|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
25-538 |
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: 977.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 25 QDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGD 104
Cdd:cd03338 1 TDKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 105 GTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:cd03338 81 GTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 185 PMSVNAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANS--GITRVEKAKIGLIQFCLSAPKTDMDN 262
Cdd:cd03338 161 PIAVDAVLKVIDPATATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKagGPTRIEKAKIGLIQFCLSPPKTDMDN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 263 QIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNKMKIMVVKDVEREDIEFICKTIGT 342
Cdd:cd03338 241 NIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQKSILRDAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 343 KPVAHIDQFTADMLGSAELAEEVSLnGSGKLFKITGCTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALI 422
Cdd:cd03338 321 KPVASIDHFTEDKLGSADLVEEVSL-GDGKIVKITGVKNPGKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 423 AGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISN 502
Cdd:cd03338 400 PGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITN 479
|
490 500 510
....*....|....*....|....*....|....*.
gi 6753322 503 ILEEMVVQPLLVSVSALTLATETVRSILKIDDVVNT 538
Cdd:cd03338 480 ILEENVVQPLLVSTSAITLATETVRMILKIDDIVLA 515
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
24-539 |
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: 918.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 24 YQDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAG 103
Cdd:TIGR02342 1 FQDKDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 104 DGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLL 183
Cdd:TIGR02342 81 DGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 184 SPMSVNAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKV--ANSGITRVEKAKIGLIQFCLSAPKTDMD 261
Cdd:TIGR02342 161 APLAVDAVLKVIDPENAKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKAskSAGGPTRIEKAKIGLIQFQISPPKTDME 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 262 NQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNKMKIMVVKDVEREDIEFICKTIG 341
Cdd:TIGR02342 241 NQIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSILRDAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 342 TKPVAHIDQFTADMLGSAELAEEVSLNGsGKLFKITGCTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRAL 421
Cdd:TIGR02342 321 CKPIASIDHFTADKLGSAELVEEVDSDG-GKIIKITGIQNAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 422 IAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGIS 501
Cdd:TIGR02342 400 IAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGIT 479
|
490 500 510
....*....|....*....|....*....|....*...
gi 6753322 502 NILEEMVVQPLLVSVSALTLATETVRSILKIDDVVNTR 539
Cdd:TIGR02342 480 NMLEEHVLQPLLVTTSAITLASETVRSILKIDDIVFTR 517
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
26-536 |
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: 586.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 26 DRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDG 105
Cdd:cd00309 2 EREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 106 TTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLSP 185
Cdd:cd00309 82 TTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 186 MSVNAVMKVIDPATatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSG-ITRVEKAKIGLIQFCLSapktdmdnqi 264
Cdd:cd00309 162 LVVDAVLKVGKENG--DVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYmPKRLENAKILLLDCKLE---------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 265 vvsdyaqmdrvlreerayilnlvkqikktgcNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDVEREDIEFICKTIGTKP 344
Cdd:cd00309 230 -------------------------------YVVIAEKGI-----DDEALHYLAKLGIMAVRRVRKEDLERIAKATGATI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 345 VAHIDQFTADMLGSAELAEEVSLnGSGKLFKITGCTSpGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAG 424
Cdd:cd00309 274 VSRLEDLTPEDLGTAGLVEETKI-GDEKYTFIEGCKG-GKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 425 GGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNIL 504
Cdd:cd00309 352 GGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMK 431
|
490 500 510
....*....|....*....|....*....|..
gi 6753322 505 EEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:cd00309 432 EAGIIDPLKVKRQALKSATEAASLILTIDDII 463
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
44-539 |
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: 559.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 44 VADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSLLDSCTKL 123
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 124 LQKGIHPTIISESFQKALEKGLEILTDM-SRPVQLSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVidPATATS 202
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAI--PKNDGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 203 VDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSG-ITRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDRVLREERA 281
Cdd:pfam00118 159 FDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDmPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 282 YILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDVEREDIEFICKTIGTKPVAHIDQFTADMLGSAEL 361
Cdd:pfam00118 239 QILEIVEKIIDSGVNVVVCQKGI-----DDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 362 AEEVSLnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELALRLTEYSR 441
Cdd:pfam00118 314 VEEEKI-GDEKYTFIEGCKSP-KAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 442 TLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEMVVQPLLVSVSALTL 521
Cdd:pfam00118 392 SVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
|
490
....*....|....*...
gi 6753322 522 ATETVRSILKIDDVVNTR 539
Cdd:pfam00118 472 ATEAASTILRIDDIIKAK 489
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
36-536 |
0e+00 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 549.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:NF041082 21 NNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 116 LLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVI 195
Cdd:NF041082 101 LLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVKAVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 196 DPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDR 274
Cdd:NF041082 181 EKDGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMpKRVENAKIALLDAPLEVKKTEIDAKISITDPDQLQA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 275 VLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDVEREDIEFICKTIGTKPVAHIDQFTAD 354
Cdd:NF041082 261 FLDQEEKMLKEMVDKIADSGANVVFCQKGI-----DDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSIDDLSPE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 355 MLGSAELAEEVSLNGSGKLFkITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELAL 434
Cdd:NF041082 336 DLGYAGLVEERKVGGDKMIF-VEGCKNP-KAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEVELAL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 435 RLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEMVVQPLLV 514
Cdd:NF041082 414 RLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVVEPLRV 493
|
490 500
....*....|....*....|..
gi 6753322 515 SVSALTLATETVRSILKIDDVV 536
Cdd:NF041082 494 KTQAIKSATEAAVMILRIDDVI 515
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
20-536 |
0e+00 |
|
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: 537.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 20 GKSAYQDRDkpAQIrfSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQD 99
Cdd:cd03343 7 GTQRTSGRD--AQR--MNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 100 IEAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQY 179
Cdd:cd03343 83 EEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAEAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 180 SSLLSPMSVNAVMKVIDPAT-ATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPK 257
Cdd:cd03343 163 KDKLADLVVDAVLQVAEKRDgKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMpKRVENAKIALLDAPLEVKK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 258 TDMDNQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDVEREDIEFIC 337
Cdd:cd03343 243 TEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGI-----DDLAQHYLAKAGILAVRRVKKSDMEKLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 338 KTIGTKPVAHIDQFTADMLGSAELAEEVSLNGSGKLFkITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVK 417
Cdd:cd03343 318 RATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVF-VEGCKNP-KAVTILLRGGTEHVVDELERALEDALRVVADALE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 418 KRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRK 497
Cdd:cd03343 396 DGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYT 475
|
490 500 510
....*....|....*....|....*....|....*....
gi 6753322 498 GGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:cd03343 476 GEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVI 514
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
20-536 |
0e+00 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 519.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 20 GKSAYQDRDkpAQirFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQD 99
Cdd:NF041083 9 GTQRTKGRD--AQ--RNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 100 IEAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQY 179
Cdd:NF041083 85 DEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKGVEEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 180 SSLLSPMSVNAVMKVIDPATAT-SVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPK 257
Cdd:NF041083 165 RDYLAEIAVKAVKQVAEKRDGKyYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMpKRVENAKIALLDAPLEVKK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 258 TDMDNQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDVEREDIEFIC 337
Cdd:NF041083 245 TEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGI-----DDLAQHYLAKAGILAVRRVKKSDMEKLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 338 KTIGTKPVAHIDQFTADMLGSAELAEEVSLnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVK 417
Cdd:NF041083 320 KATGARIVTNIDDLTPEDLGYAELVEERKV-GDDKMVFVEGCKNP-KAVTILIRGGTEHVVDEAERALEDALSVVADAVE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 418 KRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRK 497
Cdd:NF041083 398 DGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFT 477
|
490 500 510
....*....|....*....|....*....|....*....
gi 6753322 498 GGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:NF041083 478 GEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVI 516
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
36-536 |
9.75e-177 |
|
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: 508.46 E-value: 9.75e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:TIGR02339 20 NNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 116 LLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYS-SLLSPMSVNAVMKV 194
Cdd:TIGR02339 100 LLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSKASAEVAkDKLADLVVEAVKQV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 195 IDPATATS--VDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQ 271
Cdd:TIGR02339 180 AELRGDGKyyVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMpKRVENAKIALLDAPLEVEKTEIDAKIRITDPDQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 272 MDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDVEREDIEFICKTIGTKPVAHIDQF 351
Cdd:TIGR02339 260 IKKFLDQEEAMLKEMVDKIASAGANVVICQKGI-----DDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVSSIDEI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 352 TADMLGSAELAEEVSLnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIE 431
Cdd:TIGR02339 335 TESDLGYAELVEERKV-GEDKMVFVEGCKNP-KAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVAGGGAVEIE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 432 LALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEMVVQP 511
Cdd:TIGR02339 413 LALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTGEIEDMLELGVIEP 492
|
490 500
....*....|....*....|....*
gi 6753322 512 LLVSVSALTLATETVRSILKIDDVV 536
Cdd:TIGR02339 493 LRVKEQAIKSATEAATMILRIDDVI 517
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
36-536 |
6.26e-148 |
|
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: 435.19 E-value: 6.26e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:cd03339 27 SHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 116 LLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSR--PVQLSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMK 193
Cdd:cd03339 107 LLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADkiEFSPDNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAVLS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 194 VIDpATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITR-VEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQM 272
Cdd:cd03339 187 VAD-LERKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKeVKDAKIAILTCPFEPPKPKTKHKLDITSVEDY 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 273 DRVLREERAYILNLVKQIKKTGCNVLLIQKsilrdALSDLALHFLNKMKIMVVKDVEREDIEFICKTIGTKPVAHIDQFT 352
Cdd:cd03339 266 KKLQEYEQKYFREMVEQVKDAGANLVICQW-----GFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFEDLS 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 353 ADMLGSAELAEEVSLNGS-GKLFKITGCtSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIE 431
Cdd:cd03339 341 PEKLGKAGLVREISFGTTkDKMLVIEGC-PNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGGGAAEIS 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 432 LALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRH-AQGEKTTGINVRKGGISNILEEMVVQ 510
Cdd:cd03339 420 CSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPHLGIDCLGRGTNDMKEQKVFE 499
|
490 500
....*....|....*....|....*.
gi 6753322 511 PLLVSVSALTLATETVRSILKIDDVV 536
Cdd:cd03339 500 TLISKKQQILLATQVVKMILKIDDVI 525
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
27-536 |
3.17e-129 |
|
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: 387.24 E-value: 3.17e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 27 RDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGT 106
Cdd:TIGR02343 22 RLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 107 TSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPV--QLSDRETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:TIGR02343 102 TGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEIsaDNNNREPLIQAAKTSLGSKIVSKCHRRFA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 185 PMSVNAVMKVIDpATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITR-VEKAKIGLIQFCLSAPKTDMDNQ 263
Cdd:TIGR02343 182 EIAVDAVLNVAD-MERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKeVEDAKIAILTCPFEPPKPKTKHK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 264 IVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKsilrdALSDLALHFLNKMKIMVVKDVEREDIEFICKTIGTK 343
Cdd:TIGR02343 261 LDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQW-----GFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 344 PVAHIDQFTADMLGSAELAEEVSLNGSG-KLFKITGCTSpGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALI 422
Cdd:TIGR02343 336 IVPRFQELSKDKLGKAGLVREISFGTTKdRMLVIEQCKN-SKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 423 AGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRH-AQGEKTTGINVRKGGIS 501
Cdd:TIGR02343 415 YGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQlKEKNPNLGVDCLGYGTN 494
|
490 500 510
....*....|....*....|....*....|....*
gi 6753322 502 NILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:TIGR02343 495 DMKEQFVFETLIGKKQQILLATQLVRMILKIDDVI 529
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
36-536 |
1.60e-128 |
|
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: 385.10 E-value: 1.60e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:cd03340 20 SNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 116 LLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSD----RETLLNSATTSLNSKVVSQYSSLLSPMSVNAV 191
Cdd:cd03340 100 FLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDkeeqRELLEKCAATALNSKLIASEKEFFAKMVVDAV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 192 MKVIDpatatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI----TRVEKAKIGLIQFCLSApKTDMDN-QIVV 266
Cdd:cd03340 180 LSLDD-----DLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAGFeqqpKKFKNPKILLLNVELEL-KAEKDNaEVRV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 267 SDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDVEREDIEFICKTIGTKPVA 346
Cdd:cd03340 254 EDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPI-----GDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 347 HIDQFTADMLGSAELAEEVSLngSGKLFKI-TGCTSpGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGG 425
Cdd:cd03340 329 TVSNITDDVLGTCGLFEERQV--GGERYNIfTGCPK-AKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 426 GAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKT-TGINVRKGGISNIL 504
Cdd:cd03340 406 GAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKwYGVDINNEGIADNF 485
|
490 500 510
....*....|....*....|....*....|..
gi 6753322 505 EEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:cd03340 486 EAFVWEPSLVKINALTAATEAACLILSVDETI 517
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
26-536 |
1.93e-123 |
|
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: 372.39 E-value: 1.93e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 26 DRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDG 105
Cdd:cd03335 2 ERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 106 TTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTD-MSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDNLGKESLINVAKTSMSSKIIGADSDFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 185 PMSVNAVM--KVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMD 261
Cdd:cd03335 162 NMVVDAILavKTTNEKGKTKYPIKAVNILKAHGKSAKESYLVNGYALNCTRASQGMpTRVKNAKIACLDFNLQKTKMKLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 262 NQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDVEREDIEFICKTIG 341
Cdd:cd03335 242 VQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGI-----DDMCLKYFVEAGAMAVRRVKKEDLRRIAKATG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 342 TKPVAHI------DQFTADMLGSAELAEEVSLnGSGKLFKITGCtSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCL 415
Cdd:cd03335 317 ATLVSTLanlegeETFDPSYLGEAEEVVQERI-GDDELILIKGT-KKRSSASIILRGANDFMLDEMERSLHDALCVVKRT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 416 VKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHA--------QG 487
Cdd:cd03335 395 LESNSVVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAaaqvkpdkKH 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 6753322 488 EKTTGINVRKGGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:cd03335 475 LKWYGLDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLI 523
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
27-536 |
3.17e-122 |
|
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: 367.78 E-value: 3.17e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 27 RDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGT 106
Cdd:cd03337 11 RESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 107 TSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLSPM 186
Cdd:cd03337 91 TSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFVSRWSDLMCNL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 187 SVNAVMKVI--DPATATSVDL-RDIKIVKKLGGTIDDCELVEGLVLtqkvansgitrvekakigliqfclsapktdmdNQ 263
Cdd:cd03337 171 ALDAVKTVAveENGRKKEIDIkRYAKVEKIPGGEIEDSRVLDGVML--------------------------------NK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 264 IVVsdYAQMDRVLREERAYILNlvkqikktgCNVLLIqkSILRDALSDLALHFLNKMKIMVVKDVEREDIEFICKTIGTK 343
Cdd:cd03337 219 DVT--HPKMRRRIENPRIVLLD---------CPLEYL--VITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARACGAT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 344 PVAHIDQFTADMLGSAELAEEVSLNGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIA 423
Cdd:cd03337 286 IVNRPEELTESDVGTGAGLFEVKKIGDEYFTFITECKDP-KACTILLRGASKDVLNEVERNLQDAMAVARNIILNPKLVP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 424 GGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEK-TTGINVRKGGISN 502
Cdd:cd03337 365 GGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENsTWGIDGETGDIVD 444
|
490 500 510
....*....|....*....|....*....|....
gi 6753322 503 ILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:cd03337 445 MKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
26-536 |
8.32e-120 |
|
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: 363.27 E-value: 8.32e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 26 DRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDG 105
Cdd:TIGR02340 6 ERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 106 TTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTD-MSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDELGREALINVAKTSMSSKIIGLDSDFFS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 185 PMSVNAVM--KVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMD 261
Cdd:TIGR02340 166 NIVVDAVLavKTTNENGETKYPIKAINILKAHGKSARESMLVKGYALNCTVASQQMpKRIKNAKIACLDFNLQKAKMALG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 262 NQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDVEREDIEFICKTIG 341
Cdd:TIGR02340 246 VQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGI-----DDMCLKYFVEAGAMGVRRCKKEDLKRIAKATG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 342 TKPVAHI------DQFTADMLGSAELAEEVSLnGSGKLFKITGcTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCL 415
Cdd:TIGR02340 321 ATLVSTLadlegeETFEASYLGFADEVVQERI-ADDECILIKG-TKKRKSASIILRGANDFMLDEMERSLHDALCVVKRT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 416 VKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHA--------QG 487
Cdd:TIGR02340 399 LESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAaaqlkpekKH 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 6753322 488 EKTTGINVRKGGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:TIGR02340 479 LKWYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLI 527
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
36-536 |
6.53e-119 |
|
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: 360.61 E-value: 6.53e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:TIGR02345 22 SNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 116 LLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSD---RETLLNSATTSLNSKVVSQYSSLLSPMSVNAVM 192
Cdd:TIGR02345 102 LLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqRELLEKCAATALSSKLISHNKEFFSKMIVDAVL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 193 KVIDPAtatsVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI----TRVEKAKIGLIQFCLSApKTDMDN-QIVVS 267
Cdd:TIGR02345 182 SLDRDD----LDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAGFeqqpKKFANPKILLLNVELEL-KAEKDNaEIRVE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 268 DYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDVEREDIEFICKTIGTKPVAH 347
Cdd:TIGR02345 257 DVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPI-----GDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQST 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 348 IDQFTADMLGSAELAEEVSLnGSGKLFKITGCTSpGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGA 427
Cdd:TIGR02345 332 TSDLEADVLGTCALFEERQI-GSERYNYFTGCPH-AKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 428 PEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEM 507
Cdd:TIGR02345 410 IEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFEAF 489
|
490 500
....*....|....*....|....*....
gi 6753322 508 VVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:TIGR02345 490 VWEPALVKINALKAAFEAACTILSVDETI 518
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
34-536 |
1.20e-114 |
|
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: 349.32 E-value: 1.20e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 34 RFSNISAAKAVADAIRTSLGPKGMDKMIQDG--KGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVI 111
Cdd:cd03336 15 RLSSFVGAIAIGDLVKTTLGPKGMDKILQSVgrSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDGTTSVTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 112 IAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSD---RETLLNSATTSLNSKVVSQYSSLLSPMSV 188
Cdd:cd03336 95 LAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEeafREDLLNIARTTLSSKILTQDKEHFAELAV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 189 NAVMKVIDpatatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITRVEKAKIgLIQfclsapKTDMDN------ 262
Cdd:cd03336 175 DAVLRLKG-----SGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQPKRIENAKI-LIA------NTPMDTdkikif 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 263 --QIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLliqksILRDALSDLALHFLNKMKIMVVKDVEREDIEFICKTI 340
Cdd:cd03336 243 gaKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCF-----INRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 341 GTKPVAHIDQFTADMLGSAELAEEVSLnGSGKLFKITGCTSpGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRA 420
Cdd:cd03336 318 GGEIASTFDHPELVKLGTCKLIEEIMI-GEDKLIRFSGVAA-GEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 421 LIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGI 500
Cdd:cd03336 396 VVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTV 475
|
490 500 510
....*....|....*....|....*....|....*.
gi 6753322 501 SNILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:cd03336 476 GDMKELGITESFKVKRQVLLSASEAAEMILRVDDII 511
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
35-536 |
2.46e-114 |
|
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: 346.90 E-value: 2.46e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 35 FSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAG 114
Cdd:cd03341 11 LRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 115 SLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMS--RPVQLSDRETLLNSATTSLNSKVVSqYSSLLSPMSVNAVM 192
Cdd:cd03341 91 ELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVvyKIEDLRNKEEVSKALKTAIASKQYG-NEDFLSPLVAEACI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 193 KVIdPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSgITRVEKAKIGLiqfclsapktdmdnqivvsdyaqm 272
Cdd:cd03341 170 SVL-PENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKREPEGS-VKRVKKAKVAV------------------------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 273 drvlreeraYILNLvkqikKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDVEREDIEFICKTIGTKPVAHIDQFT 352
Cdd:cd03341 224 ---------FSCPF-----DIGVNVIVAGGSV-----GDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 353 ADMLGSAELAEEVSLnGSGKLFKITGCTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIEL 432
Cdd:cd03341 285 PEEIGYCDSVYVEEI-GDTKVVVFRQNKEDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIEL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 433 ALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKG--GISNILEEMVVQ 510
Cdd:cd03341 364 AKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGdeGTKDAKEAGIFD 443
|
490 500
....*....|....*....|....*.
gi 6753322 511 PLLVSVSALTLATETVRSILKIDDVV 536
Cdd:cd03341 444 HLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
34-536 |
5.04e-112 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 342.06 E-value: 5.04e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 34 RFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHP----AARMLVELSKAQDIEAGDGTTSV 109
Cdd:COG0459 12 RRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTTTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 110 VIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNSKvvsqysSLLSPMSVN 189
Cdd:COG0459 92 TVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPV--DDKEELAQVATISANGD------EEIGELIAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 190 AVMKVIDPATATsvdlrdikiVKKLGGTIDDCELVEGLVLTQKVANSGItrvekakigliqfclsapktdmdnqivVSDY 269
Cdd:COG0459 164 AMEKVGKDGVIT---------VEEGKGLETELEVVEGMQFDKGYLSPYF---------------------------VTDP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 270 AQMDRVLreERAYIL-------------NLVKQIKKTGCNVLLIQKSIlrdalSDLALHFL--NKM----KIMVVK---- 326
Cdd:COG0459 208 EKMPAEL--ENAYILltdkkissiqdllPLLEKVAQSGKPLLIIAEDI-----DGEALATLvvNGIrgvlRVVAVKapgf 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 327 -DVEREDIEFICKTIGTKPVAH-----IDQFTADMLGSAELAEEvslnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEE 400
Cdd:COG0459 281 gDRRKAMLEDIAILTGGRVISEdlglkLEDVTLDDLGRAKRVEV----DKDNTTIVEGAGNP-KAIVILVGAATEVEVKE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 401 AERSIHDALCVIRCLVKKRaLIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTEL 480
Cdd:COG0459 356 RKRRVEDALHATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKV 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 6753322 481 RnrhAQGEKTTGINVRKGGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:COG0459 435 R---AAKDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVI 487
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
22-536 |
1.20e-111 |
|
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: 342.10 E-value: 1.20e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 22 SAYQDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIE 101
Cdd:TIGR02344 6 NQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 102 AGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSS 181
Cdd:TIGR02344 86 VGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRWSD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 182 LLSPMSVNAVMKV-IDPATATSVDL-RDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITR-VEKAKIGLIQFCLSAPKT 258
Cdd:TIGR02344 166 LMCDLALDAVRTVqRDENGRKEIDIkRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRyIENPRIVLLDCPLEYKKG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 259 DMDNQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDVEREDIEFICK 338
Cdd:TIGR02344 246 ESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGV-----SDLAQHYLLKANITAIRRVRKTDNNRIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 339 TIGTKPVAHIDQFTADMLGSAELAEEVSLNGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKK 418
Cdd:TIGR02344 321 ACGATIVNRPEELRESDVGTGCGLFEVKKIGDEYFTFITECKDP-KACTILLRGASKDILNEVERNLQDAMAVARNVLLD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 419 RALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEK-TTGINVRK 497
Cdd:TIGR02344 400 PKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNcTWGIDGET 479
|
490 500 510
....*....|....*....|....*....|....*....
gi 6753322 498 GGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:TIGR02344 480 GKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
23-536 |
9.61e-111 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 340.08 E-value: 9.61e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 23 AYQDRDKPAqiRFSNISAAKAVADAIRTSLGPKGMDKMIQ-----DGKGDVTITNDGATILKQMQVLHPAARMLVELSKA 97
Cdd:PTZ00212 15 AQEEKGETA--RLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKILVDISKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 98 QDIEAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSD---RETLLNSATTSLNSK 174
Cdd:PTZ00212 93 QDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEekfKEDLLNIARTTLSSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 175 VVSQYSSLLSPMSVNAVMKVIDpatatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITRVEKAKIgliqfcLS 254
Cdd:PTZ00212 173 LLTVEKDHFAKLAVDAVLRLKG-----SGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVGQPKRLENCKI------LV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 255 ApKTDMDN--------QIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLliqksILRDALSDLALHFLNKMKIMVVK 326
Cdd:PTZ00212 242 A-NTPMDTdkikiygaKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVF-----INRQLIYNYPEQLFAEAGIMAIE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 327 DVEREDIEFICKTIGTKPVAHIDQFTADMLGSAELAEEVSLnGSGKLFKITGCTSpGKTVTIVVRGSNKLVIEEAERSIH 406
Cdd:PTZ00212 316 HADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMI-GEDKLIRFSGCAK-GEACTIVLRGASTHILDEAERSLH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 407 DALCVIRCLVKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQ 486
Cdd:PTZ00212 394 DALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYK 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 6753322 487 GEKTTGINVRKGGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:PTZ00212 474 GNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDII 523
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
37-536 |
1.06e-110 |
|
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: 339.77 E-value: 1.06e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 37 NISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSL 116
Cdd:TIGR02346 23 NIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 117 LDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMS--RPVQLSDRETLLNSATTSLNSKVVSQYSsLLSPMSVNAVMKV 194
Cdd:TIGR02346 103 LNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVvwEVKDLRDKDELIKALKASISSKQYGNED-FLAQLVAQACSTV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 195 IdPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKvANSGITRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDR 274
Cdd:TIGR02346 182 L-PKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNRE-AEGSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNAEELLN 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 275 VLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDVEREDIEFICKTIGTKPVAHIDQFTAD 354
Cdd:TIGR02346 260 YSKGEENQIEAMIKAIADSGVNVIVTGGSV-----GDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 355 MLGSAELAEeVSLNGSGKLFKITGCTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELAL 434
Cdd:TIGR02346 335 EIGYVDSVY-VSEIGGDKVTVFKQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELAS 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 435 RLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKG--GISNILEEMVVQPL 512
Cdd:TIGR02346 414 RLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAEsdGVKDASEAGIYDML 493
|
490 500
....*....|....*....|....
gi 6753322 513 LVSVSALTLATETVRSILKIDDVV 536
Cdd:TIGR02346 494 ATKKWAIKLATEAAVTVLRVDQII 517
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
20-539 |
7.91e-88 |
|
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: 280.21 E-value: 7.91e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 20 GKSAYQDRDKPAqiRFSNISAAKAVADAIRTSLGPKGMDKMIQDG--KGDVTITNDGATILKQMQVLHPAARMLVELSKA 97
Cdd:TIGR02341 4 KDGADEERAENA--RLSSFVGAIAIGDLVKSTLGPKGMDKILQSSssDASIMVTNDGATILKSIGVDNPAAKVLVDMSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 98 QDIEAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSrpVQLSD-----RETLLNSATTSLN 172
Cdd:TIGR02341 82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSA--VDNGSdevkfRQDLMNIARTTLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 173 SKVVSQYSSLLSPMSVNAVMKVidpatATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITRVEKAKIGLIQFC 252
Cdd:TIGR02341 160 SKILSQHKDHFAQLAVDAVLRL-----KGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 253 LSAPKTDM-DNQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLliqksILRDALSDLALHFLNKMKIMVVKDVERE 331
Cdd:TIGR02341 235 MDTDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCF-----INRQLIYNYPEQLFADAGVMAIEHADFE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 332 DIEFICKTIGTKPVAHIDQFTADMLGSAELAEEVSLnGSGKLFKITGCTSpGKTVTIVVRGSNKLVIEEAERSIHDALCV 411
Cdd:TIGR02341 310 GVERLALVTGGEIVSTFDHPELVKLGSCDLIEEIMI-GEDKLLKFSGVKL-GEACTIVLRGATQQILDEAERSLHDALCV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 412 IRCLVKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTT 491
Cdd:TIGR02341 388 LSQTVKESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTM 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 6753322 492 GINVRKGGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVVNTR 539
Cdd:TIGR02341 468 GLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAA 515
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
37-536 |
2.01e-87 |
|
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: 277.99 E-value: 2.01e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 37 NISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSL 116
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 117 LDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQ-LSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVI 195
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEiDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 196 DPatATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSdyaqmdr 274
Cdd:cd03342 177 KP--DEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMpKRVENAYILTCNVSLEYEKTEVNSGFFYS------- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 275 vlreerayilnlvkqikktgcnVLLIQKSIlrDALSdlaLHFLNKMKIMVVKDVEREDIEFICKTIGTKPVAHIDQFTAD 354
Cdd:cd03342 248 ----------------------VVINQKGI--DPPS---LDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 355 MLGSAELAEEVSLnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELAL 434
Cdd:cd03342 301 CLGYAGLVYERTL-GEEKYTFIEGVKNP-KSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 435 RLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEMVVQPLLV 514
Cdd:cd03342 379 HLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSV 458
|
490 500
....*....|....*....|..
gi 6753322 515 SVSALTLATETVRSILKIDDVV 536
Cdd:cd03342 459 KRQILHSATVIASQLLLVDEII 480
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
37-536 |
1.52e-81 |
|
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: 263.90 E-value: 1.52e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 37 NISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSL 116
Cdd:TIGR02347 21 NINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 117 LDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLS-DRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVI 195
Cdd:TIGR02347 101 LKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEvDREFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 196 DPATAtsVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDR 274
Cdd:TIGR02347 181 KDGED--IDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMpRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQREK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 275 VLREERAYILNLVKQI---KKTGCN-------VLLIQKSIlrDALSdlaLHFLNKMKIMVVKDVEREDIEFICKTIGTKP 344
Cdd:TIGR02347 259 LVKAERKFVDDRVKKIielKKKVCGkspdkgfVVINQKGI--DPPS---LDLLAKEGIMALRRAKRRNMERLTLACGGEA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 345 VAHIDQFTADMLGSAELAEEVSLnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAG 424
Cdd:TIGR02347 334 LNSVEDLTPECLGWAGLVYETTI-GEEKYTFIEECKNP-KSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPG 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 425 GGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNIL 504
Cdd:TIGR02347 412 AGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGVDLNTGEPIDPE 491
|
490 500 510
....*....|....*....|....*....|..
gi 6753322 505 EEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:TIGR02347 492 IKGIWDNYRVKKQLIQSATVIASQLLLVDEVM 523
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
160-417 |
3.58e-64 |
|
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: 208.09 E-value: 3.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 160 RETLLNSATTSLNSKVvSQYSSLLSPMSVNAVMKVIDPATatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSG-I 238
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNR--MDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYmP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 239 TRVEKAKIGLIQFCLSapktdmdnqivvsdyaqmdrvlreerayilnlvkqikktgcNVLLIQKSIlrdalSDLALHFLN 318
Cdd:cd03333 78 KRLENAKILLLDCPLE-----------------------------------------YVVIAEKGI-----DDLALHYLA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 319 KMKIMVVKDVEREDIEFICKTIGTKPVAHIDQFTADMLGSAELAEEVSLnGSGKLFKITGCTSpGKTVTIVVRGSNKLVI 398
Cdd:cd03333 112 KAGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKI-GEEKLTFIEGCKG-GKAATILLRGATEVEL 189
|
250
....*....|....*....
gi 6753322 399 EEAERSIHDALCVIRCLVK 417
Cdd:cd03333 190 DEVKRSLHDALCAVRAAVE 208
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
33-523 |
1.70e-22 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 101.14 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 33 IRFSN------ISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPA----ARMLVELSKAQDIEA 102
Cdd:PTZ00114 17 IRFGDearqslLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 103 GDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNSKVVsqyssl 182
Cdd:PTZ00114 97 GDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPV--KTKEDILNVATISANGDVE------ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 183 LSPMSVNAVMKVIDPATATSVDlrdikivkklGGTIDD-CELVEGLVLTQK------VANSGITRVEkakigliqfcLSA 255
Cdd:PTZ00114 169 IGSLIADAMDKVGKDGTITVED----------GKTLEDeLEVVEGMSFDRGyispyfVTNEKTQKVE----------LEN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 256 PktdmdnQIVVSDY--AQMDRVLReerayILNLVKQIKKtgcNVLLIQKSILRDALSDLAlhfLNKM----KIMVVK--- 326
Cdd:PTZ00114 229 P------LILVTDKkiSSIQSILP-----ILEHAVKNKR---PLLIIAEDVEGEALQTLI---INKLrgglKVCAVKapg 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 327 --DVEREDIEFICKTIGTKPV------AHIDQFTADMLGSAELA-----EEVSLNGSG--KLFK---------ITGCTS- 381
Cdd:PTZ00114 292 fgDNRKDILQDIAVLTGATVVsednvgLKLDDFDPSMLGSAKKVtvtkdETVILTGGGdkAEIKervellrsqIERTTSe 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 382 -------------PGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELALRL--TEYSRTLSGM 446
Cdd:PTZ00114 372 ydkeklkerlaklSGGVAVIKVGGASEVEVNEKKDRIEDALNATRAAVEE-GIVPGGGVALLRASKLLdkLEEDNELTPD 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6753322 447 ESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRhaqGEKTTGINVRKGGISNILEEMVVQPLLVSVSALTLAT 523
Cdd:PTZ00114 451 QRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEK---KDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAA 524
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
41-526 |
1.12e-17 |
|
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: 85.97 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 41 AKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQ----VLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSL 116
Cdd:cd03344 17 VNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIEledpFENMGAQLVKEVASKTNDVAGDGTTTATVLARAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 117 LDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNSkvvsqySSLLSPMSVNAVMKVID 196
Cdd:cd03344 97 IKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPV--KTKEEIAQVATISANG------DEEIGELIAEAMEKVGK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 197 PATATsvdlrdikiVKKLGGTIDDCELVEGLVLtqkvaNSGitrvekakigliqfCLSaPK--TDMDNQIVVSdyaqmdr 274
Cdd:cd03344 169 DGVIT---------VEEGKTLETELEVVEGMQF-----DRG--------------YLS-PYfvTDPEKMEVEL------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 275 vlreERAYIL------NLVKQI-------KKTGCNVLLIQKSILRDALSDLALHFL-NKMKIMVVK-----DVER---ED 332
Cdd:cd03344 213 ----ENPYILltdkkiSSIQELlpilelvAKAGRPLLIIAEDVEGEALATLVVNKLrGGLKVCAVKapgfgDRRKamlED 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 333 I------EFICKTIGTKpvahIDQFTADMLGSAELAeEVS------LNGSGKLFKITG-----------CTSP------- 382
Cdd:cd03344 289 IailtggTVISEELGLK----LEDVTLEDLGRAKKV-VVTkddttiIGGAGDKAAIKAriaqirkqieeTTSDydkeklq 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 383 -------GKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELALRLtEYSRTLSGMESYCVRAFA 455
Cdd:cd03344 364 erlaklsGGVAVIKVGGATEVELKEKKDRVEDALNATRAAVEE-GIVPGGGVALLRASPAL-DKLKALNGDEKLGIEIVR 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 456 DAMEVIPSTLAENAGLNPISTVTELRNrhaqGEKTTGINVRKGGISNILEEMVVQPLLV---------SVSALTLATETV 526
Cdd:cd03344 442 RALEAPLRQIAENAGVDGSVVVEKVLE----SPDGFGYDAATGEYVDMIEAGIIDPTKVvrsalqnaaSVASLLLTTEAL 517
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
196-394 |
8.70e-17 |
|
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: 80.34 E-value: 8.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 196 DPATATSVDLRD-IKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLsapktdmDNQIVVSDYAQMD 273
Cdd:cd03334 37 DVRAGDDMDIRQyVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMpSKIKNPRILLLQGPL-------EYQRVENKLLSLD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 274 RVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDVEREDIEFICKTIGTKPVAHID-QFT 352
Cdd:cd03334 110 PVILQEKEYLKNLVSRIVALRPDVILVEKSV-----SRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDdLLT 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6753322 353 ADMLGSAELAEE---VSLNGSGK-LFKITGCTSPGKTvTIVVRGSN 394
Cdd:cd03334 185 SPKLGTCESFRVrtyVEEHGRSKtLMFFEGCPKELGC-TILLRGGD 229
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
32-526 |
3.10e-15 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 78.24 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 32 QIRFSN------ISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHP----AARMLVELSKAQDIE 101
Cdd:PRK12851 5 EVKFHVearekmLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 102 AGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNSkvvsqyss 181
Cdd:PRK12851 85 AGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPV--TTNAEIAQVATISANG-------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 182 llspmsvnavmkvidpatatsvdlrDIKIVKKLGGTIDdcelveglvltqKVANSGITRVEKAKIGLIQFCLsAPKTDMD 261
Cdd:PRK12851 155 -------------------------DAEIGRLVAEAME------------KVGNEGVITVEESKTAETELEV-VEGMQFD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 262 NQIV----VSDYAQMDRVLreERAYIL-------------NLVKQIKKTGCNVLLIQKSILRDALSDLAlhfLNKM---- 320
Cdd:PRK12851 197 RGYLspyfVTDADKMEAEL--EDPYILihekkisnlqdllPVLEAVVQSGKPLLIIAEDVEGEALATLV---VNKLrggl 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 321 KIMVVK--------DVEREDI------EFICKTIGTKpvahIDQFTADMLGSAELA----EEVSL-NGSGKLFKITG--- 378
Cdd:PRK12851 272 KVAAVKapgfgdrrKAMLEDIailtggTVISEDLGIK----LENVTLEQLGRAKKVvvekENTTIiDGAGSKTEIEGrva 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 379 --------CTSP--------------GKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELALRL 436
Cdd:PRK12851 348 qiraqieeTTSDydreklqerlaklaGGVAVIRVGASTEVEVKEKKDRVDDALHATRAAVEE-GIVPGGGVALLRAVKAL 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 437 TEySRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNrhaqGEKTTGINVRKGGISNILEEMVVQPLLV-- 514
Cdd:PRK12851 427 DK-LETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLRE----KPGGYGFNAATNEYGDLYAQGVIDPVKVvr 501
|
570
....*....|....*....
gi 6753322 515 -------SVSALTLATETV 526
Cdd:PRK12851 502 talqnaaSVAGLLLTTEAM 520
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
43-526 |
1.23e-14 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 76.38 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 43 AVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHP----AARMLVE-LSKAQDIeAGDGTTSVVIIAGSLL 117
Cdd:PRK12849 21 KLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEvASKTNDV-AGDGTTTATVLAQALV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 118 DSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNSKVvsqyssllspmsvnAVMKVIDP 197
Cdd:PRK12849 100 QEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPV--SGSEEIAQVATISANGDE--------------EIGELIAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 198 ATATsVDLRDIKIVKKLGGTIDDCELVEGLVLtqkvaNSG------ITRVEKakigliqfclsapktdmdnqivvsdyaq 271
Cdd:PRK12849 164 AMEK-VGKDGVITVEESKTLETELEVTEGMQF-----DRGylspyfVTDPER---------------------------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 272 MDRVLreERAYIL-------------NLVKQIKKTGCNVLLIQKSILRDALSDLalhFLNKM----KIMVVKDV---ER- 330
Cdd:PRK12849 210 MEAVL--EDPLILltdkkisslqdllPLLEKVAQSGKPLLIIAEDVEGEALATL---VVNKLrgglKVAAVKAPgfgDRr 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 331 ----EDI------EFICKTIGTKpvahIDQFTADMLGSAElaeevslngsgklfKITgctsPGKTVTIVVRGSN------ 394
Cdd:PRK12849 285 kamlEDIailtggTVISEDLGLK----LEEVTLDDLGRAK--------------RVT----ITKDNTTIVDGAGdkeaie 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 395 ------KLVIEEA----------ER--------------------------SIHDALCVIRCLVKKrALIAGGGAPEIEL 432
Cdd:PRK12849 343 arvaqiRRQIEETtsdydreklqERlaklaggvavikvgaatevelkerkdRVEDALNATRAAVEE-GIVPGGGVALLRA 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 433 ALRLTEYsRTLSGMESYCVRAFADAMEVIPSTLAENAGLNP---ISTVTELRNRHaqgekttGINVRKGGISNILEEMVV 509
Cdd:PRK12849 422 AKALDEL-AGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGsvvVAKVLELEDGF-------GFNAATGEYGDLIAAGII 493
|
570 580
....*....|....*....|....*.
gi 6753322 510 QPLLV---------SVSALTLATETV 526
Cdd:PRK12849 494 DPVKVtrsalqnaaSVAGLLLTTEAL 519
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
32-526 |
1.31e-14 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 76.30 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 32 QIRFSNISAAK------AVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVEL-----SKAQDI 100
Cdd:PRK12850 5 EIRFSTDARDRllrgvnILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMvkevaSKTNDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 101 eAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQlsDRETLLNSATTSLNSKvvsqys 180
Cdd:PRK12850 85 -AGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVT--SSKEIAQVATISANGD------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 181 sllspmsvNAVMKVIdpatATSVDlrdikivkklggtiddcelveglvltqKVANSGITRVEKAK-IGL-------IQFc 252
Cdd:PRK12850 156 --------ESIGEMI----AEAMD---------------------------KVGKEGVITVEEAKtLGTeldvvegMQF- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 253 lsapktdmDNQIV----VSDYAQMDRVLreERAYIL-------------NLVKQIKKTGCNVLLIQKSILRDALSDLALH 315
Cdd:PRK12850 196 --------DRGYLspyfVTNPEKMRAEL--EDPYILlhekkisnlqdllPILEAVVQSGRPLLIIAEDVEGEALATLVVN 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 316 FLNK-MKIMVVK--------DVEREDI------EFICKTIGTKpvahIDQFTADMLGSA-----ELAEEVSLNGSGKLFK 375
Cdd:PRK12850 266 KLRGgLKSVAVKapgfgdrrKAMLEDIavltggQVISEDLGIK----LENVTLDMLGRAkrvliTKENTTIIDGAGDKKN 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 376 ITGCTS-------------------------PGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPEI 430
Cdd:PRK12850 342 IEARVKqiraqieettsdydreklqerlaklAGGVAVIRVGGATEVEVKEKKDRVDDALHATRAAVEE-GIVPGGGVALL 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 431 ElALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNP---ISTVTELRNRHaqgekttGINVRKGGISNILEEM 507
Cdd:PRK12850 421 R-ARSALRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGsvvVGKVAELPGNF-------GFNAQTGEYGDMVEAG 492
|
570 580
....*....|....*....|....*...
gi 6753322 508 VVQPLLV---------SVSALTLATETV 526
Cdd:PRK12850 493 IIDPAKVtrtalqdaaSIAALLITTEAM 520
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
30-173 |
5.87e-14 |
|
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: 74.25 E-value: 5.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 30 PAQIRFSNISAAK------AVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVEL-----SKAQ 98
Cdd:TIGR02348 1 AKQIKFDEEARKAllrgvdKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLvkevaSKTN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6753322 99 DIeAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNS 173
Cdd:TIGR02348 81 DV-AGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPV--KGKKEIAQVATISANN 152
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
24-530 |
1.56e-11 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 66.67 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 24 YQDRDKPAQIRFSNIsaakaVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVEL-----SKAQ 98
Cdd:CHL00093 7 YQDNARRALERGMDI-----LAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALirqaaSKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 99 DIeAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQlsDRETLLNSATTSL-NSKVVS 177
Cdd:CHL00093 82 DV-AGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVE--DIQAITQVASISAgNDEEVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 178 QyssllspMSVNAVMKVidpatatsvdLRDIKIVKKLG-GTIDDCELVEGLvltqkvansgitRVEKAKIgliqfclsap 256
Cdd:CHL00093 159 S-------MIADAIEKV----------GREGVISLEEGkSTVTELEITEGM------------RFEKGFI---------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 257 ktdmdNQIVVSDYAQMDRVLreERAYIL------NLVKQ--------IKKTGCNVLLIQKSILRDALSDLalhFLNKMK- 321
Cdd:CHL00093 200 -----SPYFVTDTERMEVVQ--ENPYILltdkkiTLVQQdllpileqVTKTKRPLLIIAEDVEKEALATL---VLNKLRg 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 322 IMVVKDV------ER-----EDI------EFICKTIGTKpvahIDQFTADMLGSA------------------------- 359
Cdd:CHL00093 270 IVNVVAVrapgfgDRrkamlEDIailtggQVITEDAGLS----LETIQLDLLGQArriivtkdsttiiadgneeqvkarc 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 360 -ELAEEVSLNGSG--------KLFKITGctspGKTVtIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPEI 430
Cdd:CHL00093 346 eQLRKQIEIADSSyekeklqeRLAKLSG----GVAV-IKVGAATETEMKDKKLRLEDAINATKAAVEE-GIVPGGGATLV 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 431 ELALRLTEYSRT-LSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRhaqgEKTTGINVRKGGISNILEEMVV 509
Cdd:CHL00093 420 HLSENLKTWAKNnLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQ----DFEIGYNAANNKFVNMYEAGII 495
|
570 580
....*....|....*....|.
gi 6753322 510 QPLLVSVSALTLATETVRSIL 530
Cdd:CHL00093 496 DPAKVTRSALQNAASIASMIL 516
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
44-524 |
5.55e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 64.87 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 44 VADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVL----HPAARMLVEL-SKAQDIeAGDGTTSVVIIAGSLLD 118
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVaSKTNDL-AGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 119 SCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSdrETLLNSATTSLNSKVvsqyssllspmsvnAVMKVIDPA 198
Cdd:PRK12852 102 EGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASS--AEIAQVGTISANGDA--------------AIGKMIAQA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 199 tatsvdlrdikivkklggtiddcelveglvlTQKVANSGITRVEKAKigliqfclsapktDMDNQIVVSDYAQMDR---- 274
Cdd:PRK12852 166 -------------------------------MQKVGNEGVITVEENK-------------SLETEVDIVEGMKFDRgyls 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 275 ----------VLREERAYIL-------------NLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNK-MKIMVVK---- 326
Cdd:PRK12852 202 pyfvtnaekmTVELDDAYILlhekklsglqamlPVLEAVVQSGKPLLIIAEDVEGEALATLVVNRLRGgLKVAAVKapgf 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 327 -DVER---EDI------EFICKTIGTKpvahIDQFTADMLGSAELAE-----EVSLNGSGKLFKITG-----------CT 380
Cdd:PRK12852 282 gDRRKamlEDIailtggQLISEDLGIK----LENVTLKMLGRAKKVVidkenTTIVNGAGKKADIEArvgqikaqieeTT 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 381 S--------------PGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPeielALRLTEYSRTLSGM 446
Cdd:PRK12852 358 SdydreklqerlaklAGGVAVIRVGGATEVEVKEKKDRVEDALNATRAAVQE-GIVPGGGVA----LLRAKKAVGRINND 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 447 ES---YCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQgekTTGINVRKGGISNILEEMVVQPLLV--------- 514
Cdd:PRK12852 433 NAdvqAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSE---TFGFDAQTEEYVDMVAKGIIDPAKVvrtalqdaa 509
|
570
....*....|
gi 6753322 515 SVSALTLATE 524
Cdd:PRK12852 510 SVAGLLVTTE 519
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
43-173 |
6.93e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 64.76 E-value: 6.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 43 AVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVEL-----SKAQDIeAGDGTTSVVIIAGSLL 117
Cdd:PRK00013 21 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLvkevaSKTNDV-AGDGTTTATVLAQAIV 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 6753322 118 DSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNS 173
Cdd:PRK00013 100 REGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPV--EDKEEIAQVATISANG 153
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
44-159 |
2.07e-09 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 59.94 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 44 VADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVEL-----SKAQDIeAGDGTTSVVIIAGSLLD 118
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLvrqaaAKTNDL-AGDGTTTSVVLAQGLIA 156
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 6753322 119 SCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSD 159
Cdd:PLN03167 157 EGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE 197
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
44-526 |
1.07e-08 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 57.73 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 44 VADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQV----LHPAARMLVEL-SKAQDIeAGDGTTSVVIIAGSLLD 118
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVaSKSADA-AGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 119 SCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNSKvvSQYSSLLSpmsvNAVMKVIDPA 198
Cdd:PRK14104 102 EGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKV--TSNDEIAQVGTISANGD--AEIGKFLA----DAMKKVGNEG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 199 TATSVDLRDIKIvkklggtidDCELVEGLVLTQK-VANSGITRVEKAKIgliqfclsapktDMDNQIVVSDYAQMDRvLR 277
Cdd:PRK14104 174 VITVEEAKSLET---------ELDVVEGMQFDRGyISPYFVTNADKMRV------------EMDDAYILINEKKLSS-LN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 278 EerayILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFL-NKMKIMVVK-----DVEREDIEFICKTIGTKPVAH---- 347
Cdd:PRK14104 232 E----LLPLLEAVVQTGKPLVIVAEDVEGEALATLVVNRLrGGLKVAAVKapgfgDRRKAMLQDIAILTGGQAISEdlgi 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 348 -IDQFTADMLGSA-----ELAEEVSLNGSGKLFKITG-----------CTS--------------PGKTVTIVVRGSNKL 396
Cdd:PRK14104 308 kLENVTLQMLGRAkkvmiDKENTTIVNGAGKKADIEArvaqikaqieeTTSdydreklqerlaklAGGVAVIRVGGATEV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753322 397 VIEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELALRLTEYsRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPIST 476
Cdd:PRK14104 388 EVKERKDRVDDAMHATRAAVEE-GIVPGGGVALLRASEQLKGI-KTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVI 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 6753322 477 VTELRNRHaqgEKTTGINVRKGGISNILEEMVVQPLLV---------SVSALTLATETV 526
Cdd:PRK14104 466 VGKILEKE---QYSYGFDSQTGEYGNLVSKGIIDPTKVvrtaiqnaaSVAALLITTEAM 521
|
|
| |
