|
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: 979.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 25 QDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGD 104
Cdd:cd03338 1 TDKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 105 GTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELSDRETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:cd03338 81 GTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 185 PMSVNAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNS--GITRVEKAKIGLIQFCLSAPKTDMDN 262
Cdd:cd03338 161 PIAVDAVLKVIDPATATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKagGPTRIEKAKIGLIQFCLSPPKTDMDN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 263 QIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNKMKIMVIKDIEREDIEFICKTIGT 342
Cdd:cd03338 241 NIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQKSILRDAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 343 KPVAHIDQFTADMLGSAELAEEVNLnGSGKLLKITGCASPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALI 422
Cdd:cd03338 321 KPVASIDHFTEDKLGSADLVEEVSL-GDGKIVKITGVKNPGKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 423 AGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISN 502
Cdd:cd03338 400 PGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITN 479
|
490 500 510
....*....|....*....|....*....|....*.
gi 1996390964 503 ILEELVVQPLLVSVSALTLATETVRSILKIDDVVNT 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: 919.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 24 YQDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAG 103
Cdd:TIGR02342 1 FQDKDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 104 DGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELSDRETLLNSATTSLNSKVVSQYSSLL 183
Cdd:TIGR02342 81 DGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 184 SPMSVNAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKV--SNSGITRVEKAKIGLIQFCLSAPKTDMD 261
Cdd:TIGR02342 161 APLAVDAVLKVIDPENAKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKAskSAGGPTRIEKAKIGLIQFQISPPKTDME 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 262 NQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNKMKIMVIKDIEREDIEFICKTIG 341
Cdd:TIGR02342 241 NQIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSILRDAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 342 TKPVAHIDQFTADMLGSAELAEEVNLNGsGKLLKITGCASPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRAL 421
Cdd:TIGR02342 321 CKPIASIDHFTADKLGSAELVEEVDSDG-GKIIKITGIQNAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 422 IAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGIS 501
Cdd:TIGR02342 400 IAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGIT 479
|
490 500 510
....*....|....*....|....*....|....*...
gi 1996390964 502 NILEELVVQPLLVSVSALTLATETVRSILKIDDVVNTR 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: 584.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 26 DRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDG 105
Cdd:cd00309 2 EREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 106 TTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELSDRETLLNSATTSLNSKVVSQYSSLLSP 185
Cdd:cd00309 82 TTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 186 MSVNAVMKVIDPATatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSG-ITRVEKAKIGLIQFCLSapktdmdnqi 264
Cdd:cd00309 162 LVVDAVLKVGKENG--DVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYmPKRLENAKILLLDCKLE---------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 265 vvsdyaqmdrvlreerayilnlvkqikktgcNVLLIQKSIlrdalSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTKP 344
Cdd:cd00309 230 -------------------------------YVVIAEKGI-----DDEALHYLAKLGIMAVRRVRKEDLERIAKATGATI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 345 VAHIDQFTADMLGSAELAEEVNLnGSGKLLKITGCASpGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAG 424
Cdd:cd00309 274 VSRLEDLTPEDLGTAGLVEETKI-GDEKYTFIEGCKG-GKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 425 GGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNIL 504
Cdd:cd00309 352 GGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMK 431
|
490 500 510
....*....|....*....|....*....|..
gi 1996390964 505 EELVVQPLLVSVSALTLATETVRSILKIDDVV 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: 554.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 44 VADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSLLDSCTKL 123
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 124 LQKGIHPTIISESFQKALEKGIEILTDM-SRPVELSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVidPATATS 202
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAI--PKNDGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 203 VDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSG-ITRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDRVLREERA 281
Cdd:pfam00118 159 FDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDmPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 282 YILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTKPVAHIDQFTADMLGSAEL 361
Cdd:pfam00118 239 QILEIVEKIIDSGVNVVVCQKGI-----DDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 362 AEEVNLnGSGKLLKITGCASPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELALRLTEYSR 441
Cdd:pfam00118 314 VEEEKI-GDEKYTFIEGCKSP-KAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 442 TLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNILEELVVQPLLVSVSALTL 521
Cdd:pfam00118 392 SVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
|
490
....*....|....*...
gi 1996390964 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: 542.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:NF041082 21 NNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 116 LLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVI 195
Cdd:NF041082 101 LLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVKAVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 196 DPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSGI-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDR 274
Cdd:NF041082 181 EKDGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMpKRVENAKIALLDAPLEVKKTEIDAKISITDPDQLQA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 275 VLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTKPVAHIDQFTAD 354
Cdd:NF041082 261 FLDQEEKMLKEMVDKIADSGANVVFCQKGI-----DDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSIDDLSPE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 355 MLGSAELAEEVNLNGSgKLLKITGCASPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELAL 434
Cdd:NF041082 336 DLGYAGLVEERKVGGD-KMIFVEGCKNP-KAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEVELAL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 435 RLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNILEELVVQPLLV 514
Cdd:NF041082 414 RLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVVEPLRV 493
|
490 500
....*....|....*....|..
gi 1996390964 515 SVSALTLATETVRSILKIDDVV 536
Cdd:NF041082 494 KTQAIKSATEAAVMILRIDDVI 515
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
36-536 |
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: 527.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:cd03343 19 MNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 116 LLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVI 195
Cdd:cd03343 99 LLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAEAAKDKLADLVVDAVLQVA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 196 DPAT-ATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSGI-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMD 273
Cdd:cd03343 179 EKRDgKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMpKRVENAKIALLDAPLEVKKTEIDAKIRITSPDQLQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 274 RVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTKPVAHIDQFTA 353
Cdd:cd03343 259 AFLEQEEAMLKEMVDKIADTGANVVFCQKGI-----DDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTNIDDLTP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 354 DMLGSAELAEEVNLNGSgKLLKITGCASPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELA 433
Cdd:cd03343 334 EDLGEAELVEERKVGDD-KMVFVEGCKNP-KAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGAVEIELA 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 434 LRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNILEELVVQPLL 513
Cdd:cd03343 412 KRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVDMLEKGVIEPLR 491
|
490 500
....*....|....*....|...
gi 1996390964 514 VSVSALTLATETVRSILKIDDVV 536
Cdd:cd03343 492 VKKQAIKSATEAATMILRIDDVI 514
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
26-536 |
6.08e-179 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 513.73 E-value: 6.08e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 26 DRDKPAQirFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDG 105
Cdd:NF041083 13 TKGRDAQ--RNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 106 TTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELSDRETLLNSATTSLNSKVVSQYSSLLSP 185
Cdd:NF041083 91 TTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKGVEEARDYLAE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 186 MSVNAVMKVIDPATAT-SVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSGI-TRVEKAKIGLIQFCLSAPKTDMDNQ 263
Cdd:NF041083 171 IAVKAVKQVAEKRDGKyYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMpKRVENAKIALLDAPLEVKKTEIDAE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 264 IVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTK 343
Cdd:NF041083 251 IRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGI-----DDLAQHYLAKAGILAVRRVKKSDMEKLAKATGAR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 344 PVAHIDQFTADMLGSAELAEEVNLnGSGKLLKITGCASPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIA 423
Cdd:NF041083 326 IVTNIDDLTPEDLGYAELVEERKV-GDDKMVFVEGCKNP-KAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 424 GGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNI 503
Cdd:NF041083 404 GGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVDM 483
|
490 500 510
....*....|....*....|....*....|...
gi 1996390964 504 LEELVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:NF041083 484 WELGVIEPLRVKTQAIKSATEAATMILRIDDVI 516
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
36-536 |
2.85e-175 |
|
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: 504.60 E-value: 2.85e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:TIGR02339 20 NNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 116 LLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELSDRETLLNSATTSLNSKVVSQYS-SLLSPMSVNAVMKV 194
Cdd:TIGR02339 100 LLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSKASAEVAkDKLADLVVEAVKQV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 195 IDPATATS--VDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSGI-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQ 271
Cdd:TIGR02339 180 AELRGDGKyyVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMpKRVENAKIALLDAPLEVEKTEIDAKIRITDPDQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 272 MDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTKPVAHIDQF 351
Cdd:TIGR02339 260 IKKFLDQEEAMLKEMVDKIASAGANVVICQKGI-----DDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVSSIDEI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 352 TADMLGSAELAEEVNLnGSGKLLKITGCASPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIE 431
Cdd:TIGR02339 335 TESDLGYAELVEERKV-GEDKMVFVEGCKNP-KAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVAGGGAVEIE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 432 LALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNILEELVVQP 511
Cdd:TIGR02339 413 LALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTGEIEDMLELGVIEP 492
|
490 500
....*....|....*....|....*
gi 1996390964 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 |
6.61e-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: 434.80 E-value: 6.61e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:cd03339 27 SHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 116 LLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELS--DRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMK 193
Cdd:cd03339 107 LLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSpdNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAVLS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 194 VIDpATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSGITR-VEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQM 272
Cdd:cd03339 187 VAD-LERKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKeVKDAKIAILTCPFEPPKPKTKHKLDITSVEDY 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 273 DRVLREERAYILNLVKQIKKTGCNVLLIQKsilrdALSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTKPVAHIDQFT 352
Cdd:cd03339 266 KKLQEYEQKYFREMVEQVKDAGANLVICQW-----GFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFEDLS 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 353 ADMLGSAELAEEVNLNGS-GKLLKITGCAsPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIE 431
Cdd:cd03339 341 PEKLGKAGLVREISFGTTkDKMLVIEGCP-NSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGGGAAEIS 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 432 LALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRH-AQGEKTAGINVRKGGISNILEELVVQ 510
Cdd:cd03339 420 CSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPHLGIDCLGRGTNDMKEQKVFE 499
|
490 500
....*....|....*....|....*.
gi 1996390964 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 |
1.47e-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: 388.39 E-value: 1.47e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 27 RDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGT 106
Cdd:TIGR02343 22 RLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 107 TSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELSD--RETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:TIGR02343 102 TGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNnnREPLIQAAKTSLGSKIVSKCHRRFA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 185 PMSVNAVMKVIDpATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSGITR-VEKAKIGLIQFCLSAPKTDMDNQ 263
Cdd:TIGR02343 182 EIAVDAVLNVAD-MERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKeVEDAKIAILTCPFEPPKPKTKHK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 264 IVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKsilrdALSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTK 343
Cdd:TIGR02343 261 LDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQW-----GFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 344 PVAHIDQFTADMLGSAELAEEVNLNGSG-KLLKITGCASpGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALI 422
Cdd:TIGR02343 336 IVPRFQELSKDKLGKAGLVREISFGTTKdRMLVIEQCKN-SKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 423 AGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTA-GINVRKGGIS 501
Cdd:TIGR02343 415 YGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNlGVDCLGYGTN 494
|
490 500 510
....*....|....*....|....*....|....*
gi 1996390964 502 NILEELVVQPLLVSVSALTLATETVRSILKIDDVV 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 |
3.48e-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: 384.33 E-value: 3.48e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:cd03340 20 SNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 116 LLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELSD----RETLLNSATTSLNSKVVSQYSSLLSPMSVNAV 191
Cdd:cd03340 100 FLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDkeeqRELLEKCAATALNSKLIASEKEFFAKMVVDAV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 192 MKVIDpatatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSGI----TRVEKAKIGLIQFCLSApKTDMDN-QIVV 266
Cdd:cd03340 180 LSLDD-----DLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAGFeqqpKKFKNPKILLLNVELEL-KAEKDNaEVRV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 267 SDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTKPVA 346
Cdd:cd03340 254 EDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPI-----GDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 347 HIDQFTADMLGSAELAEEVNLnGSGKLLKITGCASpGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGG 426
Cdd:cd03340 329 TVSNITDDVLGTCGLFEERQV-GGERYNIFTGCPK-AKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 427 APEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKT-AGINVRKGGISNILE 505
Cdd:cd03340 407 AIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKwYGVDINNEGIADNFE 486
|
490 500 510
....*....|....*....|....*....|.
gi 1996390964 506 ELVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:cd03340 487 AFVWEPSLVKINALTAATEAACLILSVDETI 517
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
26-536 |
4.91e-122 |
|
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: 368.92 E-value: 4.91e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 26 DRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDG 105
Cdd:cd03335 2 ERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 106 TTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTD-MSRPVELSDRETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDNLGKESLINVAKTSMSSKIIGADSDFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 185 PMSVNAVM--KVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSGI-TRVEKAKIGLIQFCLSAPKTDMD 261
Cdd:cd03335 162 NMVVDAILavKTTNEKGKTKYPIKAVNILKAHGKSAKESYLVNGYALNCTRASQGMpTRVKNAKIACLDFNLQKTKMKLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 262 NQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVIKDIEREDIEFICKTIG 341
Cdd:cd03335 242 VQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGI-----DDMCLKYFVEAGAMAVRRVKKEDLRRIAKATG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 342 TKPVAHI------DQFTADMLGSAELAEEVNLnGSGKLLKITGCaSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCL 415
Cdd:cd03335 317 ATLVSTLanlegeETFDPSYLGEAEEVVQERI-GDDELILIKGT-KKRSSASIILRGANDFMLDEMERSLHDALCVVKRT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 416 VKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHA--------QG 487
Cdd:cd03335 395 LESNSVVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAaaqvkpdkKH 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1996390964 488 EKTAGINVRKGGISNILEELVVQPLLVSVSALTLATETVRSILKIDDVV 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 |
2.66e-121 |
|
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: 365.08 E-value: 2.66e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 27 RDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGT 106
Cdd:cd03337 11 RESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 107 TSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELSDRETLLNSATTSLNSKVVSQYSSLLSPM 186
Cdd:cd03337 91 TSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFVSRWSDLMCNL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 187 SVNAVMKVI--DPATATSVDL-RDIKIVKKLGGTIDDCELVEGLVLtqkvsnsgitrvekakigliqfclsapktdmdNQ 263
Cdd:cd03337 171 ALDAVKTVAveENGRKKEIDIkRYAKVEKIPGGEIEDSRVLDGVML--------------------------------NK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 264 IVVsdYAQMDRVLREERAYILNlvkqikktgCNVLLIqkSILRDALSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTK 343
Cdd:cd03337 219 DVT--HPKMRRRIENPRIVLLD---------CPLEYL--VITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARACGAT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 344 PVAHIDQFTADMLGSAELAEEVNLNGSGKLLKITGCASPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIA 423
Cdd:cd03337 286 IVNRPEELTESDVGTGAGLFEVKKIGDEYFTFITECKDP-KACTILLRGASKDVLNEVERNLQDAMAVARNIILNPKLVP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 424 GGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEK-TAGINVRKGGISN 502
Cdd:cd03337 365 GGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENsTWGIDGETGDIVD 444
|
490 500 510
....*....|....*....|....*....|....
gi 1996390964 503 ILEELVVQPLLVSVSALTLATETVRSILKIDDVV 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 |
1.65e-118 |
|
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: 360.19 E-value: 1.65e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 26 DRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDG 105
Cdd:TIGR02340 6 ERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 106 TTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTD-MSRPVELSDRETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDELGREALINVAKTSMSSKIIGLDSDFFS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 185 PMSVNAVM--KVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSGI-TRVEKAKIGLIQFCLSAPKTDMD 261
Cdd:TIGR02340 166 NIVVDAVLavKTTNENGETKYPIKAINILKAHGKSARESMLVKGYALNCTVASQQMpKRIKNAKIACLDFNLQKAKMALG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 262 NQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVIKDIEREDIEFICKTIG 341
Cdd:TIGR02340 246 VQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGI-----DDMCLKYFVEAGAMGVRRCKKEDLKRIAKATG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 342 TKPVAHI------DQFTADMLGSAELAEEVNLnGSGKLLKITGcASPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCL 415
Cdd:TIGR02340 321 ATLVSTLadlegeETFEASYLGFADEVVQERI-ADDECILIKG-TKKRKSASIILRGANDFMLDEMERSLHDALCVVKRT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 416 VKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHA--------QG 487
Cdd:TIGR02340 399 LESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAaaqlkpekKH 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1996390964 488 EKTAGINVRKGGISNILEELVVQPLLVSVSALTLATETVRSILKIDDVV 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 |
2.38e-118 |
|
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: 359.07 E-value: 2.38e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:TIGR02345 22 SNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 116 LLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELSD---RETLLNSATTSLNSKVVSQYSSLLSPMSVNAVM 192
Cdd:TIGR02345 102 LLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqRELLEKCAATALSSKLISHNKEFFSKMIVDAVL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 193 KVIDPAtatsVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSGI----TRVEKAKIGLIQFCLSApKTDMDN-QIVVS 267
Cdd:TIGR02345 182 SLDRDD----LDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAGFeqqpKKFANPKILLLNVELEL-KAEKDNaEIRVE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 268 DYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTKPVAH 347
Cdd:TIGR02345 257 DVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPI-----GDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQST 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 348 IDQFTADMLGSAELAEEVNLnGSGKLLKITGCASpGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGA 427
Cdd:TIGR02345 332 TSDLEADVLGTCALFEERQI-GSERYNYFTGCPH-AKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 428 PEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNILEEL 507
Cdd:TIGR02345 410 IEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFEAF 489
|
490 500
....*....|....*....|....*....
gi 1996390964 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 |
3.38e-116 |
|
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: 353.56 E-value: 3.38e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 34 RFSNISAAKAVADAIRTSLGPKGMDKMIQDG--KGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVI 111
Cdd:cd03336 15 RLSSFVGAIAIGDLVKTTLGPKGMDKILQSVgrSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDGTTSVTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 112 IAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELSD---RETLLNSATTSLNSKVVSQYSSLLSPMSV 188
Cdd:cd03336 95 LAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEeafREDLLNIARTTLSSKILTQDKEHFAELAV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 189 NAVMKVIDpatatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSGITRVEKAKIgLIQfclsapKTDMDN------ 262
Cdd:cd03336 175 DAVLRLKG-----SGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQPKRIENAKI-LIA------NTPMDTdkikif 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 263 --QIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLliqksILRDALSDLALHFLNKMKIMVIKDIEREDIEFICKTI 340
Cdd:cd03336 243 gaKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCF-----INRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 341 GTKPVAHIDQFTADMLGSAELAEEVNLnGSGKLLKITGCASpGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRA 420
Cdd:cd03336 318 GGEIASTFDHPELVKLGTCKLIEEIMI-GEDKLIRFSGVAA-GEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 421 LIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGI 500
Cdd:cd03336 396 VVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTV 475
|
490 500 510
....*....|....*....|....*....|....*.
gi 1996390964 501 SNILEELVVQPLLVSVSALTLATETVRSILKIDDVV 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 |
3.08e-112 |
|
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: 341.51 E-value: 3.08e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 35 FSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAG 114
Cdd:cd03341 11 LRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 115 SLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMS--RPVELSDRETLLNSATTSLNSKVVSqYSSLLSPMSVNAVM 192
Cdd:cd03341 91 ELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVvyKIEDLRNKEEVSKALKTAIASKQYG-NEDFLSPLVAEACI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 193 KVIdPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSgITRVEKAKIGLiqfclsapktdmdnqivvsdyaqm 272
Cdd:cd03341 170 SVL-PENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKREPEGS-VKRVKKAKVAV------------------------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 273 drvlreeraYILNLvkqikKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTKPVAHIDQFT 352
Cdd:cd03341 224 ---------FSCPF-----DIGVNVIVAGGSV-----GDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 353 ADMLGSAELA--EEVnlnGSGKLLKITGCASPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEI 430
Cdd:cd03341 285 PEEIGYCDSVyvEEI---GDTKVVVFRQNKEDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 431 ELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKG--GISNILEELV 508
Cdd:cd03341 362 ELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGdeGTKDAKEAGI 441
|
490 500
....*....|....*....|....*...
gi 1996390964 509 VQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:cd03341 442 FDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
34-536 |
6.89e-112 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 341.67 E-value: 6.89e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 34 RFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHP----AARMLVELSKAQDIEAGDGTTSV 109
Cdd:COG0459 12 RRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTTTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 110 VIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVElsDRETLLNSATTSLNSKvvsqysSLLSPMSVN 189
Cdd:COG0459 92 TVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVD--DKEELAQVATISANGD------EEIGELIAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 190 AVMKVIDPATATsvdlrdikiVKKLGGTIDDCELVEGLVL------TQKVSNSG--ITRVEKAKIGLIQFCLSAPKTdmd 261
Cdd:COG0459 164 AMEKVGKDGVIT---------VEEGKGLETELEVVEGMQFdkgylsPYFVTDPEkmPAELENAYILLTDKKISSIQD--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 262 nqivvsdyaqmdrvlreerayILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFL--NKM----KIMVIK-----DIER 330
Cdd:COG0459 232 ---------------------LLPLLEKVAQSGKPLLIIAEDI-----DGEALATLvvNGIrgvlRVVAVKapgfgDRRK 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 331 EDIEFICKTIGTKPVAH-----IDQFTADMLGSAELAEEvnlnGSGKLLKITGCASPgKTVTIVVRGSNKLVIEEAERSI 405
Cdd:COG0459 286 AMLEDIAILTGGRVISEdlglkLEDVTLDDLGRAKRVEV----DKDNTTIVEGAGNP-KAIVILVGAATEVEVKERKRRV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 406 HDALCVIRCLVKKRaLIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRnrhA 485
Cdd:COG0459 361 EDALHATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVR---A 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1996390964 486 QGEKTAGINVRKGGISNILEELVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:COG0459 437 AKDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVI 487
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
34-536 |
1.16e-111 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 342.39 E-value: 1.16e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 34 RFSNISAAKAVADAIRTSLGPKGMDKMIQ-----DGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTS 108
Cdd:PTZ00212 24 RLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGDGTTS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 109 VVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELSD---RETLLNSATTSLNSKVVSQYSSLLSP 185
Cdd:PTZ00212 104 VVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEekfKEDLLNIARTTLSSKLLTVEKDHFAK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 186 MSVNAVMKVIDpatatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSGITRVEKAKIgliqfcLSApKTDMDN--- 262
Cdd:PTZ00212 184 LAVDAVLRLKG-----SGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVGQPKRLENCKI------LVA-NTPMDTdki 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 263 -----QIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLliqksILRDALSDLALHFLNKMKIMVIKDIEREDIEFIC 337
Cdd:PTZ00212 252 kiygaKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVF-----INRQLIYNYPEQLFAEAGIMAIEHADFDGMERLA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 338 KTIGTKPVAHIDQFTADMLGSAELAEEVnLNGSGKLLKITGCASpGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVK 417
Cdd:PTZ00212 327 AALGAEIVSTFDTPEKVKLGHCDLIEEI-MIGEDKLIRFSGCAK-GEACTIVLRGASTHILDEAERSLHDALCVLSQTVK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 418 KRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRK 497
Cdd:PTZ00212 405 DTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGIDMEK 484
|
490 500 510
....*....|....*....|....*....|....*....
gi 1996390964 498 GGISNILEELVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:PTZ00212 485 GTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDII 523
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
25-536 |
9.54e-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: 339.79 E-value: 9.54e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 25 QDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGD 104
Cdd:TIGR02344 9 TKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 105 GTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELSDRETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:TIGR02344 89 GTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRWSDLMC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 185 PMSVNAVMKV-IDPATATSVDL-RDIKIVKKLGGTIDDCELVEGLVLTQKVSNSGITR-VEKAKIGLIQFCLSAPKTDMD 261
Cdd:TIGR02344 169 DLALDAVRTVqRDENGRKEIDIkRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRyIENPRIVLLDCPLEYKKGESQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 262 NQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVIKDIEREDIEFICKTIG 341
Cdd:TIGR02344 249 TNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGV-----SDLAQHYLLKANITAIRRVRKTDNNRIARACG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 342 TKPVAHIDQFTADMLGSAELAEEVNLNGSGKLLKITGCASPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRAL 421
Cdd:TIGR02344 324 ATIVNRPEELRESDVGTGCGLFEVKKIGDEYFTFITECKDP-KACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 422 IAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEK-TAGINVRKGGI 500
Cdd:TIGR02344 403 VPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNcTWGIDGETGKI 482
|
490 500 510
....*....|....*....|....*....|....*.
gi 1996390964 501 SNILEELVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:TIGR02344 483 VDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
37-536 |
8.69e-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: 337.46 E-value: 8.69e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 37 NISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSL 116
Cdd:TIGR02346 23 NIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 117 LDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMS--RPVELSDRETLLNSATTSLNSKVVSQYSsLLSPMSVNAVMKV 194
Cdd:TIGR02346 103 LNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVvwEVKDLRDKDELIKALKASISSKQYGNED-FLAQLVAQACSTV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 195 IdPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKvSNSGITRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDR 274
Cdd:TIGR02346 182 L-PKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNRE-AEGSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNAEELLN 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 275 VLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTKPVAHIDQFTAD 354
Cdd:TIGR02346 260 YSKGEENQIEAMIKAIADSGVNVIVTGGSV-----GDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 355 MLGSAELA--EEVnlnGSGKLLKITGCASPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIEL 432
Cdd:TIGR02346 335 EIGYVDSVyvSEI---GGDKVTVFKQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIEL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 433 ALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKG--GISNILEELVVQ 510
Cdd:TIGR02346 412 ASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAEsdGVKDASEAGIYD 491
|
490 500
....*....|....*....|....*.
gi 1996390964 511 PLLVSVSALTLATETVRSILKIDDVV 536
Cdd:TIGR02346 492 MLATKKWAIKLATEAAVTVLRVDQII 517
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
34-539 |
9.31e-89 |
|
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: 282.52 E-value: 9.31e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 34 RFSNISAAKAVADAIRTSLGPKGMDKMIQDG--KGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVI 111
Cdd:TIGR02341 16 RLSSFVGAIAIGDLVKSTLGPKGMDKILQSSssDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEVGDGTTSVTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 112 IAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSrpVELSD-----RETLLNSATTSLNSKVVSQYSSLLSPM 186
Cdd:TIGR02341 96 LAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSA--VDNGSdevkfRQDLMNIARTTLSSKILSQHKDHFAQL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 187 SVNAVMKVidpatATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSGITRVEKAKIGLIQFCLSAPKTDM-DNQIV 265
Cdd:TIGR02341 174 AVDAVLRL-----KGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKVKIfGSRVR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 266 VSDYAQMDRVLREERAYILNLVKQIKKTGCNVLliqksILRDALSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTKPV 345
Cdd:TIGR02341 249 VDSTAKVAELEHAEKEKMKEKVEKILKHGINCF-----INRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 346 AHIDQFTADMLGSAELAEEVNLnGSGKLLKITGCASpGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGG 425
Cdd:TIGR02341 324 STFDHPELVKLGSCDLIEEIMI-GEDKLLKFSGVKL-GEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 426 GAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNILE 505
Cdd:TIGR02341 402 GCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGTIADMRQ 481
|
490 500 510
....*....|....*....|....*....|....
gi 1996390964 506 ELVVQPLLVSVSALTLATETVRSILKIDDVVNTR 539
Cdd:TIGR02341 482 LGITESYKVKRAVVSSAAEAAEVILRVDNIIKAA 515
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
37-536 |
2.48e-85 |
|
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: 272.59 E-value: 2.48e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 37 NISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSL 116
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 117 LDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVE-LSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVI 195
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEiDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 196 DPatATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSGI-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSdyaqmdr 274
Cdd:cd03342 177 KP--DEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMpKRVENAYILTCNVSLEYEKTEVNSGFFYS------- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 275 vlreerayilnlvkqikktgcnVLLIQKSIlrDALSdlaLHFLNKMKIMVIKDIEREDIEFICKTIGTKPVAHIDQFTAD 354
Cdd:cd03342 248 ----------------------VVINQKGI--DPPS---LDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 355 MLGSAELAEEVNLnGSGKLLKITGCASPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELAL 434
Cdd:cd03342 301 CLGYAGLVYERTL-GEEKYTFIEGVKNP-KSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 435 RLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNILEELVVQPLLV 514
Cdd:cd03342 379 HLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSV 458
|
490 500
....*....|....*....|..
gi 1996390964 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 |
4.49e-80 |
|
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: 260.05 E-value: 4.49e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 37 NISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSL 116
Cdd:TIGR02347 21 NINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 117 LDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELS-DRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVI 195
Cdd:TIGR02347 101 LKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEvDREFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 196 DPATAtsVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSGI-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDR 274
Cdd:TIGR02347 181 KDGED--IDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMpRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQREK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 275 VLREERAYILNLVKQI---KKTGCN-------VLLIQKSIlrDALSdlaLHFLNKMKIMVIKDIEREDIEFICKTIGTKP 344
Cdd:TIGR02347 259 LVKAERKFVDDRVKKIielKKKVCGkspdkgfVVINQKGI--DPPS---LDLLAKEGIMALRRAKRRNMERLTLACGGEA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 345 VAHIDQFTADMLGSAELAEEVNLnGSGKLLKITGCASPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAG 424
Cdd:TIGR02347 334 LNSVEDLTPECLGWAGLVYETTI-GEEKYTFIEECKNP-KSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPG 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 425 GGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNIL 504
Cdd:TIGR02347 412 AGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGVDLNTGEPIDPE 491
|
490 500 510
....*....|....*....|....*....|..
gi 1996390964 505 EELVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:TIGR02347 492 IKGIWDNYRVKKQLIQSATVIASQLLLVDEVM 523
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
160-417 |
6.63e-63 |
|
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: 204.62 E-value: 6.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 160 RETLLNSATTSLNSKVvSQYSSLLSPMSVNAVMKVIDPATatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVSNSG-I 238
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNR--MDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYmP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 239 TRVEKAKIGLIQFCLSapktdmdnqivvsdyaqmdrvlreerayilnlvkqikktgcNVLLIQKSIlrdalSDLALHFLN 318
Cdd:cd03333 78 KRLENAKILLLDCPLE-----------------------------------------YVVIAEKGI-----DDLALHYLA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 319 KMKIMVIKDIEREDIEFICKTIGTKPVAHIDQFTADMLGSAELAEEVNLnGSGKLLKITGCASpGKTVTIVVRGSNKLVI 398
Cdd:cd03333 112 KAGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKI-GEEKLTFIEGCKG-GKAATILLRGATEVEL 189
|
250
....*....|....*....
gi 1996390964 399 EEAERSIHDALCVIRCLVK 417
Cdd:cd03333 190 DEVKRSLHDALCAVRAAVE 208
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
33-523 |
2.39e-21 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 97.68 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 33 IRFSN------ISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPA----ARMLVELSKAQDIEA 102
Cdd:PTZ00114 17 IRFGDearqslLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 103 GDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVElsDRETLLNSATTSLNSKVVsqyssl 182
Cdd:PTZ00114 97 GDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVK--TKEDILNVATISANGDVE------ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 183 LSPMSVNAVMKVIDPATATSVDlrdikivkklGGTIDD-CELVEGLVLTQK------VSNSGITRVEkakigliqfcLSA 255
Cdd:PTZ00114 169 IGSLIADAMDKVGKDGTITVED----------GKTLEDeLEVVEGMSFDRGyispyfVTNEKTQKVE----------LEN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 256 PktdmdnQIVVSDY--AQMDRVLReerayILNLVKQIKKtgcNVLLIQKSILRDALSDLAlhfLNKMKIMV--------- 324
Cdd:PTZ00114 229 P------LILVTDKkiSSIQSILP-----ILEHAVKNKR---PLLIIAEDVEGEALQTLI---INKLRGGLkvcavkapg 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 325 ---IKDIEREDIEFIC--KTIGTKPV-AHIDQFTADMLGSAELA-----EEVNLNGSG---------KLLK--ITGCAS- 381
Cdd:PTZ00114 292 fgdNRKDILQDIAVLTgaTVVSEDNVgLKLDDFDPSMLGSAKKVtvtkdETVILTGGGdkaeikervELLRsqIERTTSe 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 382 -------------PGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELALRL--TEYSRTLSGM 446
Cdd:PTZ00114 372 ydkeklkerlaklSGGVAVIKVGGASEVEVNEKKDRIEDALNATRAAVEE-GIVPGGGVALLRASKLLdkLEEDNELTPD 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1996390964 447 ESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRhaqGEKTAGINVRKGGISNILEELVVQPLLVSVSALTLAT 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 |
8.57e-16 |
|
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: 80.19 E-value: 8.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 41 AKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHP----AARMLVELSKAQDIEAGDGTTSVVIIAGSL 116
Cdd:cd03344 17 VNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLARAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 117 LDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVelSDRETLLNSATTSLNSkvvsqySSLLSPMSVNAVMKVID 196
Cdd:cd03344 97 IKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPV--KTKEEIAQVATISANG------DEEIGELIAEAMEKVGK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 197 PATATsvdlrdikiVKKLGGTIDDCELVEGLVLtqkvsNSGitrvekakigliqfCLSaPK--TDMDNQIVVSdyaqmdr 274
Cdd:cd03344 169 DGVIT---------VEEGKTLETELEVVEGMQF-----DRG--------------YLS-PYfvTDPEKMEVEL------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 275 vlreERAYIL------NLVKQI-------KKTGCNVLLIQKSILRDALSDLALHFL-NKMKIMVIK-----DiER----E 331
Cdd:cd03344 213 ----ENPYILltdkkiSSIQELlpilelvAKAGRPLLIIAEDVEGEALATLVVNKLrGGLKVCAVKapgfgD-RRkamlE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 332 DI------EFICKTIGTKpvahIDQFTADMLGSAELA-----EEVNLNGSGKLLKITG-CAS------------------ 381
Cdd:cd03344 288 DIailtggTVISEELGLK----LEDVTLEDLGRAKKVvvtkdDTTIIGGAGDKAAIKArIAQirkqieettsdydkeklq 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 382 ------PGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELALRLtEYSRTLSGMESYCVRAFA 455
Cdd:cd03344 364 erlaklSGGVAVIKVGGATEVELKEKKDRVEDALNATRAAVEE-GIVPGGGVALLRASPAL-DKLKALNGDEKLGIEIVR 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 456 DAMEVIPSTLAENAGLNP---ISTVTELRNRHaqgektaGINVRKGGISNILEELVVQPLLV---------SVSALTLAT 523
Cdd:cd03344 442 RALEAPLRQIAENAGVDGsvvVEKVLESPDGF-------GYDAATGEYVDMIEAGIIDPTKVvrsalqnaaSVASLLLTT 514
|
...
gi 1996390964 524 ETV 526
Cdd:cd03344 515 EAL 517
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
196-394 |
2.73e-15 |
|
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: 75.72 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 196 DPATATSVDLRD-IKIVKKLGGTIDDCELVEGLVLTQKVSNSGI-TRVEKAKIGLIQFCLsapktdmDNQIVVSDYAQMD 273
Cdd:cd03334 37 DVRAGDDMDIRQyVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMpSKIKNPRILLLQGPL-------EYQRVENKLLSLD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 274 RVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTKPVAHID-QFT 352
Cdd:cd03334 110 PVILQEKEYLKNLVSRIVALRPDVILVEKSV-----SRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDdLLT 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1996390964 353 ADMLGSAELAEE---VNLNGSGK-LLKITGCASPGKTvTIVVRGSN 394
Cdd:cd03334 185 SPKLGTCESFRVrtyVEEHGRSKtLMFFEGCPKELGC-TILLRGGD 229
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
32-526 |
1.12e-14 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 76.68 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 32 QIRFSNISAAK------AVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVEL-----SKAQDI 100
Cdd:PRK12850 5 EIRFSTDARDRllrgvnILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMvkevaSKTNDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 101 eAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVElsDRETLLNSATTSLNSKvvsqys 180
Cdd:PRK12850 85 -AGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVT--SSKEIAQVATISANGD------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 181 sllspmsvNAVMKVIdpatATSVDlrdikivkklggtiddcelveglvltqKVSNSGITRVEKAK-IGL-------IQFc 252
Cdd:PRK12850 156 --------ESIGEMI----AEAMD---------------------------KVGKEGVITVEEAKtLGTeldvvegMQF- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 253 lsapktdmDNQIV----VSDYAQMDRVLreERAYIL-------------NLVKQIKKTGCNVLLIQKSILRDALSDLALH 315
Cdd:PRK12850 196 --------DRGYLspyfVTNPEKMRAEL--EDPYILlhekkisnlqdllPILEAVVQSGRPLLIIAEDVEGEALATLVVN 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 316 FLNK-MKIMVIK--------DIEREDI------EFICKTIGTKpvahIDQFTADMLGSAE--LAEEVN---LNGSGKLLK 375
Cdd:PRK12850 266 KLRGgLKSVAVKapgfgdrrKAMLEDIavltggQVISEDLGIK----LENVTLDMLGRAKrvLITKENttiIDGAGDKKN 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 376 ITGCAS-------------------------PGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPEI 430
Cdd:PRK12850 342 IEARVKqiraqieettsdydreklqerlaklAGGVAVIRVGGATEVEVKEKKDRVDDALHATRAAVEE-GIVPGGGVALL 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 431 ElALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNP---ISTVTELRNRHaqgektaGINVRKGGISNILEEL 507
Cdd:PRK12850 421 R-ARSALRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGsvvVGKVAELPGNF-------GFNAQTGEYGDMVEAG 492
|
570 580
....*....|....*....|....*...
gi 1996390964 508 VVQPLLV---------SVSALTLATETV 526
Cdd:PRK12850 493 IIDPAKVtrtalqdaaSIAALLITTEAM 520
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
32-526 |
1.82e-14 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 75.93 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 32 QIRFSN------ISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHP----AARMLVELSKAQDIE 101
Cdd:PRK12851 5 EVKFHVearekmLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 102 AGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVElsDRETLLNSATTSLNSkvvsqyss 181
Cdd:PRK12851 85 AGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVT--TNAEIAQVATISANG-------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 182 llspmsvnavmkvidpatatsvdlrDIKIVKKLGGTIDdcelveglvltqKVSNSGITRVEKAKIGLIQFCLsAPKTDMD 261
Cdd:PRK12851 155 -------------------------DAEIGRLVAEAME------------KVGNEGVITVEESKTAETELEV-VEGMQFD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 262 NQIV----VSDYAQMDRVLreERAYIL-------------NLVKQIKKTGCNVLLIQKSILRDALSDLAlhfLNKM---- 320
Cdd:PRK12851 197 RGYLspyfVTDADKMEAEL--EDPYILihekkisnlqdllPVLEAVVQSGKPLLIIAEDVEGEALATLV---VNKLrggl 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 321 KIMVIK--------DIEREDI------EFICKTIGTKpvahIDQFTADMLGSAE--LAEEVN---LNGSGKLLKITGCAS 381
Cdd:PRK12851 272 KVAAVKapgfgdrrKAMLEDIailtggTVISEDLGIK----LENVTLEQLGRAKkvVVEKENttiIDGAGSKTEIEGRVA 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 382 -------------------------PGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELALRL 436
Cdd:PRK12851 348 qiraqieettsdydreklqerlaklAGGVAVIRVGASTEVEVKEKKDRVDDALHATRAAVEE-GIVPGGGVALLRAVKAL 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 437 TEySRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNrhaqGEKTAGINVRKGGISNILEELVVQPLLV-- 514
Cdd:PRK12851 427 DK-LETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLRE----KPGGYGFNAATNEYGDLYAQGVIDPVKVvr 501
|
570
....*....|....*....
gi 1996390964 515 -------SVSALTLATETV 526
Cdd:PRK12851 502 talqnaaSVAGLLLTTEAM 520
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
43-526 |
2.47e-14 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 75.61 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 43 AVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHP----AARMLVE-LSKAQDIeAGDGTTSVVIIAGSLL 117
Cdd:PRK12849 21 KLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEvASKTNDV-AGDGTTTATVLAQALV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 118 DSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVelSDRETLLNSATTSLNSKVvsqyssllspmsvnAVMKVIDP 197
Cdd:PRK12849 100 QEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPV--SGSEEIAQVATISANGDE--------------EIGELIAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 198 ATATsVDLRDIKIVKKLGGTIDDCELVEGLVLtqkvsNSG------ITRVEKakigliqfclsapktdmdnqivvsdyaq 271
Cdd:PRK12849 164 AMEK-VGKDGVITVEESKTLETELEVTEGMQF-----DRGylspyfVTDPER---------------------------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 272 MDRVLreERAYIL-------------NLVKQIKKTGCNVLLIQKSILRDALSDLalhFLNKM----KIMVIKDI---ER- 330
Cdd:PRK12849 210 MEAVL--EDPLILltdkkisslqdllPLLEKVAQSGKPLLIIAEDVEGEALATL---VVNKLrgglKVAAVKAPgfgDRr 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 331 ----EDI------EFICKTIGTKpvahIDQFTADMLGSAElaeevnlngsgkllKITgcasPGKTVTIVVRGSN------ 394
Cdd:PRK12849 285 kamlEDIailtggTVISEDLGLK----LEEVTLDDLGRAK--------------RVT----ITKDNTTIVDGAGdkeaie 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 395 ------KLVIEEA----------ER--------------------------SIHDALCVIRCLVKKrALIAGGGAPEIEL 432
Cdd:PRK12849 343 arvaqiRRQIEETtsdydreklqERlaklaggvavikvgaatevelkerkdRVEDALNATRAAVEE-GIVPGGGVALLRA 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 433 ALRLTEYsRTLSGMESYCVRAFADAMEVIPSTLAENAGLNP---ISTVTELRNRHaqgektaGINVRKGGISNILEELVV 509
Cdd:PRK12849 422 AKALDEL-AGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGsvvVAKVLELEDGF-------GFNAATGEYGDLIAAGII 493
|
570 580
....*....|....*....|....*.
gi 1996390964 510 QPLLV---------SVSALTLATETV 526
Cdd:PRK12849 494 DPVKVtrsalqnaaSVAGLLLTTEAL 519
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
30-173 |
3.49e-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: 75.02 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 30 PAQIRFSNISAAK------AVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVEL-----SKAQ 98
Cdd:TIGR02348 1 AKQIKFDEEARKAllrgvdKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLvkevaSKTN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1996390964 99 DIeAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVElsDRETLLNSATTSLNS 173
Cdd:TIGR02348 81 DV-AGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVK--GKKEIAQVATISANN 152
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
24-530 |
6.67e-12 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 67.82 E-value: 6.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 24 YQDRDKPAQIRFSNIsaakaVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVEL-----SKAQ 98
Cdd:CHL00093 7 YQDNARRALERGMDI-----LAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALirqaaSKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 99 DIeAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVElsDRETLLNSATTSL-NSKVVS 177
Cdd:CHL00093 82 DV-AGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVE--DIQAITQVASISAgNDEEVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 178 QyssllspMSVNAVMKVidpatatsvdLRDIKIVKKLG-GTIDDCELVEGLvltqkvsnsgitRVEKAKIgliqfclsap 256
Cdd:CHL00093 159 S-------MIADAIEKV----------GREGVISLEEGkSTVTELEITEGM------------RFEKGFI---------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 257 ktdmdNQIVVSDYAQMDRVLreERAYIL------NLVKQ--------IKKTGCNVLLIQKSILRDALSDLalhFLNKMKI 322
Cdd:CHL00093 200 -----SPYFVTDTERMEVVQ--ENPYILltdkkiTLVQQdllpileqVTKTKRPLLIIAEDVEKEALATL---VLNKLRG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 323 MV---------IKDIEREDIEFICKTIGTKPVAH-----IDQFTADMLGSA--------------------------ELA 362
Cdd:CHL00093 270 IVnvvavrapgFGDRRKAMLEDIAILTGGQVITEdaglsLETIQLDLLGQArriivtkdsttiiadgneeqvkarceQLR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 363 EEVNLNGSG--------KLLKITGcaspGKTVtIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELAL 434
Cdd:CHL00093 350 KQIEIADSSyekeklqeRLAKLSG----GVAV-IKVGAATETEMKDKKLRLEDAINATKAAVEE-GIVPGGGATLVHLSE 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 435 RLTEYSRT-LSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRhaqgEKTAGINVRKGGISNILEELVVQPLL 513
Cdd:CHL00093 424 NLKTWAKNnLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQ----DFEIGYNAANNKFVNMYEAGIIDPAK 499
|
570
....*....|....*..
gi 1996390964 514 VSVSALTLATETVRSIL 530
Cdd:CHL00093 500 VTRSALQNAASIASMIL 516
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
43-173 |
2.58e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 65.92 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 43 AVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVEL-----SKAQDIeAGDGTTSVVIIAGSLL 117
Cdd:PRK00013 21 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLvkevaSKTNDV-AGDGTTTATVLAQAIV 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1996390964 118 DSCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVElsDRETLLNSATTSLNS 173
Cdd:PRK00013 100 REGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVE--DKEEIAQVATISANG 153
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
44-524 |
3.95e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 65.64 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 44 VADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVL----HPAARMLVEL-SKAQDIeAGDGTTSVVIIAGSLLD 118
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVaSKTNDL-AGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 119 SCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELSdrETLLNSATTSLNSkvvsqySSLLSPMSVNAVMKVIDPA 198
Cdd:PRK12852 102 EGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASS--AEIAQVGTISANG------DAAIGKMIAQAMQKVGNEG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 199 TATSVDLRDIKIvkklggtidDCELVEGLVLTQK-VSNSGITRVEKAKIGLiqfclsapktdMDNQIVVSdyaqmDRVLR 277
Cdd:PRK12852 174 VITVEENKSLET---------EVDIVEGMKFDRGyLSPYFVTNAEKMTVEL-----------DDAYILLH-----EKKLS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 278 EERAyILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNK-MKIMVIK-----DIER---EDI------EFICKTIGT 342
Cdd:PRK12852 229 GLQA-MLPVLEAVVQSGKPLLIIAEDVEGEALATLVVNRLRGgLKVAAVKapgfgDRRKamlEDIailtggQLISEDLGI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 343 KpvahIDQFTADMLGSAE--LAEEVN---LNGSGKLLKITGCAS-------------------------PGKTVTIVVRG 392
Cdd:PRK12852 308 K----LENVTLKMLGRAKkvVIDKENttiVNGAGKKADIEARVGqikaqieettsdydreklqerlaklAGGVAVIRVGG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 393 SNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPeielALRLTEYSRTLSGMES---YCVRAFADAMEVIPSTLAENA 469
Cdd:PRK12852 384 ATEVEVKEKKDRVEDALNATRAAVQE-GIVPGGGVA----LLRAKKAVGRINNDNAdvqAGINIVLKALEAPIRQIAENA 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1996390964 470 GLNPISTVTELRNRHAQgekTAGINVRKGGISNILEELVVQPLLV---------SVSALTLATE 524
Cdd:PRK12852 459 GVEGSIVVGKILENKSE---TFGFDAQTEEYVDMVAKGIIDPAKVvrtalqdaaSVAGLLVTTE 519
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
44-159 |
3.88e-10 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 62.25 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 44 VADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVEL-----SKAQDIeAGDGTTSVVIIAGSLLD 118
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLvrqaaAKTNDL-AGDGTTTSVVLAQGLIA 156
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1996390964 119 SCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVELSD 159
Cdd:PLN03167 157 EGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE 197
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
44-526 |
2.45e-09 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 59.66 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 44 VADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQV----LHPAARMLVEL-SKAQDIeAGDGTTSVVIIAGSLLD 118
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVaSKSADA-AGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 119 SCTKLLQKGIHPTIISESFQKALEKGIEILTDMSRPVelSDRETLLNSATTSLNSKvvSQYSSLLSpmsvNAVMKVIDPA 198
Cdd:PRK14104 102 EGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKV--TSNDEIAQVGTISANGD--AEIGKFLA----DAMKKVGNEG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 199 TATSVDLRDIKIvkklggtidDCELVEGLVLTQK-VSNSGITRVEKAKIgliqfclsapktDMDNQIVVSDYAQMDRvLR 277
Cdd:PRK14104 174 VITVEEAKSLET---------ELDVVEGMQFDRGyISPYFVTNADKMRV------------EMDDAYILINEKKLSS-LN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 278 EerayILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFL-NKMKIMVIK-----DIEREDIEFICKTIGTKPVAH---- 347
Cdd:PRK14104 232 E----LLPLLEAVVQTGKPLVIVAEDVEGEALATLVVNRLrGGLKVAAVKapgfgDRRKAMLQDIAILTGGQAISEdlgi 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 348 -IDQFTADMLGSAE--LAEEVN---LNGSGKLLKITGCAS-------------------------PGKTVTIVVRGSNKL 396
Cdd:PRK14104 308 kLENVTLQMLGRAKkvMIDKENttiVNGAGKKADIEARVAqikaqieettsdydreklqerlaklAGGVAVIRVGGATEV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1996390964 397 VIEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELALRLTEYsRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPIST 476
Cdd:PRK14104 388 EVKERKDRVDDAMHATRAAVEE-GIVPGGGVALLRASEQLKGI-KTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVI 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1996390964 477 VTELRNRHaqgEKTAGINVRKGGISNILEELVVQPLLV---------SVSALTLATETV 526
Cdd:PRK14104 466 VGKILEKE---QYSYGFDSQTGEYGNLVSKGIIDPTKVvrtaiqnaaSVAALLITTEAM 521
|
|
| |
