKVVLESLKE 144
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
29-97 |
5.81e-06 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 49.03 E-value: 5.81e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981642 29 ANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKVLCELAdLQDKEV-GDGTTSVVIIA 97
Cdd:PRK12849 23 ADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVA-SKTNDVaGDGTTTATVLA 95
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
28-120 |
2.40e-05 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 47.23 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 28 IANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKVLCELADLQDKEVGDGTTSVVIIAAELLKN 103
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAE 157
|
90
....*....|....*..
gi 6981642 104 ADELVKQKIHPTSVISG 120
Cdd:PLN03167 158 GVKVVAAGANPVQITRG 174
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
28-103 |
1.99e-04 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 43.96 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 28 IANIVKSSLGP----VGLDKmlvdDIGDVTITNDGATILKLLEVEHP----AAKVLCELADLQDKEVGDGTTSVVIIAA- 98
Cdd:PRK00013 22 LADAVKVTLGPkgrnVVLEK----SFGAPTITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLAQa 97
|
....*...
gi 6981642 99 ---ELLKN 103
Cdd:PRK00013 98 ivrEGLKN 105
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
18-135 |
4.92e-03 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 39.70 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981642 18 RSQNVMAAAsianiVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKV---LCELADLQDKEV-GDGTTSV 93
Cdd:CHL00093 17 RGMDILAEA-----VSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTgvaLIRQAASKTNDVaGDGTTTA 91
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 6981642 94 VIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINEN 135
Cdd:CHL00093 92 TVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEY 133
|
|
| |
