|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
2-506 |
0e+00 |
|
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: 869.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 2 ELRLSNMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVV 81
Cdd:cd03338 8 DVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 82 LAGSFLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVDLNDRASLLRAASTSLNSKIVSQYSSTLAPIAVSAV 161
Cdd:cd03338 88 LAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 162 SRLVTP-TSSNVDLRDIRVVKKVGGTIEDTELVEGVVLNQNVIVSAGGPTRMEKAKIAIIQFQLSAPKPDMDNTVVINDY 240
Cdd:cd03338 168 LKVIDPaTATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKAGGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVNDY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 241 RQMDKVIKEGRQYILNLCKKIKKANCNVLLIQKSILRDAVDDVSLNFLKRLNILVVKDVERDEIEFLSKSLDCKPVADID 320
Cdd:cd03338 248 AQMDRILREERKYILNMCKKIKKSGCNVLLIQKSILRDAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVASID 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 321 AFTEDKLGYADLMEETNDNGVKVVRITGVKNRGRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIGGGGAPEI 400
Cdd:cd03338 328 HFTEDKLGSADLVEEVSLGDGKIVKITGVKNPGKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGAPEI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 401 HVSRLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHALGDGNAGINVRRGVISNILEEEVVQ 480
Cdd:cd03338 408 EIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITNILEENVVQ 487
|
490 500
....*....|....*....|....*.
gi 170088430 481 PLLVTTSAIELSTETVCLLLKIDDYV 506
Cdd:cd03338 488 PLLVSTSAITLATETVRMILKIDDIV 513
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
2-509 |
0e+00 |
|
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: 780.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 2 ELRLSNMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVV 81
Cdd:TIGR02342 9 DVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 82 LAGSFLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVDLNDRASLLRAASTSLNSKIVSQYSSTLAPIAVSAV 161
Cdd:TIGR02342 89 LAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 162 SRLVTP-TSSNVDLRDIRVVKKVGGTIEDTELVEGVVLNQNVIVSAGGPTRMEKAKIAIIQFQLSAPKPDMDNTVVINDY 240
Cdd:TIGR02342 169 LKVIDPeNAKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAGGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 241 RQMDKVIKEGRQYILNLCKKIKKANCNVLLIQKSILRDAVDDVSLNFLKRLNILVVKDVERDEIEFLSKSLDCKPVADID 320
Cdd:TIGR02342 249 AQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSILRDAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASID 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 321 AFTEDKLGYADLMEETNDNGVKVVRITGVKNRGRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIGGGGAPEI 400
Cdd:TIGR02342 329 HFTADKLGSAELVEEVDSDGGKIIKITGIQNAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPEI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 401 HVSRLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHALGDGNAGINVRRGVISNILEEEVVQ 480
Cdd:TIGR02342 409 EIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITNMLEEHVLQ 488
|
490 500
....*....|....*....|....*....
gi 170088430 481 PLLVTTSAIELSTETVCLLLKIDDYVQAR 509
Cdd:TIGR02342 489 PLLVTTSAITLASETVRSILKIDDIVFTR 517
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
2-506 |
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: 537.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 2 ELRLSNMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVV 81
Cdd:cd00309 8 EARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDGTTTVVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 82 LAGSFLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVDLNDRASLLRAASTSLNSKIVSQYSSTLAPIAVSAV 161
Cdd:cd00309 88 LAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLGELVVDAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 162 SRlVTPTSSNVDLRDIRVVKKVGGTIEDTELVEGVVLNQNVIvSAGGPTRMEKAKIAIIQFQLSapkpdmdnTVVINdyr 241
Cdd:cd00309 168 LK-VGKENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYL-SPYMPKRLENAKILLLDCKLE--------YVVIA--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 242 qmdkvikegrqyilnlckkikkancnvlliqksilRDAVDDVSLNFLKRLNILVVKDVERDEIEFLSKSLDCKPVADIDA 321
Cdd:cd00309 235 -----------------------------------EKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLED 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 322 FTEDKLGYADLMEETNDNGVKVVRITGVKNrGRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIGGGGAPEIH 401
Cdd:cd00309 280 LTPEDLGTAGLVEETKIGDEKYTFIEGCKG-GKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGAAEIE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 402 VSRLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHALGDGNAGINVRRGVISNILEEEVVQP 481
Cdd:cd00309 359 LSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKEAGIIDP 438
|
490 500
....*....|....*....|....*
gi 170088430 482 LLVTTSAIELSTETVCLLLKIDDYV 506
Cdd:cd00309 439 LKVKRQALKSATEAASLILTIDDII 463
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
14-509 |
2.68e-177 |
|
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: 507.51 E-value: 2.68e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 14 ISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVVLAGSFLGAAEKM 93
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 94 LQKGIHPTIVAESFIKASAKAVEYLTDI-SIPVDLNDRASLLRAASTSLNSKIVSQYSSTLAPIAVSAVSrLVTPTSSNV 172
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVL-AIPKNDGSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 173 DLRDIRVVKKVGGTIEDTELVEGVVLNQNViVSAGGPTRMEKAKIAIIQFQLSAPKPDMDNTVVINDYRQMDKVIKEGRQ 252
Cdd:pfam00118 160 DLGNIGVVKILGGSLEDSELVDGVVLDKGP-LHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 253 YILNLCKKIKKANCNVLLIQKSIlrdavDDVSLNFLKRLNILVVKDVERDEIEFLSKSLDCKPVADIDAFTEDKLGYADL 332
Cdd:pfam00118 239 QILEIVEKIIDSGVNVVVCQKGI-----DDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 333 MEETNDNGVKVVRITGVKNrGRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIGGGGAPEIHVSRLLSQYAQS 412
Cdd:pfam00118 314 VEEEKIGDEKYTFIEGCKS-PKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 413 LKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHALGDGNAGINVRRGVISNILEEEVVQPLLVTTSAIELS 492
Cdd:pfam00118 393 VSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSA 472
|
490
....*....|....*..
gi 170088430 493 TETVCLLLKIDDYVQAR 509
Cdd:pfam00118 473 TEAASTILRIDDIIKAK 489
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
6-508 |
7.02e-170 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 489.40 E-value: 7.02e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 6 SNMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVVLAGS 85
Cdd:NF041082 21 NNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 86 FLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVDLNDRASLLRAASTSLNSKIVSQYSSTLAPIAVSAVSRLV 165
Cdd:NF041082 101 LLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVKAVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 166 TPT-SSNVDLRDIRVVKKVGGTIEDTELVEGVVLNQNViVSAGGPTRMEKAKIAIIQFQLSAPKPDMDNTVVINDYRQMD 244
Cdd:NF041082 181 EKDgGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKER-VHPGMPKRVENAKIALLDAPLEVKKTEIDAKISITDPDQLQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 245 KVIKEGRQYILNLCKKIKKANCNVLLIQKSIlrdavDDVSLNFLKRLNILVVKDVERDEIEFLSKSLDCKPVADIDAFTE 324
Cdd:NF041082 260 AFLDQEEKMLKEMVDKIADSGANVVFCQKGI-----DDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSIDDLSP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 325 DKLGYADLMEETNDNGVKVVRITGVKNrGRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIGGGGAPEIHVSR 404
Cdd:NF041082 335 EDLGYAGLVEERKVGGDKMIFVEGCKN-PKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEVELAL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 405 LLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHALGDGNAGINVRRGVISNILEEEVVQPLLV 484
Cdd:NF041082 414 RLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVVEPLRV 493
|
490 500
....*....|....*....|....
gi 170088430 485 TTSAIELSTETVCLLLKIDDYVQA 508
Cdd:NF041082 494 KTQAIKSATEAAVMILRIDDVIAA 517
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
6-509 |
2.84e-169 |
|
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: 487.93 E-value: 2.84e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 6 SNMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVVLAGS 85
Cdd:cd03343 19 MNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 86 FLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVDLNDRASLLRAASTSLNSKIVSQYSSTLAPIAVSAVSRLV 165
Cdd:cd03343 99 LLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAEAAKDKLADLVVDAVLQVA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 166 TPT--SSNVDLRDIRVVKKVGGTIEDTELVEGVVLNQNViVSAGGPTRMEKAKIAIIQFQLSAPKPDMDNTVVINDYRQM 243
Cdd:cd03343 179 EKRdgKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEV-VHPGMPKRVENAKIALLDAPLEVKKTEIDAKIRITSPDQL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 244 DKVIKEGRQYILNLCKKIKKANCNVLLIQKSIlrdavDDVSLNFLKRLNILVVKDVERDEIEFLSKSLDCKPVADIDAFT 323
Cdd:cd03343 258 QAFLEQEEAMLKEMVDKIADTGANVVFCQKGI-----DDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTNIDDLT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 324 EDKLGYADLMEETNDNGVKVVRITGVKNrGRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIGGGGAPEIHVS 403
Cdd:cd03343 333 PEDLGEAELVEERKVGDDKMVFVEGCKN-PKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGAVEIELA 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 404 RLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHALGDGNAGINVRRGVISNILEEEVVQPLL 483
Cdd:cd03343 412 KRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVDMLEKGVIEPLR 491
|
490 500
....*....|....*....|....*.
gi 170088430 484 VTTSAIELSTETVCLLLKIDDYVQAR 509
Cdd:cd03343 492 VKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
6-509 |
4.94e-163 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 472.13 E-value: 4.94e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 6 SNMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVVLAGS 85
Cdd:NF041083 21 NNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAVVLAGE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 86 FLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVDLNDRASLLRAASTSLNSKIVSQYSSTLAPIAVSAVSRLV 165
Cdd:NF041083 101 LLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKGVEEARDYLAEIAVKAVKQVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 166 TPT--SSNVDLRDIRVVKKVGGTIEDTELVEGVVLNQNViVSAGGPTRMEKAKIAIIQFQLSAPKPDMDNTVVINDYRQM 243
Cdd:NF041083 181 EKRdgKYYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEV-VHPGMPKRVENAKIALLDAPLEVKKTEIDAEIRITDPDQL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 244 DKVIKEGRQYILNLCKKIKKANCNVLLIQKSIlrdavDDVSLNFLKRLNILVVKDVERDEIEFLSKSLDCKPVADIDAFT 323
Cdd:NF041083 260 QKFLDQEEKMLKEMVDKIKATGANVVFCQKGI-----DDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVTNIDDLT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 324 EDKLGYADLMEETNDNGVKVVRITGVKNrGRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIGGGGAPEIHVS 403
Cdd:NF041083 335 PEDLGYAELVEERKVGDDKMVFVEGCKN-PKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGAPEVELA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 404 RLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHALGDGNAGINVRRGVISNILEEEVVQPLL 483
Cdd:NF041083 414 KRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVDMWELGVIEPLR 493
|
490 500
....*....|....*....|....*.
gi 170088430 484 VTTSAIELSTETVCLLLKIDDYVQAR 509
Cdd:NF041083 494 VKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
2-508 |
3.83e-162 |
|
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: 469.94 E-value: 3.83e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 2 ELRLSNMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVV 81
Cdd:TIGR02339 16 DAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 82 LAGSFLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVDLNDRASLLRAASTSLNSKIVSQYS-STLAPIAVSA 160
Cdd:TIGR02339 96 LAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSKASAEVAkDKLADLVVEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 161 VSRLVTPT---SSNVDLRDIRVVKKVGGTIEDTELVEGVVLNQNViVSAGGPTRMEKAKIAIIQFQLSAPKPDMDNTVVI 237
Cdd:TIGR02339 176 VKQVAELRgdgKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEV-VHPGMPKRVENAKIALLDAPLEVEKTEIDAKIRI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 238 NDYRQMDKVIKEGRQYILNLCKKIKKANCNVLLIQKSIlrdavDDVSLNFLKRLNILVVKDVERDEIEFLSKSLDCKPVA 317
Cdd:TIGR02339 255 TDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGI-----DDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 318 DIDAFTEDKLGYADLMEETNDNGVKVVRITGVKNrGRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIGGGGA 397
Cdd:TIGR02339 330 SIDEITESDLGYAELVEERKVGEDKMVFVEGCKN-PKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVAGGGA 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 398 PEIHVSRLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHALGDGNAGINVRRGVISNILEEE 477
Cdd:TIGR02339 409 VEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTGEIEDMLELG 488
|
490 500 510
....*....|....*....|....*....|.
gi 170088430 478 VVQPLLVTTSAIELSTETVCLLLKIDDYVQA 508
Cdd:TIGR02339 489 VIEPLRVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
6-504 |
7.19e-134 |
|
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: 397.83 E-value: 7.19e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 6 SNMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVVLAGS 85
Cdd:cd03339 27 SHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 86 FLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDIS--IPVDLNDRASLLRAASTSLNSKIVSQYSSTLAPIAVSAVSR 163
Cdd:cd03339 107 LLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIAdkIEFSPDNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAVLS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 164 LVTPTSSNVDLRDIRVVKKVGGTIEDTELVEGVVLNQNvIVSAGGPTRMEKAKIAIIQFQLSAPKPDMDNTVVINDYRQM 243
Cdd:cd03339 187 VADLERKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKD-FSHPQMPKEVKDAKIAILTCPFEPPKPKTKHKLDITSVEDY 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 244 DKVIKEGRQYILNLCKKIKKANCNVLLIQKSIlrdavDDVSLNFLKRLNILVVKDVERDEIEFLSKSLDCKPVADIDAFT 323
Cdd:cd03339 266 KKLQEYEQKYFREMVEQVKDAGANLVICQWGF-----DDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFEDLS 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 324 EDKLGYADLMEE-----TNDngvKVVRITGVKNrGRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIGGGGAP 398
Cdd:cd03339 341 PEKLGKAGLVREisfgtTKD---KMLVIEGCPN-SKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGGGAA 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 399 EIHVSRLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRH-ALGDGNAGINVRRGVISNILEEE 477
Cdd:cd03339 417 EISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPHLGIDCLGRGTNDMKEQK 496
|
490 500
....*....|....*....|....*..
gi 170088430 478 VVQPLLVTTSAIELSTETVCLLLKIDD 504
Cdd:cd03339 497 VFETLISKKQQILLATQVVKMILKIDD 523
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
1-506 |
7.63e-118 |
|
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: 357.19 E-value: 7.63e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 1 MELRLSNMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVV 80
Cdd:TIGR02343 26 LEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 81 VLAGSFLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDIS--IPVDLNDRASLLRAASTSLNSKIVSQYSSTLAPIAV 158
Cdd:TIGR02343 106 VLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISdeISADNNNREPLIQAAKTSLGSKIVSKCHRRFAEIAV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 159 SAVSRLVTPTSSNVDLRDIRVVKKVGGTIEDTELVEGVVLNQNvIVSAGGPTRMEKAKIAIIQFQLSAPKPDMDNTVVIN 238
Cdd:TIGR02343 186 DAVLNVADMERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKD-FSHPQMPKEVEDAKIAILTCPFEPPKPKTKHKLDIS 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 239 DYRQMDKVIKEGRQYILNLCKKIKKANCNVLLIQKSIlrdavDDVSLNFLKRLNILVVKDVERDEIEFLSKSLDCKPVAD 318
Cdd:TIGR02343 265 SVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGF-----DDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 319 IDAFTEDKLGYADLMEE-----TNDngvKVVRITGVKNrGRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIG 393
Cdd:TIGR02343 340 FQELSKDKLGKAGLVREisfgtTKD---RMLVIEQCKN-SKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVY 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 394 GGGAPEIHVSRLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHaLGDGNAGINVR-RGVISN 472
Cdd:TIGR02343 416 GGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQ-LKEKNPNLGVDcLGYGTN 494
|
490 500 510
....*....|....*....|....*....|....*
gi 170088430 473 ILEEE-VVQPLLVTTSAIELSTETVCLLLKIDDYV 506
Cdd:TIGR02343 495 DMKEQfVFETLIGKKQQILLATQLVRMILKIDDVI 529
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
5-508 |
1.71e-110 |
|
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: 337.72 E-value: 1.71e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 5 LSNMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVVLAG 84
Cdd:cd03340 19 ISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 85 SFLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVDLND----RASLLRAASTSLNSKIVSQYSSTLAPIAVSA 160
Cdd:cd03340 99 EFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDkeeqRELLEKCAATALNSKLIASEKEFFAKMVVDA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 161 VSRLvtptSSNVDLRDIRVVKKVGGTIEDTELVEGVVLnQNVIVSAG---GPTRMEKAKIAIIQFQLSApKPDMDNTVV- 236
Cdd:cd03340 179 VLSL----DDDLDLDMIGIKKVPGGSLEDSQLVNGVAF-KKTFSYAGfeqQPKKFKNPKILLLNVELEL-KAEKDNAEVr 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 237 INDYRQMDKVIKEGRQYILNLCKKIKKANCNVLLIQKSIlrdavDDVSLNFLKRLNILVVKDVERDEIEFLSKSLDCKPV 316
Cdd:cd03340 253 VEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPI-----GDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 317 ADIDAFTEDKLGYADLMEETNDNGVKVVRITGVKNrGRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIGGGG 396
Cdd:cd03340 328 TTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPK-AKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 397 APEIHVSRLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHALGDG-NAGINVRRGVISNILE 475
Cdd:cd03340 407 AIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGkWYGVDINNEGIADNFE 486
|
490 500 510
....*....|....*....|....*....|...
gi 170088430 476 EEVVQPLLVTTSAIELSTETVCLLLKIDDYVQA 508
Cdd:cd03340 487 AFVWEPSLVKINALTAATEAACLILSVDETIKN 519
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
4-509 |
3.05e-108 |
|
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: 331.99 E-value: 3.05e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 4 RLSNMVAAKAISDAVRTSLGPRGMDKMIQTS--KGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVV 81
Cdd:cd03336 15 RLSSFVGAIAIGDLVKTTLGPKGMDKILQSVgrSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDGTTSVTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 82 LAGSFLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVDLND---RASLLRAASTSLNSKIVSQYSSTLAPIAV 158
Cdd:cd03336 95 LAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEeafREDLLNIARTTLSSKILTQDKEHFAELAV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 159 SAVSRLvtptSSNVDLRDIRVVKKVGGTIEDTELVEGVVLNQNVIVsaGGPTRMEKAKIAIiqfqlsAPKPdMDN----- 233
Cdd:cd03336 175 DAVLRL----KGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGV--NQPKRIENAKILI------ANTP-MDTdkiki 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 234 ---TVVINDYRQMDKVIKEGRQYILNLCKKIKKANCNVLliqksILRDAVDDVSLNFLKRLNILVVKDVERDEIEFLSKS 310
Cdd:cd03336 242 fgaKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCF-----INRQLIYNYPEQLFADAGIMAIEHADFDGVERLALV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 311 LDCKPVADIDAFTEDKLGYADLMEETNDNGVKVVRITGVKnRGRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRA 390
Cdd:cd03336 317 TGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVA-AGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 391 LIGGGGAPEIHVSRLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHALGDGNAGINVRRGVI 470
Cdd:cd03336 396 VVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTV 475
|
490 500 510
....*....|....*....|....*....|....*....
gi 170088430 471 SNILEEEVVQPLLVTTSAIELSTETVCLLLKIDDYVQAR 509
Cdd:cd03336 476 GDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKCA 514
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
4-508 |
4.03e-108 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 331.99 E-value: 4.03e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 4 RLSNMVAAKAISDAVRTSLGPRGMDKMIQTSK-----GEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTS 78
Cdd:PTZ00212 24 RLQSFVGAIAVADLVKTTLGPKGMDKILQPMSegprsGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGDGTTS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 79 VVVLAGSFLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVDLND---RASLLRAASTSLNSKIVSQYSSTLAP 155
Cdd:PTZ00212 104 VVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEekfKEDLLNIARTTLSSKLLTVEKDHFAK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 156 IAVSAVSRLvtPTSSNVDLrdIRVVKKVGGTIEDTELVEGVVLNQNVIVsaGGPTRMEKAKIaiiqfqLSAPKPdMDN-- 233
Cdd:PTZ00212 184 LAVDAVLRL--KGSGNLDY--IQIIKKPGGTLRDSYLEDGFILEKKIGV--GQPKRLENCKI------LVANTP-MDTdk 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 234 ------TVVINDYRQMDKVIKEGRQYILNLCKKIKKANCNVLliqksILRDAVDDVSLNFLKRLNILVVKDVERDEIEFL 307
Cdd:PTZ00212 251 ikiygaKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVF-----INRQLIYNYPEQLFAEAGIMAIEHADFDGMERL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 308 SKSLDCKPVADIDAFTEDKLGYADLMEETNDNGVKVVRITGVKnRGRTVSILAMGSNHLVVDECERSLHDALCVVRCLVK 387
Cdd:PTZ00212 326 AAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCA-KGEACTIVLRGASTHILDEAERSLHDALCVLSQTVK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 388 KRALIGGGGAPEIHVSRLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHALGDGNAGINVRR 467
Cdd:PTZ00212 405 DTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGIDMEK 484
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 170088430 468 GVISNILEEEVVQPLLVTTSAIELSTETVCLLLKIDDYVQA 508
Cdd:PTZ00212 485 GTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRC 525
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
4-506 |
2.01e-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: 325.79 E-value: 2.01e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 4 RLSNMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVVLA 83
Cdd:cd03337 18 QLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 84 GSFLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVDLNDRASLLRAASTSLNSKIVSQYSSTLAPIAVSAVSR 163
Cdd:cd03337 98 GEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFVSRWSDLMCNLALDAVKT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 164 LVTPTS---SNVDL-RDIRVVKKVGGTIEDTELVEGVVLNQNVIvsaggptrmekakiaiiqfqlsAPKpdmdntvvind 239
Cdd:cd03337 178 VAVEENgrkKEIDIkRYAKVEKIPGGEIEDSRVLDGVMLNKDVT----------------------HPK----------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 240 yrqMDKVIKEGRQYILnlckkikkaNCNVLLIqkSILRDAVDDVSLNFLKRLNILVVKDVERDEIEFLSKSLDCKPVADI 319
Cdd:cd03337 225 ---MRRRIENPRIVLL---------DCPLEYL--VITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARACGATIVNRP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 320 DAFTEDKLGYADLMEETNDNGVK-VVRITGVKNrGRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIGGGGAP 398
Cdd:cd03337 291 EELTESDVGTGAGLFEVKKIGDEyFTFITECKD-PKACTILLRGASKDVLNEVERNLQDAMAVARNIILNPKLVPGGGAT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 399 EIHVSRLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHALGDGNA-GINVRRGVISNILEEE 477
Cdd:cd03337 370 EMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTwGIDGETGDIVDMKELG 449
|
490 500
....*....|....*....|....*....
gi 170088430 478 VVQPLLVTTSAIELSTETVCLLLKIDDYV 506
Cdd:cd03337 450 IWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
2-506 |
3.87e-104 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239451 Cd Length: 527 Bit Score: 321.54 E-value: 3.87e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 2 ELRLSNMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVV 81
Cdd:cd03335 8 DVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 82 LAGSFLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTD-ISIPVDLNDRASLLRAASTSLNSKIVSQYSSTLAPIAVSA 160
Cdd:cd03335 88 IAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDNLGKESLINVAKTSMSSKIIGADSDFFANMVVDA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 161 VSRLVTPTSSNVD---LRDIRVVKKVGGTIEDTELVEGVVLNQnVIVSAGGPTRMEKAKIAIIQFQLSAPKPDMDNTVVI 237
Cdd:cd03335 168 ILAVKTTNEKGKTkypIKAVNILKAHGKSAKESYLVNGYALNC-TRASQGMPTRVKNAKIACLDFNLQKTKMKLGVQVVV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 238 NDYRQMDKVIKEGRQYILNLCKKIKKANCNVLLIQKSIlrdavDDVSLNFLKRLNILVVKDVERDEIEFLSKSLD---CK 314
Cdd:cd03335 247 TDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGI-----DDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGatlVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 315 PVADID---AFTEDKLGYADLMEETNDNGVKVVRITGVKNRgRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRAL 391
Cdd:cd03335 322 TLANLEgeeTFDPSYLGEAEEVVQERIGDDELILIKGTKKR-SSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 392 IGGGGAPEIHVSRLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHALGDGNA--------GI 463
Cdd:cd03335 401 VPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKPdkkhlkwyGL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 170088430 464 NVRRGVISNILEEEVVQPLLVTTSAIELSTETVCLLLKIDDYV 506
Cdd:cd03335 481 DLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLI 523
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
2-504 |
1.88e-103 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 318.95 E-value: 1.88e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 2 ELRLSNMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHP----AAKMLVDLSAAQDIEAGDGTT 77
Cdd:COG0459 10 DARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 78 SVVVLAGSFLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVDlnDRASLLRAASTSLNSKivsqysSTLAPIA 157
Cdd:COG0459 90 TATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVD--DKEELAQVATISANGD------EEIGELI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 158 VSAVSRLVtptssnvdlRDIRV-VKKVGGTIEDTELVEGVVLNQNVI------VSAGGPTRMEKAKIAIIQFQLSapkpd 230
Cdd:COG0459 162 AEAMEKVG---------KDGVItVEEGKGLETELEVVEGMQFDKGYLspyfvtDPEKMPAELENAYILLTDKKIS----- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 231 mdntvVINDYRQM-DKVIKEGRqyilnlckkikkancNVLLIQKSIlrdavDDVSLNFL------KRLNILVVK-----D 298
Cdd:COG0459 228 -----SIQDLLPLlEKVAQSGK---------------PLLIIAEDI-----DGEALATLvvngirGVLRVVAVKapgfgD 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 299 VERDEIEFLSKSLDCKPVAD-----IDAFTEDKLGYADLMEETNDNgvkVVRITGVKNRgRTVSILAMGSNHLVVDECER 373
Cdd:COG0459 283 RRKAMLEDIAILTGGRVISEdlglkLEDVTLDDLGRAKRVEVDKDN---TTIVEGAGNP-KAIVILVGAATEVEVKERKR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 374 SLHDALCVVRCLVKKRaLIGGGGAPEIHVSRLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRnr 453
Cdd:COG0459 359 RVEDALHATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVR-- 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 170088430 454 hALGDGNAGINVRRGVISNILEEEVVQPLLVTTSAIELSTETVCLLLKIDD 504
Cdd:COG0459 436 -AAKDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEA 485
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
4-506 |
1.33e-102 |
|
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274081 [Multi-domain] Cd Length: 536 Bit Score: 317.82 E-value: 1.33e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 4 RLSNMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVVLA 83
Cdd:TIGR02340 14 RTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVIIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 84 GSFLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTD-ISIPVDLNDRASLLRAASTSLNSKIVSQYSSTLAPIAVSAVS 162
Cdd:TIGR02340 94 AELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDELGREALINVAKTSMSSKIIGLDSDFFSNIVVDAVL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 163 RLVTPTSSNVD---LRDIRVVKKVGGTIEDTELVEGVVLNQNViVSAGGPTRMEKAKIAIIQFQLSAPKPDMDNTVVIND 239
Cdd:TIGR02340 174 AVKTTNENGETkypIKAINILKAHGKSARESMLVKGYALNCTV-ASQQMPKRIKNAKIACLDFNLQKAKMALGVQIVVDD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 240 YRQMDKVIKEGRQYILNLCKKIKKANCNVLLIQKSIlrdavDDVSLNFLKRLNILVVKDVERDEIEFLSKSLDCKPV--- 316
Cdd:TIGR02340 253 PEKLEQIRQREADITKERIKKILDAGANVVLTTGGI-----DDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVstl 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 317 ADI---DAFTEDKLGYADLMEETNDNGVKVVRITGVKNRgRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIG 393
Cdd:TIGR02340 328 ADLegeETFEASYLGFADEVVQERIADDECILIKGTKKR-KSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVP 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 394 GGGAPEIHVSRLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHAL--------GDGNAGINV 465
Cdd:TIGR02340 407 GGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAaqlkpekkHLKWYGLDL 486
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 170088430 466 RRGVISNILEEEVVQPLLVTTSAIELSTETVCLLLKIDDYV 506
Cdd:TIGR02340 487 VNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLI 527
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
5-509 |
1.03e-101 |
|
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: 315.50 E-value: 1.03e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 5 LSNMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVVLAG 84
Cdd:TIGR02346 21 IKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 85 SFLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISI--PVDLNDRASLLRAASTSLNSKIVSQYSsTLAPIAVSAVS 162
Cdd:TIGR02346 101 ELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVweVKDLRDKDELIKALKASISSKQYGNED-FLAQLVAQACS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 163 RLVTPTSSNVDLRDIRVVKKVGGTIEDTELVEGVVLNQNvivSAGGPTRMEKAKIAIIQFQLSAPKPDMDNTVVINDYRQ 242
Cdd:TIGR02346 180 TVLPKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNRE---AEGSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNAEE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 243 MDKVIKEGRQYILNLCKKIKKANCNVLliqksILRDAVDDVSLNFLKRLNILVVKDVERDEIEFLSKSLDCKPVADIDAF 322
Cdd:TIGR02346 257 LLNYSKGEENQIEAMIKAIADSGVNVI-----VTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 323 TEDKLGYADLMEETNDNGVKVVRITGVKNRGRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIGGGGAPEIHV 402
Cdd:TIGR02346 332 TPEEIGYVDSVYVSEIGGDKVTVFKQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIEL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 403 SRLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHALGDGNAGINVRRGVIS--NILEEEVVQ 480
Cdd:TIGR02346 412 ASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAESDGvkDASEAGIYD 491
|
490 500
....*....|....*....|....*....
gi 170088430 481 PLLVTTSAIELSTETVCLLLKIDDYVQAR 509
Cdd:TIGR02346 492 MLATKKWAIKLATEAAVTVLRVDQIIMAK 520
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
5-508 |
1.81e-100 |
|
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: 312.08 E-value: 1.81e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 5 LSNMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVVLAG 84
Cdd:TIGR02345 21 ISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 85 SFLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVDLND---RASLLRAASTSLNSKIVSQYSSTLAPIAVSAV 161
Cdd:TIGR02345 101 ELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqRELLEKCAATALSSKLISHNKEFFSKMIVDAV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 162 SRLVTptsSNVDLRDIRVVKKVGGTIEDTELVEGVVLnQNVIVSAG---GPTRMEKAKIAIIQFQLSApKPDMDNTVV-I 237
Cdd:TIGR02345 181 LSLDR---DDLDLKLIGIKKVQGGALEDSQLVNGVAF-KKTFSYAGfeqQPKKFANPKILLLNVELEL-KAEKDNAEIrV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 238 NDYRQMDKVIKEGRQYILNLCKKIKKANCNVLLIQKSIlrdavDDVSLNFLKRLNILVVKDVERDEIEFLSKSLDCKPVA 317
Cdd:TIGR02345 256 EDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPI-----GDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 318 DIDAFTEDKLGYADLMEETNDNGVKVVRITGVKNrGRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIGGGGA 397
Cdd:TIGR02345 331 TTSDLEADVLGTCALFEERQIGSERYNYFTGCPH-AKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 398 PEIHVSRLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHALGDGNAGINVRRGVISNILEEE 477
Cdd:TIGR02345 410 IEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFEAF 489
|
490 500 510
....*....|....*....|....*....|.
gi 170088430 478 VVQPLLVTTSAIELSTETVCLLLKIDDYVQA 508
Cdd:TIGR02345 490 VWEPALVKINALKAAFEAACTILSVDETITN 520
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
2-509 |
9.95e-100 |
|
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: 308.38 E-value: 9.95e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 2 ELRLSNMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVV 81
Cdd:cd03341 8 EAVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 82 LAGSFLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIP--VDLNDRASLLRAASTSLNSKIVSqYSSTLAPIAVS 159
Cdd:cd03341 88 LAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYkiEDLRNKEEVSKALKTAIASKQYG-NEDFLSPLVAE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 160 AVSRLVTPTSSNVDLRDIRVVKKVGGTIEDTELVEGVVLNQNvivSAGGPTRMEKAKIAIiqfqLSAPKpDMDNTVVInd 239
Cdd:cd03341 167 ACISVLPENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKRE---PEGSVKRVKKAKVAV----FSCPF-DIGVNVIV-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 240 yrqmdkvikegrqyilnlckkikkanCNvlliqksilrDAVDDVSLNFLKRLNILVVKDVERDEIEFLSKSLDCKPVADI 319
Cdd:cd03341 237 --------------------------AG----------GSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 320 DAFTEDKLGYADLMEETNDNGVKVVRITGVKNRGRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIGGGGAPE 399
Cdd:cd03341 281 GAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 400 IHVSRLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHALGDGNAGINVRRGVIS--NILEEE 477
Cdd:cd03341 361 IELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDEGtkDAKEAG 440
|
490 500 510
....*....|....*....|....*....|..
gi 170088430 478 VVQPLLVTTSAIELSTETVCLLLKIDDYVQAR 509
Cdd:cd03341 441 IFDHLATKKWAIKLATEAAVTVLRVDQIIMAK 472
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
4-506 |
9.78e-98 |
|
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: 305.12 E-value: 9.78e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 4 RLSNMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVVLA 83
Cdd:TIGR02344 18 QLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 84 GSFLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVDLNDRASLLRAASTSLNSKIVSQYSSTLAPIAVSAVsR 163
Cdd:TIGR02344 98 GEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRWSDLMCDLALDAV-R 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 164 LVTPTSS---NVDL-RDIRVVKKVGGTIEDTELVEGVVLNQNViVSAGGPTRMEKAKIAIIQFQLSAPKPDMDNTVVIND 239
Cdd:TIGR02344 177 TVQRDENgrkEIDIkRYAKVEKIPGGDIEDSCVLKGVMINKDV-THPKMRRYIENPRIVLLDCPLEYKKGESQTNIEITK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 240 YRQMDKVIKEGRQYILNLCKKIKKANCNVLLIQKsilrdAVDDVSLNFLKRLNILVVKDVERDEIEFLSKSLDCKPVADI 319
Cdd:TIGR02344 256 EEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEK-----GVSDLAQHYLLKANITAIRRVRKTDNNRIARACGATIVNRP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 320 DAFTEDKLGY-ADLMEETNDNGVKVVRITGVKNRgRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIGGGGAP 398
Cdd:TIGR02344 331 EELRESDVGTgCGLFEVKKIGDEYFTFITECKDP-KACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKLVPGGGAT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 399 EIHVSRLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHALGDG-NAGINVRRGVISNILEEE 477
Cdd:TIGR02344 410 EMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNcTWGIDGETGKIVDMKEKG 489
|
490 500
....*....|....*....|....*....
gi 170088430 478 VVQPLLVTTSAIELSTETVCLLLKIDDYV 506
Cdd:TIGR02344 490 IWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
4-509 |
1.27e-87 |
|
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: 278.67 E-value: 1.27e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 4 RLSNMVAAKAISDAVRTSLGPRGMDKMIQT--SKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVV 81
Cdd:TIGR02341 16 RLSSFVGAIAIGDLVKSTLGPKGMDKILQSssSDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEVGDGTTSVTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 82 LAGSFLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVDLND---RASLLRAASTSLNSKIVSQYSSTLAPIAV 158
Cdd:TIGR02341 96 LAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEvkfRQDLMNIARTTLSSKILSQHKDHFAQLAV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 159 SAVSRLvtPTSSNVDlrDIRVVKKVGGTIEDTELVEGVVLNQNVIVSAggPTRMEKAKIAIIQFQLSAPKPDMDNTVV-I 237
Cdd:TIGR02341 176 DAVLRL--KGSGNLE--AIQIIKKLGGSLADSYLDEGFLLDKKIGVNQ--PKRIENAKILIANTGMDTDKVKIFGSRVrV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 238 NDYRQMDKVIKEGRQYILNLCKKIKKANCNVLliqksILRDAVDDVSLNFLKRLNILVVKDVERDEIEFLSKSLDCKPVA 317
Cdd:TIGR02341 250 DSTAKVAELEHAEKEKMKEKVEKILKHGINCF-----INRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIVS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 318 DIDAFTEDKLGYADLMEETNDNGVKVVRITGVKnRGRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIGGGGA 397
Cdd:TIGR02341 325 TFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVK-LGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGGGC 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 398 PEIHVSRLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHALGDGNAGINVRRGVISNILEEE 477
Cdd:TIGR02341 404 SEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGTIADMRQLG 483
|
490 500 510
....*....|....*....|....*....|..
gi 170088430 478 VVQPLLVTTSAIELSTETVCLLLKIDDYVQAR 509
Cdd:TIGR02341 484 ITESYKVKRAVVSSAAEAAEVILRVDNIIKAA 515
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
7-508 |
5.01e-71 |
|
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: 234.07 E-value: 5.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 7 NMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVVLAGSF 86
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 87 LGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVD-LNDRASLLRAASTSLNSKIVSQYSSTLAPIAVSAVsRLV 165
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEiDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAV-LAI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 166 TPTSSNVDLRDIRVVKKVGGTIEDTELVEGVVLNQnvivsaGG-----PTRMEKAKIAIIQFQLSAPKPDMdNT-----V 235
Cdd:cd03342 176 YKPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDH------GArhpdmPKRVENAYILTCNVSLEYEKTEV-NSgffysV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 236 VINdyrqmdkvikegrqyilnlckkikkancnvlliQKSIlrdavDDVSLNFLKRLNILVVKDVERDEIEFLSKSLDCKP 315
Cdd:cd03342 249 VIN---------------------------------QKGI-----DPPSLDMLAKEGILALRRAKRRNMERLTLACGGVA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 316 VADIDAFTEDKLGYADLMEETNDNGVKVVRITGVKNrGRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIGGG 395
Cdd:cd03342 291 MNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGVKN-PKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 396 GAPEIHVSRLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHALGDGNAGINVRRGVISNILE 475
Cdd:cd03342 370 GAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPES 449
|
490 500 510
....*....|....*....|....*....|...
gi 170088430 476 EEVVQPLLVTTSAIELSTETVCLLLKIDDYVQA 508
Cdd:cd03342 450 EGIWDNYSVKRQILHSATVIASQLLLVDEIIRA 482
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
7-508 |
9.36e-67 |
|
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: 224.23 E-value: 9.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 7 NMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDLSAAQDIEAGDGTTSVVVLAGSF 86
Cdd:TIGR02347 21 NINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 87 LGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPV-DLNDRASLLRAASTSLNSKIVSQYSSTLAPIAVSAVSRLV 165
Cdd:TIGR02347 101 LKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKeDEVDREFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 166 TPTSSnVDLRDIRVVKKVGGTIEDTELVEGVVLNQNViVSAGGPTRMEKAKIAIIQFQLSAPKPDMDNTVVINDYRQMDK 245
Cdd:TIGR02347 181 KDGED-IDLFMVEIMEMKHKSATDTTLIRGLVLDHGA-RHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQREK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 246 VIKEGRQYILNLCKKI---------KKANCNVLLI-QKSIlrdavDDVSLNFLKRLNILVVKDVERDEIEFLSKSLDCKP 315
Cdd:TIGR02347 259 LVKAERKFVDDRVKKIielkkkvcgKSPDKGFVVInQKGI-----DPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 316 VADIDAFTEDKLGYADLMEETNDNGVKVVRITGVKNRgRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIGGG 395
Cdd:TIGR02347 334 LNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNP-KSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 396 GAPEIHVSRLLSQYAQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNRHALGDGNAGINVRRGVISNILE 475
Cdd:TIGR02347 413 GAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGVDLNTGEPIDPEI 492
|
490 500 510
....*....|....*....|....*....|...
gi 170088430 476 EEVVQPLLVTTSAIELSTETVCLLLKIDDYVQA 508
Cdd:TIGR02347 493 KGIWDNYRVKKQLIQSATVIASQLLLVDEVMRA 525
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
130-387 |
1.21e-56 |
|
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: 187.67 E-value: 1.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 130 RASLLRAASTSLNSKIvSQYSSTLAPIAVSAVSRlVTPTSSNVDLRDIRVVKKVGGTIEDTELVEGVVLNQNVIvSAGGP 209
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLK-VGPDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYA-SPYMP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 210 TRMEKAKIAIIQFQLSapkpdmdntvvindyrqmdkvikegrqyilnlckkikkancNVLLIQKSIlrdavDDVSLNFLK 289
Cdd:cd03333 78 KRLENAKILLLDCPLE-----------------------------------------YVVIAEKGI-----DDLALHYLA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 290 RLNILVVKDVERDEIEFLSKSLDCKPVADIDAFTEDKLGYADLMEETNDNGVKVVRITGVKNrGRTVSILAMGSNHLVVD 369
Cdd:cd03333 112 KAGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKG-GKAATILLRGATEVELD 190
|
250
....*....|....*...
gi 170088430 370 ECERSLHDALCVVRCLVK 387
Cdd:cd03333 191 EVKRSLHDALCAVRAAVE 208
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
12-500 |
5.91e-21 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 96.13 E-value: 5.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 12 KAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSI----QALHPAAKMLVDLSAAQDIEAGDGTTSVVVLAGSFL 87
Cdd:PTZ00114 32 ERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIefsdRFENVGAQLIRQVASKTNDKAGDGTTTATILARAIF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 88 GAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVdlNDRASLLRAASTSLN-----SKIVSQysstlapiAVSAVS 162
Cdd:PTZ00114 112 REGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPV--KTKEDILNVATISANgdveiGSLIAD--------AMDKVG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 163 RlvtptSSNVDLRDirvvkkvGGTIEDT-ELVEGVVLNQNVIvsagGPTRMEKAKiaiiqfqlsAPKPDMDNTVVIndyr 241
Cdd:PTZ00114 182 K-----DGTITVED-------GKTLEDElEVVEGMSFDRGYI----SPYFVTNEK---------TQKVELENPLIL---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 242 QMDKVIkEGRQYILNLCKKIKKANCNVLLIQKSILRDAVDDVSLNFLK-RLNILVVK-----DVERDEIEFLSKSLDCKP 315
Cdd:PTZ00114 233 VTDKKI-SSIQSILPILEHAVKNKRPLLIIAEDVEGEALQTLIINKLRgGLKVCAVKapgfgDNRKDILQDIAVLTGATV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 316 V------ADIDAFTEDKLGYADLMEETNDN-------GVKVV---RITGVKNR---------------------GRTVSI 358
Cdd:PTZ00114 312 VsednvgLKLDDFDPSMLGSAKKVTVTKDEtviltggGDKAEikeRVELLRSQierttseydkeklkerlaklsGGVAVI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 359 LAMGSNHLVVDECERSLHDALCVVRCLVKKRALIGGGGApEIHVSRLLS--QYAQSLKGMEAYCFQAYADALEVIPTTLA 436
Cdd:PTZ00114 392 KVGGASEVEVNEKKDRIEDALNATRAAVEEGIVPGGGVA-LLRASKLLDklEEDNELTPDQRTGVKIVRNALRLPTKQIA 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170088430 437 ENAGLNPIAIVTELRNRhalGDGNAGINVRRGVISNILEEEVVQPLLVTTSAIELSTETVCLLL 500
Cdd:PTZ00114 471 ENAGVEGAVVVEKILEK---KDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLML 531
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
148-334 |
5.63e-16 |
|
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. Fab1p is important for vacuole size regulation, presumably by modulating PtdIns(3,5)P2 effector activity. In the human homolog p235/PIKfyve deletion of this domain leads to loss of catalytic activity. However no exact function this domain has been defined. In general, chaperonins are involved in productive folding of proteins.
Pssm-ID: 239450 [Multi-domain] Cd Length: 261 Bit Score: 77.65 E-value: 5.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 148 QYSSTLAPIAVSAVSrLVTPTSSNVDLRDIRV---VKKV-GGTIEDTELVEGVVLNQNViVSAGGPTRMEKAKIAIIQFQ 223
Cdd:cd03334 18 SWLDILLPLVWKAAS-NVKPDVRAGDDMDIRQyvkIKKIpGGSPSDSEVVDGVVFTKNV-AHKRMPSKIKNPRILLLQGP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 224 LSAPKPDmdntvviNDYRQMDKVIKEGRQYILNLCKKIKKANCNVLLIQKSILRDAVDdvslnFLKRLNILVVKDVERDE 303
Cdd:cd03334 96 LEYQRVE-------NKLLSLDPVILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQD-----LLLEAGITLVLNVKPSV 163
|
170 180 190
....*....|....*....|....*....|..
gi 170088430 304 IEFLSKSLDCKPVADIDAF-TEDKLGYADLME 334
Cdd:cd03334 164 LERISRCTGADIISSMDDLlTSPKLGTCESFR 195
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
2-500 |
1.67e-15 |
|
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). With the aid of cochaperonin GroES, GroEL encapsulates non-native substrate proteins inside the cavity of the GroEL-ES complex and promotes folding by using energy derived from ATP hydrolysis.
Pssm-ID: 239460 Cd Length: 520 Bit Score: 79.04 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 2 ELRLSNMVAAKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHP----AAKMLVDLSAAQDIEAGDGTT 77
Cdd:cd03344 8 EARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 78 SVVVLAGSFLGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVdlNDRASLLRAASTSLNS-----KIVSQysst 152
Cdd:cd03344 88 TATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPV--KTKEEIAQVATISANGdeeigELIAE---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 153 lapiAVSAVSRlvtptSSNVDLRDirvvkkvGGTIEDT-ELVEGVVLNQNVI----VSagGPTRM----EKAKIAIIQFQ 223
Cdd:cd03344 162 ----AMEKVGK-----DGVITVEE-------GKTLETElEVVEGMQFDRGYLspyfVT--DPEKMevelENPYILLTDKK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 224 LSAPKPdmdntvvindyrqmdkvikegrqyILNLCKKIKKANCNVLLIQKSILRDAVDDVSLNFLK-RLNILVVK----- 297
Cdd:cd03344 224 ISSIQE------------------------LLPILELVAKAGRPLLIIAEDVEGEALATLVVNKLRgGLKVCAVKapgfg 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 298 DVERDEIE---------FLSKSLDCKpvadIDAFTEDKLGYADLMEETNDN-------GVKVV---RITGVKNR------ 352
Cdd:cd03344 280 DRRKAMLEdiailtggtVISEELGLK----LEDVTLEDLGRAKKVVVTKDDttiiggaGDKAAikaRIAQIRKQieetts 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 353 ---------------GRTVSILAMGSNHLVVDECERSLHDALCVVRCLVKKRALIGGGGApEIHVSRLLSQyAQSLKGME 417
Cdd:cd03344 356 dydkeklqerlaklsGGVAVIKVGGATEVELKEKKDRVEDALNATRAAVEEGIVPGGGVA-LLRASPALDK-LKALNGDE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 418 AYCFQAYADALEVIPTTLAENAGLNPIAIVTELRNrhalGDGNAGINVRRGVISNILEEEVVQPLLVTTSAIELSTETVC 497
Cdd:cd03344 434 KLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLE----SPDGFGYDAATGEYVDMIEAGIIDPTKVVRSALQNAASVAS 509
|
...
gi 170088430 498 LLL 500
Cdd:cd03344 510 LLL 512
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
12-143 |
2.44e-13 |
|
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: 72.33 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 12 KAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHP----AAKMLVDLSAAQDIEAGDGTTSVVVLAGSFL 87
Cdd:TIGR02348 19 DKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVASKTNDVAGDGTTTATVLAQAIV 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 170088430 88 GAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVdlNDRASLLRAASTSLNS 143
Cdd:TIGR02348 99 KEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPV--KGKKEIAQVATISANN 152
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
11-500 |
1.40e-12 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 69.77 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 11 AKAISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHP----AAKMLVDLSAAQDIEAGDGTTSVVVLAGSF 86
Cdd:PRK12851 20 VNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 87 LGAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVDlnDRASLLRAASTSLNSKivsqysstlapiavSAVSRLVT 166
Cdd:PRK12851 100 VREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVT--TNAEIAQVATISANGD--------------AEIGRLVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 167 PTSSNVDLRDIRVVKKVGGTIEDTELVEGVVLNQNVIVS--AGGPTRMEKA-----------KIAIIQFQL-------SA 226
Cdd:PRK12851 164 EAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPyfVTDADKMEAEledpyilihekKISNLQDLLpvleavvQS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 227 PKP------DMDN----TVVINDYRQMDKVIK-------EGRQYILNlckkikkaNCNVLLIQKSILRDA---VDDVSLN 286
Cdd:PRK12851 244 GKPlliiaeDVEGealaTLVVNKLRGGLKVAAvkapgfgDRRKAMLE--------DIAILTGGTVISEDLgikLENVTLE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 287 FLKRLNILVvkdVERDEIEFLSKSLDckpVADIDAFTEDKlgYADLMEETNDNGVKVVRITGVKNRGRTVSILAMGSNHL 366
Cdd:PRK12851 316 QLGRAKKVV---VEKENTTIIDGAGS---KTEIEGRVAQI--RAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 367 VVDECERSLHDALCVVRCLVKKRALIGGGGAPEIHVSRLLSQyaQSLKGMEAYCFQAYADALEVIPTTLAENAGLNPIAI 446
Cdd:PRK12851 388 EVKEKKDRVDDALHATRAAVEEGIVPGGGVALLRAVKALDKL--ETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVV 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 170088430 447 VTELRNrhalGDGNAGINVRRGVISNILEEEVVQPLLVTTSAIELSTETVCLLL 500
Cdd:PRK12851 466 VGKLRE----KPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLL 515
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
13-143 |
2.28e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 65.98 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 13 AISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHP----AAKMLVDLSAAQDIEAGDGTTSVVVLAGSFLG 88
Cdd:PRK12849 21 KLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQALVQ 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 170088430 89 AAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVDlnDRASLLRAASTSLNS 143
Cdd:PRK12849 101 EGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVS--GSEEIAQVATISANG 153
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
16-490 |
6.69e-11 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 64.36 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 16 DAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDL-----SAAQDIeAGDGTTSVVVLAGSFLGAA 90
Cdd:CHL00093 24 EAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALirqaaSKTNDV-AGDGTTTATVLAYAIVKQG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 91 EKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVDlnDRASLLRAASTSL--NSKIVSQYSSTLAPIAVSAVSRLVTPT 168
Cdd:CHL00093 103 MKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVE--DIQAITQVASISAgnDEEVGSMIADAIEKVGREGVISLEEGK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 169 SSNVDLrdirvvkkvggtiedtELVEGVVLNQNVIVS--AGGPTRMEkakiaiiqfqlsapkpdmdnTVVINDYRQM-DK 245
Cdd:CHL00093 181 STVTEL----------------EITEGMRFEKGFISPyfVTDTERME--------------------VVQENPYILLtDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 246 VIKEGRQYILNLCKKIKKANCNVLLIQKSILRDAVDDVSLNFLKrlNILVVKDVERDEIEFLSKSLdckpVADIDAFTED 325
Cdd:CHL00093 225 KITLVQQDLLPILEQVTKTKRPLLIIAEDVEKEALATLVLNKLR--GIVNVVAVRAPGFGDRRKAM----LEDIAILTGG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 326 KLGYAD----LMEETNDNGVKVVRITGVKNrgrTVSILAMGSNHLVVDECER---------------------------- 373
Cdd:CHL00093 299 QVITEDaglsLETIQLDLLGQARRIIVTKD---STTIIADGNEEQVKARCEQlrkqieiadssyekeklqerlaklsggv 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 374 ------------------SLHDALCVVRCLVKKrALIGGGGAPEIHVSRLLSQYAQS-LKGMEAYCFQAYADALEVIPTT 434
Cdd:CHL00093 376 avikvgaatetemkdkklRLEDAINATKAAVEE-GIVPGGGATLVHLSENLKTWAKNnLKEDELIGALIVARAILAPLKR 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 170088430 435 LAENAGLNPIAIVTELRNRhalgDGNAGINVRRGVISNILEEEVVQPLLVTTSAIE 490
Cdd:CHL00093 455 IAENAGKNGSVIIEKVQEQ----DFEIGYNAANNKFVNMYEAGIIDPAKVTRSALQ 506
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
13-143 |
1.67e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 63.22 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 13 AISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDL-----SAAQDIeAGDGTTSVVVLAGSFL 87
Cdd:PRK00013 21 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLvkevaSKTNDV-AGDGTTTATVLAQAIV 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 170088430 88 GAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVdlNDRASLLRAASTSLNS 143
Cdd:PRK00013 100 REGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPV--EDKEEIAQVATISANG 153
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
13-142 |
1.15e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 60.50 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 13 AISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHPAAKMLVDL-----SAAQDIeAGDGTTSVVVLAGSFL 87
Cdd:PRK12850 22 ILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMvkevaSKTNDL-AGDGTTTATVLAQAIV 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 170088430 88 GAAEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVdlNDRASLLRAASTSLN 142
Cdd:PRK12850 101 REGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKV--TSSKEIAQVATISAN 153
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
14-126 |
5.27e-08 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 55.32 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 14 ISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQALHP----AAKMLVDLSAAQDIEAGDGTTSVVVLAGSFLGA 89
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAE 157
|
90 100 110
....*....|....*....|....*....|....*..
gi 170088430 90 AEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVD 126
Cdd:PLN03167 158 GVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVE 194
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
14-125 |
5.46e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 55.24 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 14 ISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQAL----HPAAKMLVDLSAAQDIEAGDGTTSVVVLAGSFLGA 89
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110
....*....|....*....|....*....|....*.
gi 170088430 90 AEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPV 125
Cdd:PRK12852 103 GAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPV 138
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
14-145 |
5.68e-07 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 51.95 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170088430 14 ISDAVRTSLGPRGMDKMIQTSKGEVIVTNDGATILKSIQA----LHPAAKMLVDLSAAQDIEAGDGTTSVVVLAGSFLGA 89
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 170088430 90 AEKMLQKGIHPTIVAESFIKASAKAVEYLTDISIPVDLNDRASLLRAASTSLNSKI 145
Cdd:PRK14104 103 GAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEI 158
|
|
| |
