|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
12-538 |
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: 1026.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 12 GTRQSGASVRTQNVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEVGD 91
Cdd:cd03335 1 GERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 92 GTTSVVILAAELLKNADELVKQKIHPTSIISGYRIACKEACKYISEHLTAPVDELGRDSLINIAKTSMSSKIIGADAEFF 171
Cdd:cd03335 81 GTTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEHLSISVDNLGKESLINVAKTSMSSKIIGADSDFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 172 SAMVVDAAQSVKITDPRGQAAYSIKAINVLKAHGKSARESVLIPGYALNCTIASQQMPKKIVNAKIACLDFSLQKTKMKM 251
Cdd:cd03335 161 ANMVVDAILAVKTTNEKGKTKYPIKAVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 252 GVQVLINDPDKLEAIRARELDITKERINMILGTGVNVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATGAAFI 331
Cdd:cd03335 241 GVQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 332 TSLTNMDGEESFDASMVGEAAEVAQERICDDELILIKGTKARAAASIILRGPNDFYCDEMERSVHDALCVVKRVLESKKV 411
Cdd:cd03335 321 STLANLEGEETFDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 412 VAGGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNSSQTKPERSDLKWTGL 491
Cdd:cd03335 401 VPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKPDKKHLKWYGL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24649029 492 DLIEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMIKLNP 538
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 ... |
8-543 |
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: 944.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 8 LSIAGTRQSGASVRTQNVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDE 87
Cdd:TIGR02340 1 LFLGGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 88 EVGDGTTSVVILAAELLKNADELVKQKIHPTSIISGYRIACKEACKYISEHLTAPVDELGRDSLINIAKTSMSSKIIGAD 167
Cdd:TIGR02340 81 EVGDGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKENLSVSVDELGREALINVAKTSMSSKIIGLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 168 AEFFSAMVVDAAQSVKITDPRGQAAYSIKAINVLKAHGKSARESVLIPGYALNCTIASQQMPKKIVNAKIACLDFSLQKT 247
Cdd:TIGR02340 161 SDFFSNIVVDAVLAVKTTNENGETKYPIKAINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 248 KMKMGVQVLINDPDKLEAIRARELDITKERINMILGTGVNVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATG 327
Cdd:TIGR02340 241 KMALGVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 328 AAFITSLTNMDGEESFDASMVGEAAEVAQERICDDELILIKGTKARAAASIILRGPNDFYCDEMERSVHDALCVVKRVLE 407
Cdd:TIGR02340 321 ATLVSTLADLEGEETFEASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 408 SKKVVAGGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNSSQTKPERSDLK 487
Cdd:TIGR02340 401 SNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAQLKPEKKHLK 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 24649029 488 WTGLDLIEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMIKLNPEDKSG 543
Cdd:TIGR02340 481 WYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIKLNPEQSKG 536
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
14-535 |
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: 551.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 14 RQSGASVRTQNVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEVGDGT 93
Cdd:cd00309 3 REFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 94 TSVVILAAELLKNADELVKQKIHPTSIISGYRIACKEACKYISEHLTaPVDELGRDSLINIAKTSMSSKIIGADAEFFSA 173
Cdd:cd00309 83 TTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAV-PIDVEDREELLKVATTSLNSKLVSGGDDFLGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 174 MVVDAAQSVKITDPRgqaaYSIKAINVLKAHGKSARESVLIPGYALNCTIASQQMPKKIVNAKIACLDFSLQktkmkmgv 253
Cdd:cd00309 162 LVVDAVLKVGKENGD----VDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLE-------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 254 qvlindpdkleairarelditkerinmilgtgvNVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATGAAFITS 333
Cdd:cd00309 230 ---------------------------------YVVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSR 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 334 LtnmdgeESFDASMVGEAAEVAQERICDDELILIKGTKARAAASIILRGPNDFYCDEMERSVHDALCVVKRVLESKKVVA 413
Cdd:cd00309 277 L------EDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 414 GGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNSSQtkpersdlKWTGLDL 493
Cdd:cd00309 351 GGGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGG--------GNAGGDV 422
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 24649029 494 IEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMIK 535
Cdd:cd00309 423 ETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
31-535 |
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: 541.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 31 ISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEVGDGTTSVVILAAELLKNADEL 110
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 111 VKQKIHPTSIISGYRIACKEACKYISEHLTAPVDELGRDSLINIAKTSMSSKIIGADAEFFSAMVVDAAQSVKITDPRGQ 190
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDGSFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 191 aaysIKAINVLKAHGKSARESVLIPGYALNCTIASQQMPKKIVNAKIACLDFSLQKTKMKMGVQVLINDPDKLEAIRARE 270
Cdd:pfam00118 161 ----LGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 271 LDITKERINMILGTGVNVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATGAAFITSLtnmdgeESFDASMVGE 350
Cdd:pfam00118 237 EEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSL------DDLTPDDLGT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 351 AAEVAQERICDDELILIKGTKARAAASIILRGPNDFYCDEMERSVHDALCVVKRVLESKKVVAGGGCVEAALSIYLENFA 430
Cdd:pfam00118 311 AGKVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 431 TSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNSSQtkpersdlKWTGLDLIEGVVRDNKKAGVLEPA 510
Cdd:pfam00118 391 KSVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGE--------KHAGIDVETGEIIDMKEAGVVDPL 462
|
490 500
....*....|....*....|....*
gi 24649029 511 MSKIKSLKFATEAAITILRIDDMIK 535
Cdd:pfam00118 463 KVKRQALKSATEAASTILRIDDIIK 487
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
14-534 |
6.39e-168 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 486.31 E-value: 6.39e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 14 RQSGASVRTQNVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEVGDGT 93
Cdd:NF041082 12 RTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 94 TSVVILAAELLKNADELVKQKIHPTSIISGYRIACKEACKyISEHLTAPVDELGRDSLINIAKTSMSSKIIGADAEFFSA 173
Cdd:NF041082 92 TTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALE-ILDEIAIKVDPDDKETLKKIAATAMTGKGAEAAKDKLAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 174 MVVDAAQSVkiTDPRGQAAYSIKAINVLKAHGKSARESVLIPGYALNCTIASQQMPKKIVNAKIACLDFSLQKTKMKMGV 253
Cdd:NF041082 171 LVVDAVKAV--AEKDGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 254 QVLINDPDKLEAIRARELDITKERINMILGTGVNVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATGAAFITS 333
Cdd:NF041082 249 KISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 334 LTNMDGEEsfdasmVGEAAEVAQERICDDELILIKGTKARAAASIILRGPNDFYCDEMERSVHDALCVVKRVLESKKVVA 413
Cdd:NF041082 329 IDDLSPED------LGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 414 GGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNSSqtkpersdLKWTGLDL 493
Cdd:NF041082 403 GGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKG--------NKTAGLDV 474
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 24649029 494 IEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMI 534
Cdd:NF041082 475 YTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVI 515
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
14-535 |
4.11e-163 |
|
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: 474.06 E-value: 4.11e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 14 RQSGASVRTQNVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEVGDGT 93
Cdd:cd03343 10 RTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 94 TSVVILAAELLKNADELVKQKIHPTSIISGYRIACKEACKYISEHLTaPVDELGRDSLINIAKTSMSSKIIGADAEFFSA 173
Cdd:cd03343 90 TTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAI-KVDPDDKDTLRKIAKTSLTGKGAEAAKDKLAD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 174 MVVDAAQSVKITDPrGQAAYSIKAINVLKAHGKSARESVLIPGYALNCTIASQQMPKKIVNAKIACLDFSL--QKTKMKM 251
Cdd:cd03343 169 LVVDAVLQVAEKRD-GKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLevKKTEIDA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 252 GVQvlINDPDKLEAIRARELDITKERINMILGTGVNVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATGAAFI 331
Cdd:cd03343 248 KIR--ITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 332 TSLTNMDGEEsfdasmVGEAAEVAQERICDDELILIKGTKARAAASIILRGPNDFYCDEMERSVHDALCVVKRVLESKKV 411
Cdd:cd03343 326 TNIDDLTPED------LGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 412 VAGGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNssqtkperSDLKWTGL 491
Cdd:cd03343 400 VAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHE--------KGNKNAGL 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 24649029 492 DLIEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMIK 535
Cdd:cd03343 472 DVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIA 515
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
14-534 |
3.12e-162 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 472.13 E-value: 3.12e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 14 RQSGASVRTQNVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEVGDGT 93
Cdd:NF041083 12 RTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 94 TSVVILAAELLKNADELVKQKIHPTSIISGYRIACKEACKYISEhLTAPVDELGRDSLINIAKTSMSSKIIGADAEFFSA 173
Cdd:NF041083 92 TTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDE-IAEKVDPDDRETLKKIAETSLTSKGVEEARDYLAE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 174 MVVDAAQSVkiTDPRGQAAY-SIKAINVLKAHGKSARESVLIPGYALNCTIASQQMPKKIVNAKIACLDFSLQKTKMKMG 252
Cdd:NF041083 171 IAVKAVKQV--AEKRDGKYYvDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEID 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 253 VQVLINDPDKLEAIRARELDITKERINMILGTGVNVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATGAAFIT 332
Cdd:NF041083 249 AEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 333 SLtnmdgeESFDASMVGEAAEVAQERICDDELILIKGTKARAAASIILRGPNDFYCDEMERSVHDALCVVKRVLESKKVV 412
Cdd:NF041083 329 NI------DDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 413 AGGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNSSQtkpersdlKWTGLD 492
Cdd:NF041083 403 AGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGK--------KWAGIN 474
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 24649029 493 LIEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMI 534
Cdd:NF041083 475 VFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVI 516
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
14-534 |
4.91e-153 |
|
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: 448.37 E-value: 4.91e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 14 RQSGASVRTQNVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEVGDGT 93
Cdd:TIGR02339 11 RTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 94 TSVVILAAELLKNADELVKQKIHPTSIISGYRIACKEACKYIsEHLTAPVDELGRDSLINIAKTSMSSKIIGADA-EFFS 172
Cdd:TIGR02339 91 TTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEII-DEIATKISPEDRDLLKKIAYTSLTSKASAEVAkDKLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 173 AMVVDAAQSVKITDPRGQAAYSIKAINVLKAHGKSARESVLIPGYALNCTIASQQMPKKIVNAKIACLDFSLQKTKMKMG 252
Cdd:TIGR02339 170 DLVVEAVKQVAELRGDGKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAPLEVEKTEID 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 253 VQVLINDPDKLEAIRARELDITKERINMILGTGVNVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATGAAFIT 332
Cdd:TIGR02339 250 AKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 333 SLTNMDGEEsfdasmVGEAAEVAQERICDDELILIKGTKARAAASIILRGPNDFYCDEMERSVHDALCVVKRVLESKKVV 412
Cdd:TIGR02339 330 SIDEITESD------LGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 413 AGGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNSSqtkpersdLKWTGLD 492
Cdd:TIGR02339 404 AGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKG--------NKNAGIN 475
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 24649029 493 LIEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMI 534
Cdd:TIGR02339 476 VFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVI 517
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
24-539 |
2.03e-139 |
|
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: 413.99 E-value: 2.03e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 24 NVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEVGDGTTSVVILAAEL 103
Cdd:cd03340 21 NINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 104 LKNADELVKQKIHPTSIISGYRIACKEACKYISE---HLTAPVDELGRDSLINIAKTSMSSKIIGADAEFFSAMVVDAAQ 180
Cdd:cd03340 101 LKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEiavNIDKEDKEEQRELLEKCAATALNSKLIASEKEFFAKMVVDAVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 181 SVKITDPrgqaaysIKAINVLKAHGKSARESVLIPGYALNCTIAS---QQMPKKIVNAKIACLDFSLQKTKMKMGVQVLI 257
Cdd:cd03340 181 SLDDDLD-------LDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYagfEQQPKKFKNPKILLLNVELELKAEKDNAEVRV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 258 NDPDKLEAIRARELDITKERINMILGTGVNVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATGAAFITSLTNM 337
Cdd:cd03340 254 EDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQTTVSNI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 338 DgEESFDASMVGEAAEVAQERICddelILIKGTKARaAASIILRGPNDFYCDEMERSVHDALCVVKRVLESKKVVAGGGC 417
Cdd:cd03340 334 T-DDVLGTCGLFEERQVGGERYN----IFTGCPKAK-TCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 418 VEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHnssqtkpERSDLKWTGLDLIEGV 497
Cdd:cd03340 408 IEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKH-------AQGGGKWYGVDINNEG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 24649029 498 VRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMIKlNPE 539
Cdd:cd03340 481 IADNFEAFVWEPSLVKINALTAATEAACLILSVDETIK-NPK 521
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
24-536 |
1.16e-120 |
|
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: 365.62 E-value: 1.16e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 24 NVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEVGDGTTSVVILAAEL 103
Cdd:TIGR02345 23 NINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 104 LKNADELVKQKIHPTSIISGYRIACKEACKYISEhLTAPVDEL---GRDSLINIAKTSMSSKIIGADAEFFSAMVVDAAQ 180
Cdd:TIGR02345 103 LKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKE-IAVTIDEEkgeQRELLEKCAATALSSKLISHNKEFFSKMIVDAVL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 181 SVKITDPRgqaaysIKAINVLKAHGKSARESVLIPGYALNCTIAS---QQMPKKIVNAKIACLDFSLQKTKMKMGVQVLI 257
Cdd:TIGR02345 182 SLDRDDLD------LKLIGIKKVQGGALEDSQLVNGVAFKKTFSYagfEQQPKKFANPKILLLNVELELKAEKDNAEIRV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 258 NDPDKLEAIRARELDITKERINMILGTGVNVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATGAAFITSLTNM 337
Cdd:TIGR02345 256 EDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTTSDL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 338 DGeESFDASMVGEAAEVAQERICddeliLIKGTKARAAASIILRGPNDFYCDEMERSVHDALCVVKRVLESKKVVAGGGC 417
Cdd:TIGR02345 336 EA-DVLGTCALFEERQIGSERYN-----YFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 418 VEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNssqtkperSDLKWTGLDLIEGV 497
Cdd:TIGR02345 410 IEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHA--------KGGKWYGVDINTED 481
|
490 500 510
....*....|....*....|....*....|....*....
gi 24649029 498 VRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMIKL 536
Cdd:TIGR02345 482 IGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITN 520
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
12-538 |
1.56e-118 |
|
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: 360.11 E-value: 1.56e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 12 GTRQSGASVRTQNVMAALSISNIVKSSLGPVGLDKML--VDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEV 89
Cdd:cd03336 6 AQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 90 GDGTTSVVILAAELLKNADELVKQKIHPTSIISGYRIACKEACKYIsehLTAPVD-----ELGRDSLINIAKTSMSSKII 164
Cdd:cd03336 86 GDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREAL---LSSAVDhssdeEAFREDLLNIARTTLSSKIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 165 GADAEFFSAMVVDAAQSVKitdprGQAaySIKAINVLKAHGKSARESVLIPGYALNCTIASQQmPKKIVNAKIACLDFSL 244
Cdd:cd03336 163 TQDKEHFAELAVDAVLRLK-----GSG--NLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTPM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 245 QKTKMKM-GVQVLINDPDKLEAIRARELDITKERINMILGTGVNVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIA 323
Cdd:cd03336 235 DTDKIKIfGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 324 KATGAAFITSLTNMD----GE-ESFDASMVGEaaevaqericdDELILIKGTKARAAASIILRGPNDFYCDEMERSVHDA 398
Cdd:cd03336 315 LVTGGEIASTFDHPElvklGTcKLIEEIMIGE-----------DKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 399 LCVVKRVLESKKVVAGGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNSSQ 478
Cdd:cd03336 384 LCVLAQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGN 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 479 TKpersdlkwTGLDLIEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMIKLNP 538
Cdd:cd03336 464 TT--------AGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKCAP 515
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
18-534 |
1.98e-117 |
|
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: 356.98 E-value: 1.98e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 18 ASVRTQNVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEVGDGTTSVV 97
Cdd:cd03338 7 ADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 98 ILAAELLKNADELVKQKIHPTSIISGYRIACKEACKYISEhLTAPVDELGRDSLINIAKTSMSSKIIGADAEFFSAMVVD 177
Cdd:cd03338 87 VLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDS-MSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 178 AAqsVKITDPRGQAAYSIKAINVLKAHGKSARESVLIPGYALNCTIASQ-QMPKKIVNAKIACLDFSLQKTKMKMGVQVL 256
Cdd:cd03338 166 AV--LKVIDPATATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKaGGPTRIEKAKIGLIQFCLSPPKTDMDNNIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 257 INDPDKLEAIRARELDITKERINMILGTGVNVVLVSG-----GVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATGAAFI 331
Cdd:cd03338 244 VNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQKsilrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 332 TSLtnmdgeESFDASMVGEAAEVAQERICDDELILIKGTK-ARAAASIILRGPNDFYCDEMERSVHDALCVVKRVLESKK 410
Cdd:cd03338 324 ASI------DHFTEDKLGSADLVEEVSLGDGKIVKITGVKnPGKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 411 VVAGGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNSSQtkpersdlKWTG 490
Cdd:cd03338 398 LIPGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGE--------KNAG 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 24649029 491 LDLIEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMI 534
Cdd:cd03338 470 INVRKGAITNILEENVVQPLLVSTSAITLATETVRMILKIDDIV 513
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
17-543 |
6.42e-116 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 353.95 E-value: 6.42e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 17 GASVRTQNVMAALSISNIVKSSLGPVGLDKMLV-----DDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEVGD 91
Cdd:PTZ00212 20 GETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 92 GTTSVVILAAELLKNADELVKQKIHPTSIISGYRIACKEACKYISEhltAPVD-----ELGRDSLINIAKTSMSSKIIGA 166
Cdd:PTZ00212 100 GTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEE---IAFDhgsdeEKFKEDLLNIARTTLSSKLLTV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 167 DAEFFSAMVVDAAQSVKitdprgqAAYSIKAINVLKAHGKSARESVLIPGYALNCTIASQQmPKKIVNAKIACLDFSLQK 246
Cdd:PTZ00212 177 EKDHFAKLAVDAVLRLK-------GSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVGQ-PKRLENCKILVANTPMDT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 247 TKMKM-GVQVLINDPDKLEAIRARELDITKERINMILGTGVNVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKA 325
Cdd:PTZ00212 249 DKIKIyGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 326 TGAAFITsltnmdgeeSFDA---SMVGEAAEVAQERICDDELILIKGTKARAAASIILRGPNDFYCDEMERSVHDALCVV 402
Cdd:PTZ00212 329 LGAEIVS---------TFDTpekVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 403 KRVLESKKVVAGGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNSSQTKpe 482
Cdd:PTZ00212 400 SQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKT-- 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24649029 483 rsdlkwTGLDLIEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMIKLNPEDKSG 543
Cdd:PTZ00212 478 ------AGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRCAPRQREQ 532
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
12-535 |
1.36e-107 |
|
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: 331.96 E-value: 1.36e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 12 GTRQSGASVRTQNVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEVGD 91
Cdd:cd03339 16 KKRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 92 GTTSVVILAAELLKNADELVKQKIHPTSIISGYRIACKEACKYISE-HLTAPVDELGRDSLINIAKTSMSSKIIGADAEF 170
Cdd:cd03339 96 GTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEiADKIEFSPDNKEPLIQTAMTSLGSKIVSRCHRQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 171 FSAMVVDAAQSVKITDPRGqaaYSIKAINVLKAHGKSARESVLIPGYALNCTIASQQMPKKIVNAKIACLDFSLQKTKMK 250
Cdd:cd03339 176 FAEIAVDAVLSVADLERKD---VNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIAILTCPFEPPKPK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 251 MGVQVLINDPDKLEAIRARELDITKERINMILGTGVNVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATGAAF 330
Cdd:cd03339 253 TKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 331 ITSLTNMDGEESFDASMVGEAAEVAQEricdDELILIKGTKARAAASIILRGPNDFYCDEMERSVHDALCVVKRVLESKK 410
Cdd:cd03339 333 VPRFEDLSPEKLGKAGLVREISFGTTK----DKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 411 VVAGGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRsyhnSSQTKPERSDLkwtG 490
Cdd:cd03339 409 IVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVK----ARQVKEKNPHL---G 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 24649029 491 LDLIEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMIK 535
Cdd:cd03339 482 IDCLGRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
14-534 |
3.36e-106 |
|
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: 326.95 E-value: 3.36e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 14 RQSGASVRTQNVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEVGDGT 93
Cdd:cd03337 11 RESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 94 TSVVILAAELLKNADELVKQKIHPTSIISGYRIACKEACKyISEHLTAPVDELGRDSLINIAKTSMSSKIIGADAEFFSA 173
Cdd:cd03337 91 TSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALK-ILEEISIPVDVNDRAQMLKIIKSCIGTKFVSRWSDLMCN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 174 MVVDAAQSVKITDPRGQAAYSIKA-INVLKAHGKSARESVLIPGYALNCTIASQQMPKKIVNAKIACLDFSLQKtkmkmg 252
Cdd:cd03337 170 LALDAVKTVAVEENGRKKEIDIKRyAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPLEY------ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 253 vqvlindpdkleairarelditkerinmilgtgvnVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATGAAfIT 332
Cdd:cd03337 244 -----------------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARACGAT-IV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 333 SLTnmdgeESFDASMVGEAAEVAQERICDDE-LILIKGTKARAAASIILRGPNDFYCDEMERSVHDALCVVKRVLESKKV 411
Cdd:cd03337 288 NRP-----EELTESDVGTGAGLFEVKKIGDEyFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILNPKL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 412 VAGGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHnssqTKPERSdlkWTGL 491
Cdd:cd03337 363 VPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKH----AQGENS---TWGI 435
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 24649029 492 DLIEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMI 534
Cdd:cd03337 436 DGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
12-535 |
1.54e-102 |
|
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: 319.44 E-value: 1.54e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 12 GTRQSGASVRTQNVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEVGD 91
Cdd:TIGR02343 20 KKRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 92 GTTSVVILAAELLKNADELVKQKIHPTSIISGYRIACKEACKYISE-HLTAPVDELGRDSLINIAKTSMSSKIIGADAEF 170
Cdd:TIGR02343 100 GTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEiSDEISADNNNREPLIQAAKTSLGSKIVSKCHRR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 171 FSAMVVDAAQSVKITDPRGqaaYSIKAINVLKAHGKSARESVLIPGYALNCTIASQQMPKKIVNAKIACLDFSLQKTKMK 250
Cdd:TIGR02343 180 FAEIAVDAVLNVADMERRD---VDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAILTCPFEPPKPK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 251 MGVQVLINDPDKLEAIRARELDITKERINMILGTGVNVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATGAAF 330
Cdd:TIGR02343 257 TKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 331 ITSLtnmdgeESFDASMVGEAAEVAQERI--CDDELILIKGTKARAAASIILRGPNDFYCDEMERSVHDALCVVKRVLES 408
Cdd:TIGR02343 337 VPRF------QELSKDKLGKAGLVREISFgtTKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 409 KKVVAGGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNsSQTKPErsdlkw 488
Cdd:TIGR02343 411 SRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQL-KEKNPN------ 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24649029 489 TGLDLIEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMIK 535
Cdd:TIGR02343 484 LGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVIS 530
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
18-534 |
3.95e-102 |
|
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: 317.88 E-value: 3.95e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 18 ASVRTQNVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEVGDGTTSVV 97
Cdd:TIGR02342 8 QDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 98 ILAAELLKNADELVKQKIHPTSIISGYRIACKEACKYISEhLTAPVDELGRDSLINIAKTSMSSKIIGADAEFFSAMVVD 177
Cdd:TIGR02342 88 ILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDE-MSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 178 AAqsVKITDPRGQAAYSIKAINVLKAHGKSARESVLIPGYAL-NCTIASQQMPKKIVNAKIACLDFSLQKTKMKMGVQVL 256
Cdd:TIGR02342 167 AV--LKVIDPENAKNVDLNDIKVVKKLGGTIDDTELIEGLVFtQKASKSAGGPTRIEKAKIGLIQFQISPPKTDMENQII 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 257 INDPDKLEAIRARELDITKERINMILGTGVNVVLVS-----GGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATGAAFI 331
Cdd:TIGR02342 245 VNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQksilrDAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 332 TSLtnmdgeESFDASMVGEAAEVAQERICDDELILIKGTK-ARAAASIILRGPNDFYCDEMERSVHDALCVVKRVLESKK 410
Cdd:TIGR02342 325 ASI------DHFTADKLGSAELVEEVDSDGGKIIKITGIQnAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 411 VVAGGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNSSQtkpersdlKWTG 490
Cdd:TIGR02342 399 LIAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGE--------KTAG 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 24649029 491 LDLIEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMI 534
Cdd:TIGR02342 471 ISVRKGGITNMLEEHVLQPLLVTTSAITLASETVRSILKIDDIV 514
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
17-544 |
9.91e-102 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 315.86 E-value: 9.91e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 17 GASVRTQNVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHP----AAKVLVELAQLQDEEVGDG 92
Cdd:COG0459 8 GEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 93 TTSVVILAAELLKNADELVKQKIHPTSIISGYRIACKEACKYISEhLTAPVDelGRDSLINIAKTSMSSKiigadaEFFS 172
Cdd:COG0459 88 TTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKK-IAKPVD--DKEELAQVATISANGD------EEIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 173 AMVVDAAQSVkitdprGQAAYsikaINVLKAhGKSARESVLIPGYALNCTIAS-------QQMPKKIVNAKIACLDfslq 245
Cdd:COG0459 159 ELIAEAMEKV------GKDGV----ITVEEG-KGLETELEVVEGMQFDKGYLSpyfvtdpEKMPAELENAYILLTD---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 246 ktkmkmgvqvlindpDKLEAIraRELditKERINMILGTGVNVVLVSGGVDDLCMKYFVEAGAMAVRRV----------- 314
Cdd:COG0459 224 ---------------KKISSI--QDL---LPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgdr 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 315 KKSDLKIIAKATGAAFITSLTNMDgEESFDASMVGEAAEVaqeRICDDELILIKGTKARAAASIILRGPNDFYCDEMERS 394
Cdd:COG0459 284 RKAMLEDIAILTGGRVISEDLGLK-LEDVTLDDLGRAKRV---EVDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 395 VHDALCVVKRVLESkKVVAGGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSyh 474
Cdd:COG0459 360 VEDALHATRAAVEE-GIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRA-- 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 475 nssqtkperSDLKWTGLDLIEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMIKLNPEDKSGK 544
Cdd:COG0459 437 ---------AKDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
8-534 |
4.36e-99 |
|
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: 310.13 E-value: 4.36e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 8 LSIAGTRQSGASVRTQNVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDE 87
Cdd:TIGR02344 5 LNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 88 EVGDGTTSVVILAAELLKNADELVKQKIHPTSIISGYRIACKEACKYISEhLTAPVDELGRDSLINIAKTSMSSKIIGAD 167
Cdd:TIGR02344 85 EVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEE-ISIPVDVNDDAAMLKLIQSCIGTKFVSRW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 168 AEFFSAMVVDAAQSVKItDPRGQAAYSIKA-INVLKAHGKSARESVLIPGYALNCTIASQQMPKKIVNAKIACLDFSLQK 246
Cdd:TIGR02344 164 SDLMCDLALDAVRTVQR-DENGRKEIDIKRyAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 247 TKMKMGVQVLINDPDKLEAIRARELDITKERINMILGTGVNVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKAT 326
Cdd:TIGR02344 243 KKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARAC 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 327 GAAFITSLtnmdgeESFDASMVGEAAEVAQ-ERICDDELILIKGTKARAAASIILRGPNDFYCDEMERSVHDALCVVKRV 405
Cdd:TIGR02344 323 GATIVNRP------EELRESDVGTGCGLFEvKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 406 LESKKVVAGGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNSSQTkpersd 485
Cdd:TIGR02344 397 LLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENN------ 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 24649029 486 lKWTGLDLIEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMI 534
Cdd:TIGR02344 471 -CTWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
24-534 |
3.72e-94 |
|
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: 295.67 E-value: 3.72e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 24 NVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEVGDGTTSVVILAAEL 103
Cdd:cd03341 13 NIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 104 LKNADELVKQKIHPTSIISGYRIACKEACKYISEHLTAPV-DELGRDSLINIAKTSMSSKIIGADaEFFSAMVVDAAQSV 182
Cdd:cd03341 93 LEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIeDLRNKEEVSKALKTAIASKQYGNE-DFLSPLVAEACISV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 183 KITDPRgqaAYSIKAINVLKAHGKSARESVLIPGYALNcTIASQQMpKKIVNAKIACLdfslqktkmkmgvqvlindpdk 262
Cdd:cd03341 172 LPENIG---NFNVDNIRVVKILGGSLEDSKVVRGMVFK-REPEGSV-KRVKKAKVAVF---------------------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 263 leairarelditkeriNMILGTGVNVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATGAAFITSLTNMDGEEs 342
Cdd:cd03341 225 ----------------SCPFDIGVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEE- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 343 fdasmVGEAAEVAQERICDDELILIKGTK-ARAAASIILRGPNDFYCDEMERSVHDALCVVKRVLESKKVVAGGGCVEAA 421
Cdd:cd03341 288 -----IGYCDSVYVEEIGDTKVVVFRQNKeDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 422 LSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNSSQTKpersdlkwTGLDLIEGV--VR 499
Cdd:cd03341 363 LAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKS--------AGVDIESGDegTK 434
|
490 500 510
....*....|....*....|....*....|....*
gi 24649029 500 DNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMI 534
Cdd:cd03341 435 DAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
12-538 |
2.54e-93 |
|
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT beta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274082 Cd Length: 519 Bit Score: 294.84 E-value: 2.54e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 12 GTRQSGASVRTQNVMAALSISNIVKSSLGPVGLDKMLVDD--IGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEV 89
Cdd:TIGR02341 7 ADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSssDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 90 GDGTTSVVILAAELLKNADELVKQKIHPTSIISGYRIACKEAckyiSEHLTAPVDELG------RDSLINIAKTSMSSKI 163
Cdd:TIGR02341 87 GDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAA----RDALLKSAVDNGsdevkfRQDLMNIARTTLSSKI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 164 IGADAEFFSAMVVDAAQSVKitdprgqAAYSIKAINVLKAHGKSARESVLIPGYALNCTIASQQmPKKIVNAKIACLDFS 243
Cdd:TIGR02341 163 LSQHKDHFAQLAVDAVLRLK-------GSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 244 LQKTKMKM-GVQVLINDPDKLEAIRARELDITKERINMILGTGVNVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKII 322
Cdd:TIGR02341 235 MDTDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 323 AKATGAAFITSLtnmdgeESFDASMVGEAAEVAQERICDDELILIKGTKARAAASIILRGPNDFYCDEMERSVHDALCVV 402
Cdd:TIGR02341 315 ALVTGGEIVSTF------DHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 403 KRVLESKKVVAGGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNSSQTKpe 482
Cdd:TIGR02341 389 SQTVKESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTT-- 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 24649029 483 rsdlkwTGLDLIEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMIKLNP 538
Cdd:TIGR02341 467 ------MGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAP 516
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
23-538 |
1.79e-91 |
|
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: 290.46 E-value: 1.79e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 23 QNVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEVGDGTTSVVILAAE 102
Cdd:TIGR02346 22 KNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 103 LLKNADELVKQKIHPTSIISGYRIACKEACKYISEHLTAPVDEL-GRDSLINIAKTSMSSKIIGaDAEFFSAMVVDAAQS 181
Cdd:TIGR02346 102 LLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDLrDKDELIKALKASISSKQYG-NEDFLAQLVAQACST 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 182 VKitdPRGQAAYSIKAINVLKAHGKSARESVLIPGYALNCTiaSQQMPKKIVNAKIACLDFSLQKTKMKMGVQVLINDPD 261
Cdd:TIGR02346 181 VL---PKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNRE--AEGSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNAE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 262 KLEAIRARELDITKERINMILGTGVNVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATGAAFITSLTNMDGEE 341
Cdd:TIGR02346 256 ELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 342 sfdasmVGEAAEVAQERICDDELILIKGTKARAA-ASIILRGPNDFYCDEMERSVHDALCVVKRVLESKKVVAGGGCVEA 420
Cdd:TIGR02346 336 ------IGYVDSVYVSEIGGDKVTVFKQENGDSKiSTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEI 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 421 ALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNSSQTKpersdlkwTGLDLIEGV--V 498
Cdd:TIGR02346 410 ELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKS--------KGIDIEAESdgV 481
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 24649029 499 RDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMIKLNP 538
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 ... |
24-535 |
7.27e-74 |
|
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: 244.26 E-value: 7.27e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 24 NVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEVGDGTTSVVILAAEL 103
Cdd:TIGR02347 21 NINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 104 LKNADELVKQKIHPTSIISGYRIACKEACKYISEHLTAPVDELGRDSLINIAKTSMSSKIIGADAEFFSAMVVDAAQSVK 183
Cdd:TIGR02347 101 LKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEVDREFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 184 itdpRGQAAYSIKAINVLKAHGKSARESVLIPGYALNCTIASQQMPKKIVNAKIACLDFSLQKTKMKMGVQVLINDPDKL 263
Cdd:TIGR02347 181 ----KDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 264 EAIRARELDITKERINMIL-------GTGVN---VVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATGAAFITS 333
Cdd:TIGR02347 257 EKLVKAERKFVDDRVKKIIelkkkvcGKSPDkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEALNS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 334 LTNMDGEEsfdasmVGEAAEVAQERICDDELILIKGTKARAAASIILRGPNDFYCDEMERSVHDALCVVKRVLESKKVVA 413
Cdd:TIGR02347 337 VEDLTPEC------LGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVP 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 414 GGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNSSQtkpersdlKWTGLDL 493
Cdd:TIGR02347 411 GAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGG--------EVVGVDL 482
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 24649029 494 IEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMIK 535
Cdd:TIGR02347 483 NTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMR 524
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
15-535 |
9.69e-74 |
|
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: 242.55 E-value: 9.69e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 15 QSGASVRTqNVMAALSISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVELAQLQDEEVGDGTT 94
Cdd:cd03342 9 RRGQALAV-NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 95 SVVILAAELLKNADELVKQKIHPTSIISGYRIACKEACKYISEHLTAPVDELGRDSLINIAKTSMSSKIIGADAEFFSAM 174
Cdd:cd03342 88 SNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDTDRELLLSVARTSLRTKLHADLADQLTEI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 175 VVDAAQSVKitdpRGQAAYSIKAINVLKAHGKSARESVLIPGYALNCTIASQQMPKKIVNAKIACLDFSLQktkmkmgvq 254
Cdd:cd03342 168 VVDAVLAIY----KPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLE--------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 255 vlindpdkleairareldITKERINmilgTGV--NVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATGAAFIT 332
Cdd:cd03342 235 ------------------YEKTEVN----SGFfySVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 333 SLTNMDGEEsfdasmVGEAAEVAQERICDDELILIKGTKARAAASIILRGPNDFYCDEMERSVHDALCVVKRVLESKKVV 412
Cdd:cd03342 293 SVDDLSPEC------LGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 413 AGGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIPKTLSVNAAKDATDLVAKLRSYHNSSQTKPersdlkwtGLD 492
Cdd:cd03342 367 PGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVG--------GVD 438
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 24649029 493 LIEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMIK 535
Cdd:cd03342 439 LDTGEPMDPESEGIWDNYSVKRQILHSATVIASQLLLVDEIIR 481
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
148-408 |
3.45e-62 |
|
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: 203.47 E-value: 3.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 148 RDSLINIAKTSMSSKIiGADAEFFSAMVVDAAQSVKITDPRgqaaYSIKAINVLKAHGKSARESVLIPGYALNCTIASQQ 227
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNRM----DDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 228 MPKKIVNAKIACLDFSLQktkmkmgvqvlindpdkleairarelditkerinmilgtgvNVVLVSGGVDDLCMKYFVEAG 307
Cdd:cd03333 76 MPKRLENAKILLLDCPLE-----------------------------------------YVVIAEKGIDDLALHYLAKAG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 308 AMAVRRVKKSDLKIIAKATGAAFITSLtnmdgeESFDASMVGEAAEVAQERICDDELILIKGTKARAAASIILRGPNDFY 387
Cdd:cd03333 115 IMAVRRVKKEDLERIARATGATIVSSL------EDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVE 188
|
250 260
....*....|....*....|.
gi 24649029 388 CDEMERSVHDALCVVKRVLES 408
Cdd:cd03333 189 LDEVKRSLHDALCAVRAAVEE 209
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
178-427 |
2.92e-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: 66.86 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 178 AAQSVKiTDPRGQAAYSIKA-INVLKAHGKSARESVLIPGYALNCTIASQQMPKKIVNAKIACLDFSLqktkmkmGVQVL 256
Cdd:cd03334 30 AASNVK-PDVRAGDDMDIRQyVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPL-------EYQRV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 257 INDPDKLEAIRARELDITKERINMILGTGVNVVLVSGGVDDLCMKYFVEAGAMAVRRVKKSDLKIIAKATGAAFITSltn 336
Cdd:cd03334 102 ENKLLSLDPVILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISS--- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 337 mdGEESFDASMVGEAAEVAQERICDDE-----LILIKGTKARAAASIILRGPNdfycdemersvHDALCVVKRVLESkkv 411
Cdd:cd03334 179 --MDDLLTSPKLGTCESFRVRTYVEEHgrsktLMFFEGCPKELGCTILLRGGD-----------LEELKKVKRVVEF--- 242
|
250
....*....|....*.
gi 24649029 412 vagggCVEAALSIYLE 427
Cdd:cd03334 243 -----MVFAAYHLKLE 253
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
31-158 |
4.36e-09 |
|
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: 59.01 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 31 ISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHP----AAKVLVELAQLQDEEVGDGTTSVVILAAELLKN 106
Cdd:cd03344 20 LADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLARAIIKE 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 24649029 107 ADELVKQKIHPTSIISGYRIACKEACKYISEhLTAPVDelGRDSLINIAKTS 158
Cdd:cd03344 100 GLKAVAAGANPMDLKRGIEKAVEAVVEELKK-LSKPVK--TKEEIAQVATIS 148
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
31-138 |
4.44e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 55.88 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 31 ISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHP----AAKVLVELAQLQDEEVGDGTTSVVILAAELLKN 106
Cdd:PRK12850 23 LANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110
....*....|....*....|....*....|..
gi 24649029 107 ADELVKQKIHPTSIISGYRIACKEACKYISEH 138
Cdd:PRK12850 103 GAKLVAAGMNPMDLKRGIDLAVAAVVDELKKI 134
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
31-158 |
9.49e-08 |
|
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: 54.61 E-value: 9.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 31 ISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHP----AAKVLVELAQLQDEEVGDGTTSVVILAAELLKN 106
Cdd:TIGR02348 21 LADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVASKTNDVAGDGTTTATVLAQAIVKE 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 24649029 107 ADELVKQKIHPTSIISGYRIACKEACKYIsEHLTAPVDelGRDSLINIAKTS 158
Cdd:TIGR02348 101 GLKNVAAGANPIELKRGIEKAVEAVVEEL-KKLSKPVK--GKKEIAQVATIS 149
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
35-158 |
1.27e-06 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 51.07 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 35 VKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPA----AKVLVELAQLQDEEVGDGTTSVVILAAELLKNADEL 110
Cdd:PTZ00114 38 VAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKAGDGTTTATILARAIFREGCKA 117
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 24649029 111 VKQKIHPTSIISGYRIACKEACKYISEhLTAPVDelGRDSLINIAKTS 158
Cdd:PTZ00114 118 VAAGLNPMDLKRGIDLAVKVVLESLKE-QSRPVK--TKEDILNVATIS 162
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
33-100 |
3.02e-06 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 49.81 E-value: 3.02e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24649029 33 NIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHP----AAKVLVELAQLQDEEVGDGTTSVVILA 100
Cdd:PRK12849 24 DAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLA 95
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
31-105 |
4.43e-06 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 49.35 E-value: 4.43e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24649029 31 ISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHP----AAKVLVELAQLQDEEVGDGTTSVVILAAELLK 105
Cdd:PRK12851 23 LADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAIVR 101
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
31-546 |
5.36e-06 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 49.15 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 31 ISNIVKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHP----AAKVLVELAQLQDEEVGDGTTSVVILAAELLKN 106
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 107 ADELVKQKIHPTSIISGyriackeackyISEHLTAPVDELgrdsliniakTSMSSKIigADAEFFSAMVVDAAQSVKITD 186
Cdd:PLN03167 158 GVKVVAAGANPVQITRG-----------IEKTAKALVKEL----------KKMSKEV--EDSELADVAAVSAGNNYEVGN 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 187 PRGQAAYSIKAINVLK-AHGKSARESVLI-------PGYALNCTIA-SQQMPKKIVNAKIACLDFSLQKTKMKMGVQVli 257
Cdd:PLN03167 215 MIAEAMSKVGRKGVVTlEEGKSAENNLYVvegmqfdRGYISPYFVTdSEKMSVEYDNCKLLLVDKKITNARDLIGILE-- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 258 ndpdklEAIRAR------ELDITKER-----INMILGTGVNVVLVSGGVDDLCMKYF----VEAGAMAVR-----RVKKS 317
Cdd:PLN03167 293 ------DAIRGGyplliiAEDIEQEAlatlvVNKLRGSLKIAALKAPGFGERKSQYLddiaILTGGTVIReevglSLDKV 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 318 DLKIIAKATGAAFITSLTNMDGEESFDASMVGEAAEV-----AQERICDDELILIKGTKARAAASIILRGPN-DFYCDEM 391
Cdd:PLN03167 367 GKEVLGTAAKVVLTKDTTTIVGDGSTQEAVNKRVAQIknlieAAEQDYEKEKLNERIAKLSGGVAVIQVGAQtETELKEK 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 392 ERSVHDALCVVKRVLEsKKVVAGGGCVEAALSIYLENFATSLASREQLAIAEFAKSLLVIP-KTLSVNAAKDATDLVAKL 470
Cdd:PLN03167 447 KLRVEDALNATKAAVE-EGIVVGGGCTLLRLASKVDAIKDTLENDEQKVGADIVKRALSYPlKLIAKNAGVNGSVVSEKV 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 471 RSYHNSSQtkpersdlkwtGLDLIEGVVRDNKKAGVLEPAMSKIKSLKFATEAAITILRIDDMI----------KLNPED 540
Cdd:PLN03167 526 LSNDNPKF-----------GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVveikepepvpAGNPMD 594
|
....*.
gi 24649029 541 KSGKSY 546
Cdd:PLN03167 595 NSGYGY 600
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
31-106 |
3.41e-04 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 43.19 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 31 ISNIVKSSLGP----VGLDKmlvdDIGDVTVTNDGATILRLLEVEHP----AAKVLVELAQLQDEEVGDGTTSVVILAA- 101
Cdd:PRK00013 22 LADAVKVTLGPkgrnVVLEK----SFGAPTITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLAQa 97
|
....*...
gi 24649029 102 ---ELLKN 106
Cdd:PRK00013 98 ivrEGLKN 105
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
35-182 |
4.71e-04 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 42.78 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649029 35 VKSSLGPVGLDKMLVDDIGDVTVTNDGATILRLLEVEHPAAKVLVEL----AQLQDEEVGDGTTSVVILAAELLKNADEL 110
Cdd:CHL00093 26 VSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALirqaASKTNDVAGDGTTTATVLAYAIVKQGMKN 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24649029 111 VKQKIHPTSIISGYRIACKEACKYISEHlTAPVDELgrDSLINIAktSMSSkiiGADAEfFSAMVVDAAQSV 182
Cdd:CHL00093 106 VAAGANPISLKRGIEKATQYVVSQIAEY-ARPVEDI--QAITQVA--SISA---GNDEE-VGSMIADAIEKV 168
|
|
| |
