|
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: 980.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 25 QDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGD 104
Cdd:cd03338 1 TDKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 105 GTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:cd03338 81 GTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 185 PMSVNAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANS--GITRVEKAKIGLIQFCLSAPKTDMDN 262
Cdd:cd03338 161 PIAVDAVLKVIDPATATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKagGPTRIEKAKIGLIQFCLSPPKTDMDN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 263 QIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNKMKIMVVKDIEREDIEFICKTIGT 342
Cdd:cd03338 241 NIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQKSILRDAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 343 KPVAHIDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALI 422
Cdd:cd03338 321 KPVASIDHFTEDKLGSADLVEEVSL-GDGKIVKITGVKNPGKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 423 AGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISN 502
Cdd:cd03338 400 PGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITN 479
|
490 500 510
....*....|....*....|....*....|....*.
gi 33414505 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: 923.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 24 YQDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAG 103
Cdd:TIGR02342 1 FQDKDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 104 DGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLL 183
Cdd:TIGR02342 81 DGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 184 SPMSVNAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKV--ANSGITRVEKAKIGLIQFCLSAPKTDMD 261
Cdd:TIGR02342 161 APLAVDAVLKVIDPENAKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKAskSAGGPTRIEKAKIGLIQFQISPPKTDME 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 262 NQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNKMKIMVVKDIEREDIEFICKTIG 341
Cdd:TIGR02342 241 NQIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSILRDAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 342 TKPVAHIDQFTPDMLGSAELAEEVSLNGsGKLFKITGCTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRAL 421
Cdd:TIGR02342 321 CKPIASIDHFTADKLGSAELVEEVDSDG-GKIIKITGIQNAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 422 IAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGIS 501
Cdd:TIGR02342 400 IAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGIT 479
|
490 500 510
....*....|....*....|....*....|....*...
gi 33414505 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: 588.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 26 DRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDG 105
Cdd:cd00309 2 EREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 106 TTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLSP 185
Cdd:cd00309 82 TTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 186 MSVNAVMKVIDPATatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSG-ITRVEKAKIGLIQFCLSapktdmdnqi 264
Cdd:cd00309 162 LVVDAVLKVGKENG--DVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYmPKRLENAKILLLDCKLE---------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 265 vvsdyaqmdrvlreerayilnlvkqikktgcNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKP 344
Cdd:cd00309 230 -------------------------------YVVIAEKGI-----DDEALHYLAKLGIMAVRRVRKEDLERIAKATGATI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 345 VAHIDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSpGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAG 424
Cdd:cd00309 274 VSRLEDLTPEDLGTAGLVEETKI-GDEKYTFIEGCKG-GKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 425 GGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNIL 504
Cdd:cd00309 352 GGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMK 431
|
490 500 510
....*....|....*....|....*....|..
gi 33414505 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: 562.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 44 VADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSLLDSCTKL 123
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 124 LQKGIHPTIISESFQKALEKGLEILTDM-SRPVQLSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVidPATATS 202
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAI--PKNDGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 203 VDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSG-ITRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDRVLREERA 281
Cdd:pfam00118 159 FDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDmPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 282 YILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHIDQFTPDMLGSAEL 361
Cdd:pfam00118 239 QILEIVEKIIDSGVNVVVCQKGI-----DDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 362 AEEVSLnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELALRLTEYSR 441
Cdd:pfam00118 314 VEEEKI-GDEKYTFIEGCKSP-KAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 442 TLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEMVVQPLLVSVSALTL 521
Cdd:pfam00118 392 SVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
|
490
....*....|....*...
gi 33414505 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: 550.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:NF041082 21 NNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 116 LLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVI 195
Cdd:NF041082 101 LLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVKAVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 196 DPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDR 274
Cdd:NF041082 181 EKDGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMpKRVENAKIALLDAPLEVKKTEIDAKISITDPDQLQA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 275 VLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHIDQFTPD 354
Cdd:NF041082 261 FLDQEEKMLKEMVDKIADSGANVVFCQKGI-----DDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSIDDLSPE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 355 MLGSAELAEEVSLNGSGKLFkITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELAL 434
Cdd:NF041082 336 DLGYAGLVEERKVGGDKMIF-VEGCKNP-KAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEVELAL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 435 RLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEMVVQPLLV 514
Cdd:NF041082 414 RLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVVEPLRV 493
|
490 500
....*....|....*....|..
gi 33414505 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: 538.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:cd03343 19 MNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 116 LLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVI 195
Cdd:cd03343 99 LLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAEAAKDKLADLVVDAVLQVA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 196 DPAT-ATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMD 273
Cdd:cd03343 179 EKRDgKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMpKRVENAKIALLDAPLEVKKTEIDAKIRITSPDQLQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 274 RVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHIDQFTP 353
Cdd:cd03343 259 AFLEQEEAMLKEMVDKIADTGANVVFCQKGI-----DDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTNIDDLTP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 354 DMLGSAELAEEVSLNGSGKLFkITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELA 433
Cdd:cd03343 334 EDLGEAELVEERKVGDDKMVF-VEGCKNP-KAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGAVEIELA 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 434 LRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEMVVQPLL 513
Cdd:cd03343 412 KRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVDMLEKGVIEPLR 491
|
490 500
....*....|....*....|...
gi 33414505 514 VSVSALTLATETVRSILKIDDVV 536
Cdd:cd03343 492 VKKQAIKSATEAATMILRIDDVI 514
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
22-539 |
0e+00 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 521.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 22 GAYQDRDKPAQirFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIE 101
Cdd:NF041083 9 GTQRTKGRDAQ--RNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 102 AGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSS 181
Cdd:NF041083 87 VGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKGVEEARD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 182 LLSPMSVNAVMKVIDPATAT-SVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTD 259
Cdd:NF041083 167 YLAEIAVKAVKQVAEKRDGKyYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMpKRVENAKIALLDAPLEVKKTE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 260 MDNQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKT 339
Cdd:NF041083 247 IDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGI-----DDLAQHYLAKAGILAVRRVKKSDMEKLAKA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 340 IGTKPVAHIDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKR 419
Cdd:NF041083 322 TGARIVTNIDDLTPEDLGYAELVEERKV-GDDKMVFVEGCKNP-KAVTILIRGGTEHVVDEAERALEDALSVVADAVEDG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 420 ALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGG 499
Cdd:NF041083 400 KIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGE 479
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 33414505 500 ISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVVNTR 539
Cdd:NF041083 480 VVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
36-536 |
3.43e-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: 509.61 E-value: 3.43e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:TIGR02339 20 NNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 116 LLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYS-SLLSPMSVNAVMKV 194
Cdd:TIGR02339 100 LLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSKASAEVAkDKLADLVVEAVKQV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 195 IDPATATS--VDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQ 271
Cdd:TIGR02339 180 AELRGDGKyyVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMpKRVENAKIALLDAPLEVEKTEIDAKIRITDPDQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 272 MDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHIDQF 351
Cdd:TIGR02339 260 IKKFLDQEEAMLKEMVDKIASAGANVVICQKGI-----DDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVSSIDEI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 352 TPDMLGSAELAEEVSLnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIE 431
Cdd:TIGR02339 335 TESDLGYAELVEERKV-GEDKMVFVEGCKNP-KAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVAGGGAVEIE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 432 LALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEMVVQP 511
Cdd:TIGR02339 413 LALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTGEIEDMLELGVIEP 492
|
490 500
....*....|....*....|....*
gi 33414505 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 |
4.47e-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: 435.57 E-value: 4.47e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:cd03339 27 SHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 116 LLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSR--PVQLSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMK 193
Cdd:cd03339 107 LLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADkiEFSPDNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAVLS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 194 VIDpATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITR-VEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQM 272
Cdd:cd03339 187 VAD-LERKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKeVKDAKIAILTCPFEPPKPKTKHKLDITSVEDY 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 273 DRVLREERAYILNLVKQIKKTGCNVLLIQKsilrdALSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHIDQFT 352
Cdd:cd03339 266 KKLQEYEQKYFREMVEQVKDAGANLVICQW-----GFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFEDLS 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 353 PDMLGSAELAEEVSLNGS-GKLFKITGCtSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIE 431
Cdd:cd03339 341 PEKLGKAGLVREISFGTTkDKMLVIEGC-PNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGGGAAEIS 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 432 LALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRH-AQGEKTTGINVRKGGISNILEEMVVQ 510
Cdd:cd03339 420 CSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPHLGIDCLGRGTNDMKEQKVFE 499
|
490 500
....*....|....*....|....*.
gi 33414505 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 |
2.02e-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: 388.01 E-value: 2.02e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 27 RDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGT 106
Cdd:TIGR02343 22 RLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 107 TSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPV--QLSDRETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:TIGR02343 102 TGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEIsaDNNNREPLIQAAKTSLGSKIVSKCHRRFA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 185 PMSVNAVMKVIDpATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITR-VEKAKIGLIQFCLSAPKTDMDNQ 263
Cdd:TIGR02343 182 EIAVDAVLNVAD-MERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKeVEDAKIAILTCPFEPPKPKTKHK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 264 IVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKsilrdALSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTK 343
Cdd:TIGR02343 261 LDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQW-----GFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 344 PVAHIDQFTPDMLGSAELAEEVSLNGSG-KLFKITGCTSpGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALI 422
Cdd:TIGR02343 336 IVPRFQELSKDKLGKAGLVREISFGTTKdRMLVIEQCKN-SKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 423 AGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRH-AQGEKTTGINVRKGGIS 501
Cdd:TIGR02343 415 YGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQlKEKNPNLGVDCLGYGTN 494
|
490 500 510
....*....|....*....|....*....|....*
gi 33414505 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 |
7.91e-129 |
|
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: 385.87 E-value: 7.91e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:cd03340 20 SNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 116 LLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSD----RETLLNSATTSLNSKVVSQYSSLLSPMSVNAV 191
Cdd:cd03340 100 FLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDkeeqRELLEKCAATALNSKLIASEKEFFAKMVVDAV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 192 MKVIDpatatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI----TRVEKAKIGLIQFCLSApKTDMDN-QIVV 266
Cdd:cd03340 180 LSLDD-----DLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAGFeqqpKKFKNPKILLLNVELEL-KAEKDNaEVRV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 267 SDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVA 346
Cdd:cd03340 254 EDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPI-----GDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 347 HIDQFTPDMLGSAELAEEVSLngSGKLFKI-TGCTSpGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGG 425
Cdd:cd03340 329 TVSNITDDVLGTCGLFEERQV--GGERYNIfTGCPK-AKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 426 GAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKT-TGINVRKGGISNIL 504
Cdd:cd03340 406 GAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKwYGVDINNEGIADNF 485
|
490 500 510
....*....|....*....|....*....|..
gi 33414505 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 |
1.08e-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: 373.16 E-value: 1.08e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 26 DRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDG 105
Cdd:cd03335 2 ERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 106 TTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTD-MSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDNLGKESLINVAKTSMSSKIIGADSDFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 185 PMSVNAVM--KVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMD 261
Cdd:cd03335 162 NMVVDAILavKTTNEKGKTKYPIKAVNILKAHGKSAKESYLVNGYALNCTRASQGMpTRVKNAKIACLDFNLQKTKMKLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 262 NQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIG 341
Cdd:cd03335 242 VQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGI-----DDMCLKYFVEAGAMAVRRVKKEDLRRIAKATG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 342 TKPVAHI------DQFTPDMLGSAELAEEVSLnGSGKLFKITGCtSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCL 415
Cdd:cd03335 317 ATLVSTLanlegeETFDPSYLGEAEEVVQERI-GDDELILIKGT-KKRSSASIILRGANDFMLDEMERSLHDALCVVKRT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 416 VKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHA--------QG 487
Cdd:cd03335 395 LESNSVVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAaaqvkpdkKH 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 33414505 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 |
4.16e-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: 367.39 E-value: 4.16e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 27 RDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGT 106
Cdd:cd03337 11 RESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 107 TSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLSPM 186
Cdd:cd03337 91 TSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFVSRWSDLMCNL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 187 SVNAVMKVI--DPATATSVDL-RDIKIVKKLGGTIDDCELVEGLVLtqkvansgitrvekakigliqfclsapktdmdNQ 263
Cdd:cd03337 171 ALDAVKTVAveENGRKKEIDIkRYAKVEKIPGGEIEDSRVLDGVML--------------------------------NK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 264 IVVsdYAQMDRVLREERAYILNlvkqikktgCNVLLIqkSILRDALSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTK 343
Cdd:cd03337 219 DVT--HPKMRRRIENPRIVLLD---------CPLEYL--VITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARACGAT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 344 PVAHIDQFTPDMLGSAELAEEVSLNGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIA 423
Cdd:cd03337 286 IVNRPEELTESDVGTGAGLFEVKKIGDEYFTFITECKDP-KACTILLRGASKDVLNEVERNLQDAMAVARNIILNPKLVP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 424 GGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEK-TTGINVRKGGISN 502
Cdd:cd03337 365 GGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENsTWGIDGETGDIVD 444
|
490 500 510
....*....|....*....|....*....|....
gi 33414505 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 |
2.16e-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: 364.81 E-value: 2.16e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 26 DRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDG 105
Cdd:TIGR02340 6 ERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 106 TTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTD-MSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDELGREALINVAKTSMSSKIIGLDSDFFS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 185 PMSVNAVM--KVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMD 261
Cdd:TIGR02340 166 NIVVDAVLavKTTNENGETKYPIKAINILKAHGKSARESMLVKGYALNCTVASQQMpKRIKNAKIACLDFNLQKAKMALG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 262 NQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIG 341
Cdd:TIGR02340 246 VQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGI-----DDMCLKYFVEAGAMGVRRCKKEDLKRIAKATG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 342 TKPVAHI------DQFTPDMLGSAELAEEVSLnGSGKLFKITGcTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCL 415
Cdd:TIGR02340 321 ATLVSTLadlegeETFEASYLGFADEVVQERI-ADDECILIKG-TKKRKSASIILRGANDFMLDEMERSLHDALCVVKRT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 416 VKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHA--------QG 487
Cdd:TIGR02340 399 LESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAaaqlkpekKH 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 33414505 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 |
8.36e-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: 360.23 E-value: 8.36e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 36 SNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGS 115
Cdd:TIGR02345 22 SNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 116 LLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSD---RETLLNSATTSLNSKVVSQYSSLLSPMSVNAVM 192
Cdd:TIGR02345 102 LLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqRELLEKCAATALSSKLISHNKEFFSKMIVDAVL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 193 KVIDPAtatsVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI----TRVEKAKIGLIQFCLSApKTDMDN-QIVVS 267
Cdd:TIGR02345 182 SLDRDD----LDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAGFeqqpKKFANPKILLLNVELEL-KAEKDNaEIRVE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 268 DYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAH 347
Cdd:TIGR02345 257 DVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPI-----GDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQST 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 348 IDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSpGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGA 427
Cdd:TIGR02345 332 TSDLEADVLGTCALFEERQI-GSERYNYFTGCPH-AKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 428 PEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEM 507
Cdd:TIGR02345 410 IEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFEAF 489
|
490 500
....*....|....*....|....*....
gi 33414505 508 VVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:TIGR02345 490 VWEPALVKINALKAAFEAACTILSVDETI 518
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
35-536 |
2.47e-115 |
|
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: 349.60 E-value: 2.47e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 35 FSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAG 114
Cdd:cd03341 11 LRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 115 SLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMS--RPVQLSDRETLLNSATTSLNSKVVSqYSSLLSPMSVNAVM 192
Cdd:cd03341 91 ELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVvyKIEDLRNKEEVSKALKTAIASKQYG-NEDFLSPLVAEACI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 193 KVIdPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSgITRVEKAKIGLiqfclsapktdmdnqivvsdyaqm 272
Cdd:cd03341 170 SVL-PENIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKREPEGS-VKRVKKAKVAV------------------------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 273 drvlreeraYILNLvkqikKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHIDQFT 352
Cdd:cd03341 224 ---------FSCPF-----DIGVNVIVAGGSV-----GDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 353 PDMLGSAELAEEVSLnGSGKLFKITGCTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIEL 432
Cdd:cd03341 285 PEEIGYCDSVYVEEI-GDTKVVVFRQNKEDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIEL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 433 ALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKG--GISNILEEMVVQ 510
Cdd:cd03341 364 AKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGdeGTKDAKEAGIFD 443
|
490 500
....*....|....*....|....*.
gi 33414505 511 PLLVSVSALTLATETVRSILKIDDVV 536
Cdd:cd03341 444 HLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
22-536 |
2.77e-115 |
|
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: 351.25 E-value: 2.77e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 22 GAYQDRDKPAqiRFSNISAAKAVADAIRTSLGPKGMDKMIQDG--KGDVTITNDGATILKQMQVLHPAARMLVELSKAQD 99
Cdd:cd03336 5 GAQEEKGETA--RLSSFVGAIAIGDLVKTTLGPKGMDKILQSVgrSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 100 IEAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSD---RETLLNSATTSLNSKVV 176
Cdd:cd03336 83 DEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEeafREDLLNIARTTLSSKIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 177 SQYSSLLSPMSVNAVMKVIDpatatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITRVEKAKIgLIQfclsap 256
Cdd:cd03336 163 TQDKEHFAELAVDAVLRLKG-----SGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQPKRIENAKI-LIA------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 257 KTDMDN--------QIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLliqksILRDALSDLALHFLNKMKIMVVKDI 328
Cdd:cd03336 231 NTPMDTdkikifgaKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCF-----INRQLIYNYPEQLFADAGIMAIEHA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 329 EREDIEFICKTIGTKPVAHIDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSpGKTVTIVVRGSNKLVIEEAERSIHDA 408
Cdd:cd03336 306 DFDGVERLALVTGGEIASTFDHPELVKLGTCKLIEEIMI-GEDKLIRFSGVAA-GEACTIVLRGASQQILDEAERSLHDA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 409 LCVIRCLVKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGE 488
Cdd:cd03336 384 LCVLAQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGN 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 33414505 489 KTTGINVRKGGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:cd03336 464 TTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDII 511
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
34-536 |
1.02e-112 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 343.60 E-value: 1.02e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 34 RFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHP----AARMLVELSKAQDIEAGDGTTSV 109
Cdd:COG0459 12 RRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTTTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 110 VIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNSKvvsqysSLLSPMSVN 189
Cdd:COG0459 92 TVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPV--DDKEELAQVATISANGD------EEIGELIAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 190 AVMKVIDPATATsvdlrdikiVKKLGGTIDDCELVEGLVLTQKVANSGItrvekakigliqfclsapktdmdnqivVSDY 269
Cdd:COG0459 164 AMEKVGKDGVIT---------VEEGKGLETELEVVEGMQFDKGYLSPYF---------------------------VTDP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 270 AQMDRVLreERAYIL-------------NLVKQIKKTGCNVLLIQKSIlrdalSDLALHFL--NKM----KIMVVK---- 326
Cdd:COG0459 208 EKMPAEL--ENAYILltdkkissiqdllPLLEKVAQSGKPLLIIAEDI-----DGEALATLvvNGIrgvlRVVAVKapgf 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 327 -DIEREDIEFICKTIGTKPVAH-----IDQFTPDMLGSAELAEEvslnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEE 400
Cdd:COG0459 281 gDRRKAMLEDIAILTGGRVISEdlglkLEDVTLDDLGRAKRVEV----DKDNTTIVEGAGNP-KAIVILVGAATEVEVKE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 401 AERSIHDALCVIRCLVKKRaLIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTEL 480
Cdd:COG0459 356 RKRRVEDALHATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKV 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 33414505 481 RnrhAQGEKTTGINVRKGGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:COG0459 435 R---AAKDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVI 487
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
37-536 |
2.76e-112 |
|
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: 344.01 E-value: 2.76e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 37 NISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSL 116
Cdd:TIGR02346 23 NIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 117 LDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMS--RPVQLSDRETLLNSATTSLNSKVVSQYSsLLSPMSVNAVMKV 194
Cdd:TIGR02346 103 LNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVvwEVKDLRDKDELIKALKASISSKQYGNED-FLAQLVAQACSTV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 195 IdPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKvANSGITRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDR 274
Cdd:TIGR02346 182 L-PKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNRE-AEGSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNAEELLN 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 275 VLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHIDQFTPD 354
Cdd:TIGR02346 260 YSKGEENQIEAMIKAIADSGVNVIVTGGSV-----GDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 355 MLGSAELAEeVSLNGSGKLFKITGCTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELAL 434
Cdd:TIGR02346 335 EIGYVDSVY-VSEIGGDKVTVFKQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELAS 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 435 RLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKG--GISNILEEMVVQPL 512
Cdd:TIGR02346 414 RLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAEsdGVKDASEAGIYDML 493
|
490 500
....*....|....*....|....
gi 33414505 513 LVSVSALTLATETVRSILKIDDVV 536
Cdd:TIGR02346 494 ATKKWAIKLATEAAVTVLRVDQII 517
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
22-536 |
4.68e-112 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 343.16 E-value: 4.68e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 22 GAYQDRDKPAqiRFSNISAAKAVADAIRTSLGPKGMDKMIQ-----DGKGDVTITNDGATILKQMQVLHPAARMLVELSK 96
Cdd:PTZ00212 14 GAQEEKGETA--RLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPAAKILVDISK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 97 AQDIEAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSD---RETLLNSATTSLNS 173
Cdd:PTZ00212 92 TQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEekfKEDLLNIARTTLSS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 174 KVVSQYSSLLSPMSVNAVMKVIDpatatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITRVEKAKIgliqfcL 253
Cdd:PTZ00212 172 KLLTVEKDHFAKLAVDAVLRLKG-----SGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVGQPKRLENCKI------L 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 254 SApKTDMDN--------QIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLliqksILRDALSDLALHFLNKMKIMVV 325
Cdd:PTZ00212 241 VA-NTPMDTdkikiygaKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVF-----INRQLIYNYPEQLFAEAGIMAI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 326 KDIEREDIEFICKTIGTKPVAHIDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSpGKTVTIVVRGSNKLVIEEAERSI 405
Cdd:PTZ00212 315 EHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMI-GEDKLIRFSGCAK-GEACTIVLRGASTHILDEAERSL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 406 HDALCVIRCLVKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHA 485
Cdd:PTZ00212 393 HDALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHY 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 33414505 486 QGEKTTGINVRKGGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:PTZ00212 473 KGNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDII 523
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
25-536 |
2.36e-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: 341.33 E-value: 2.36e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 25 QDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGD 104
Cdd:TIGR02344 9 TKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 105 GTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLS 184
Cdd:TIGR02344 89 GTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFVSRWSDLMC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 185 PMSVNAVMKV-IDPATATSVDL-RDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITR-VEKAKIGLIQFCLSAPKTDMD 261
Cdd:TIGR02344 169 DLALDAVRTVqRDENGRKEIDIkRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRyIENPRIVLLDCPLEYKKGESQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 262 NQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIG 341
Cdd:TIGR02344 249 TNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGV-----SDLAQHYLLKANITAIRRVRKTDNNRIARACG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 342 TKPVAHIDQFTPDMLGSAELAEEVSLNGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRAL 421
Cdd:TIGR02344 324 ATIVNRPEELRESDVGTGCGLFEVKKIGDEYFTFITECKDP-KACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 422 IAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEK-TTGINVRKGGI 500
Cdd:TIGR02344 403 VPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNcTWGIDGETGKI 482
|
490 500 510
....*....|....*....|....*....|....*.
gi 33414505 501 SNILEEMVVQPLLVSVSALTLATETVRSILKIDDVV 536
Cdd:TIGR02344 483 VDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
37-536 |
1.40e-88 |
|
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: 281.07 E-value: 1.40e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 37 NISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSL 116
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 117 LDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQ-LSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVI 195
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEiDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 196 DPatATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSdyaqmdr 274
Cdd:cd03342 177 KP--DEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMpKRVENAYILTCNVSLEYEKTEVNSGFFYS------- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 275 vlreerayilnlvkqikktgcnVLLIQKSIlrDALSdlaLHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHIDQFTPD 354
Cdd:cd03342 248 ----------------------VVINQKGI--DPPS---LDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 355 MLGSAELAEEVSLnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELAL 434
Cdd:cd03342 301 CLGYAGLVYERTL-GEEKYTFIEGVKNP-KSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 435 RLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEMVVQPLLV 514
Cdd:cd03342 379 HLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSV 458
|
490 500
....*....|....*....|..
gi 33414505 515 SVSALTLATETVRSILKIDDVV 536
Cdd:cd03342 459 KRQILHSATVIASQLLLVDEII 480
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
20-539 |
4.70e-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: 280.59 E-value: 4.70e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 20 GKGAYQDRDKPAqiRFSNISAAKAVADAIRTSLGPKGMDKMIQDG--KGDVTITNDGATILKQMQVLHPAARMLVELSKA 97
Cdd:TIGR02341 4 KDGADEERAENA--RLSSFVGAIAIGDLVKSTLGPKGMDKILQSSssDASIMVTNDGATILKSIGVDNPAAKVLVDMSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 98 QDIEAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSrpVQLSD-----RETLLNSATTSLN 172
Cdd:TIGR02341 82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSA--VDNGSdevkfRQDLMNIARTTLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 173 SKVVSQYSSLLSPMSVNAVMKVidpatATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITRVEKAKIGLIQFC 252
Cdd:TIGR02341 160 SKILSQHKDHFAQLAVDAVLRL-----KGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 253 LSAPKTDM-DNQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLliqksILRDALSDLALHFLNKMKIMVVKDIERE 331
Cdd:TIGR02341 235 MDTDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCF-----INRQLIYNYPEQLFADAGVMAIEHADFE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 332 DIEFICKTIGTKPVAHIDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSpGKTVTIVVRGSNKLVIEEAERSIHDALCV 411
Cdd:TIGR02341 310 GVERLALVTGGEIVSTFDHPELVKLGSCDLIEEIMI-GEDKLLKFSGVKL-GEACTIVLRGATQQILDEAERSLHDALCV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 412 IRCLVKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTT 491
Cdd:TIGR02341 388 LSQTVKESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTM 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 33414505 492 GINVRKGGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVVNTR 539
Cdd:TIGR02341 468 GLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAA 515
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
37-536 |
2.71e-83 |
|
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: 268.53 E-value: 2.71e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 37 NISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSL 116
Cdd:TIGR02347 21 NINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 117 LDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLS-DRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVI 195
Cdd:TIGR02347 101 LKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEvDREFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 196 DPATAtsVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDR 274
Cdd:TIGR02347 181 KDGED--IDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMpRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQREK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 275 VLREERAYILNLVKQI---KKTGCN-------VLLIQKSIlrDALSdlaLHFLNKMKIMVVKDIEREDIEFICKTIGTKP 344
Cdd:TIGR02347 259 LVKAERKFVDDRVKKIielKKKVCGkspdkgfVVINQKGI--DPPS---LDLLAKEGIMALRRAKRRNMERLTLACGGEA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 345 VAHIDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSPgKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAG 424
Cdd:TIGR02347 334 LNSVEDLTPECLGWAGLVYETTI-GEEKYTFIEECKNP-KSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPG 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 425 GGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNIL 504
Cdd:TIGR02347 412 AGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGVDLNTGEPIDPE 491
|
490 500 510
....*....|....*....|....*....|..
gi 33414505 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 |
1.87e-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: 208.86 E-value: 1.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 160 RETLLNSATTSLNSKVvSQYSSLLSPMSVNAVMKVIDPATatSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSG-I 238
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNR--MDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYmP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 239 TRVEKAKIGLIQFCLSapktdmdnqivvsdyaqmdrvlreerayilnlvkqikktgcNVLLIQKSIlrdalSDLALHFLN 318
Cdd:cd03333 78 KRLENAKILLLDCPLE-----------------------------------------YVVIAEKGI-----DDLALHYLA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 319 KMKIMVVKDIEREDIEFICKTIGTKPVAHIDQFTPDMLGSAELAEEVSLnGSGKLFKITGCTSpGKTVTIVVRGSNKLVI 398
Cdd:cd03333 112 KAGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKI-GEEKLTFIEGCKG-GKAATILLRGATEVEL 189
|
250
....*....|....*....
gi 33414505 399 EEAERSIHDALCVIRCLVK 417
Cdd:cd03333 190 DEVKRSLHDALCAVRAAVE 208
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
33-523 |
6.43e-23 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 102.30 E-value: 6.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 33 IRFSN------ISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQM----QVLHPAARMLVELSKAQDIEA 102
Cdd:PTZ00114 17 IRFGDearqslLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIefsdRFENVGAQLIRQVASKTNDKA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 103 GDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNSKVVsqyssl 182
Cdd:PTZ00114 97 GDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPV--KTKEDILNVATISANGDVE------ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 183 LSPMSVNAVMKVIDPATATSVDlrdikivkklGGTIDD-CELVEGLVLTQK------VANSGITRVEkakigliqfcLSA 255
Cdd:PTZ00114 169 IGSLIADAMDKVGKDGTITVED----------GKTLEDeLEVVEGMSFDRGyispyfVTNEKTQKVE----------LEN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 256 PktdmdnQIVVSDY--AQMDRVLReerayILNLVKQIKKtgcNVLLIQKSILRDALSDLAlhfLNKMKIMV--------- 324
Cdd:PTZ00114 229 P------LILVTDKkiSSIQSILP-----ILEHAVKNKR---PLLIIAEDVEGEALQTLI---INKLRGGLkvcavkapg 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 325 ---VKDIEREDIEFIC--KTIGTKPV-AHIDQFTPDMLGSAELA-----EEVSLNGSG--KLFK---------ITGCTS- 381
Cdd:PTZ00114 292 fgdNRKDILQDIAVLTgaTVVSEDNVgLKLDDFDPSMLGSAKKVtvtkdETVILTGGGdkAEIKervellrsqIERTTSe 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 382 -------------PGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELALRL--TEYSRTLSGM 446
Cdd:PTZ00114 372 ydkeklkerlaklSGGVAVIKVGGASEVEVNEKKDRIEDALNATRAAVEE-GIVPGGGVALLRASKLLdkLEEDNELTPD 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33414505 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 |
5.11e-18 |
|
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: 87.13 E-value: 5.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 41 AKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHP----AARMLVELSKAQDIEAGDGTTSVVIIAGSL 116
Cdd:cd03344 17 VNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLARAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 117 LDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNSkvvsqySSLLSPMSVNAVMKVID 196
Cdd:cd03344 97 IKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPV--KTKEEIAQVATISANG------DEEIGELIAEAMEKVGK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 197 PATATsvdlrdikiVKKLGGTIDDCELVEGlvltqkvansgitrvekakiglIQF---CLSaPK--TDMDNQIVVSdyaq 271
Cdd:cd03344 169 DGVIT---------VEEGKTLETELEVVEG----------------------MQFdrgYLS-PYfvTDPEKMEVEL---- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 272 mdrvlreERAYIL------NLVKQI-------KKTGCNVLLIQKSILRDALSDLALHFL-NKMKIMVVK-----DiER-- 330
Cdd:cd03344 213 -------ENPYILltdkkiSSIQELlpilelvAKAGRPLLIIAEDVEGEALATLVVNKLrGGLKVCAVKapgfgD-RRka 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 331 --EDI------EFICKTIGTKpvahIDQFTPDMLGSAELAeEVS------LNGSGKLFKITG-----------CTSP--- 382
Cdd:cd03344 285 mlEDIailtggTVISEELGLK----LEDVTLEDLGRAKKV-VVTkddttiIGGAGDKAAIKAriaqirkqieeTTSDydk 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 383 -----------GKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELALRLtEYSRTLSGMESYCV 451
Cdd:cd03344 360 eklqerlaklsGGVAVIKVGGATEVELKEKKDRVEDALNATRAAVEE-GIVPGGGVALLRASPAL-DKLKALNGDEKLGI 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 452 RAFADAMEVIPSTLAENAGLNPISTVTELRNrhaqGEKTTGINVRKGGISNILEEMVVQPLLV---------SVSALTLA 522
Cdd:cd03344 438 EIVRRALEAPLRQIAENAGVDGSVVVEKVLE----SPDGFGYDAATGEYVDMIEAGIIDPTKVvrsalqnaaSVASLLLT 513
|
....
gi 33414505 523 TETV 526
Cdd:cd03344 514 TEAL 517
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
196-394 |
9.47e-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: 9.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 196 DPATATSVDLRD-IKIVKKLGGTIDDCELVEGLVLTQKVANSGI-TRVEKAKIGLIQFCLsapktdmDNQIVVSDYAQMD 273
Cdd:cd03334 37 DVRAGDDMDIRQyVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMpSKIKNPRILLLQGPL-------EYQRVENKLLSLD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 274 RVLREERAYILNLVKQIKKTGCNVLLIQKSIlrdalSDLALHFLNKMKIMVVKDIEREDIEFICKTIGTKPVAHID-QFT 352
Cdd:cd03334 110 PVILQEKEYLKNLVSRIVALRPDVILVEKSV-----SRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDdLLT 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 33414505 353 PDMLGSAELAEE---VSLNGSGK-LFKITGCTSPGKTvTIVVRGSN 394
Cdd:cd03334 185 SPKLGTCESFRVrtyVEEHGRSKtLMFFEGCPKELGC-TILLRGGD 229
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
32-526 |
4.15e-15 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 77.86 E-value: 4.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 32 QIRFSN------ISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHP----AARMLVELSKAQDIE 101
Cdd:PRK12851 5 EVKFHVearekmLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 102 AGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNSkvvsqyss 181
Cdd:PRK12851 85 AGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPV--TTNAEIAQVATISANG-------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 182 llspmsvnavmkvidpatatsvdlrDIKIVKKLGGTIDdcelveglvltqKVANSGITRVEKAKIGLIQFCLsAPKTDMD 261
Cdd:PRK12851 155 -------------------------DAEIGRLVAEAME------------KVGNEGVITVEESKTAETELEV-VEGMQFD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 262 NQIV----VSDYAQMDRVLreERAYIL-------------NLVKQIKKTGCNVLLIQKSILRDALSDLAlhfLNKM---- 320
Cdd:PRK12851 197 RGYLspyfVTDADKMEAEL--EDPYILihekkisnlqdllPVLEAVVQSGKPLLIIAEDVEGEALATLV---VNKLrggl 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 321 KIMVVK--------DIEREDI------EFICKTIGTKpvahIDQFTPDMLGSAELA----EEVSL-NGSGKLFKITG--- 378
Cdd:PRK12851 272 KVAAVKapgfgdrrKAMLEDIailtggTVISEDLGIK----LENVTLEQLGRAKKVvvekENTTIiDGAGSKTEIEGrva 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 379 --------CTSP--------------GKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELALRL 436
Cdd:PRK12851 348 qiraqieeTTSDydreklqerlaklaGGVAVIRVGASTEVEVKEKKDRVDDALHATRAAVEE-GIVPGGGVALLRAVKAL 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 437 TEySRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNrhaqGEKTTGINVRKGGISNILEEMVVQPLLV-- 514
Cdd:PRK12851 427 DK-LETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLRE----KPGGYGFNAATNEYGDLYAQGVIDPVKVvr 501
|
570
....*....|....*....
gi 33414505 515 -------SVSALTLATETV 526
Cdd:PRK12851 502 talqnaaSVAGLLLTTEAM 520
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
43-526 |
8.90e-15 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 76.77 E-value: 8.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 43 AVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHP----AARMLVE-LSKAQDIeAGDGTTSVVIIAGSLL 117
Cdd:PRK12849 21 KLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEvASKTNDV-AGDGTTTATVLAQALV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 118 DSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNSKVvsqyssllspmsvnAVMKVIdp 197
Cdd:PRK12849 100 QEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPV--SGSEEIAQVATISANGDE--------------EIGELI-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 198 ATA-TSVDLRDIKIVKKLGGTIDDCELVEGLVLtqkvaNSG------ITRVEKakigliqfclsapktdmdnqivvsdya 270
Cdd:PRK12849 162 AEAmEKVGKDGVITVEESKTLETELEVTEGMQF-----DRGylspyfVTDPER--------------------------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 271 qMDRVLreERAYIL-------------NLVKQIKKTGCNVLLIQKSILRDALSDLalhFLNKM----KIMVVKDI---ER 330
Cdd:PRK12849 210 -MEAVL--EDPLILltdkkisslqdllPLLEKVAQSGKPLLIIAEDVEGEALATL---VVNKLrgglKVAAVKAPgfgDR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 331 -----EDI------EFICKTIGTKpvahIDQFTPDMLGSAElaeevslngsgklfKITgctsPGKTVTIVVRGSN----- 394
Cdd:PRK12849 284 rkamlEDIailtggTVISEDLGLK----LEEVTLDDLGRAK--------------RVT----ITKDNTTIVDGAGdkeai 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 395 -------KLVIEEA----------ER--------------------------SIHDALCVIRCLVKKrALIAGGGAPEIE 431
Cdd:PRK12849 342 earvaqiRRQIEETtsdydreklqERlaklaggvavikvgaatevelkerkdRVEDALNATRAAVEE-GIVPGGGVALLR 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 432 LALRLTEYsRTLSGMESYCVRAFADAMEVIPSTLAENAGLNP---ISTVTELRNRHaqgekttGINVRKGGISNILEEMV 508
Cdd:PRK12849 421 AAKALDEL-AGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGsvvVAKVLELEDGF-------GFNAATGEYGDLIAAGI 492
|
570 580
....*....|....*....|....*..
gi 33414505 509 VQPLLV---------SVSALTLATETV 526
Cdd:PRK12849 493 IDPVKVtrsalqnaaSVAGLLLTTEAL 519
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
32-526 |
3.11e-14 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 75.14 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 32 QIRFSNISAAK------AVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVEL-----SKAQDI 100
Cdd:PRK12850 5 EIRFSTDARDRllrgvnILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMvkevaSKTNDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 101 eAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQlsDRETLLNSATTSLNSKvvsqys 180
Cdd:PRK12850 85 -AGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVT--SSKEIAQVATISANGD------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 181 sllspmsvNAVMKVIdpatATSVDlrdikivkklggtiddcelveglvltqKVANSGITRVEKAK-IGL-------IQFc 252
Cdd:PRK12850 156 --------ESIGEMI----AEAMD---------------------------KVGKEGVITVEEAKtLGTeldvvegMQF- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 253 lsapktdmDNQIV----VSDYAQMDRVLreERAYIL-------------NLVKQIKKTGCNVLLIQKSILRDALSDLALH 315
Cdd:PRK12850 196 --------DRGYLspyfVTNPEKMRAEL--EDPYILlhekkisnlqdllPILEAVVQSGRPLLIIAEDVEGEALATLVVN 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 316 FLNK-MKIMVVK--------DIEREDI------EFICKTIGTKpvahIDQFTPDMLGSA-----ELAEEVSLNGSGKLFK 375
Cdd:PRK12850 266 KLRGgLKSVAVKapgfgdrrKAMLEDIavltggQVISEDLGIK----LENVTLDMLGRAkrvliTKENTTIIDGAGDKKN 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 376 ITGCTS-------------------------PGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPEI 430
Cdd:PRK12850 342 IEARVKqiraqieettsdydreklqerlaklAGGVAVIRVGGATEVEVKEKKDRVDDALHATRAAVEE-GIVPGGGVALL 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 431 ElALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNP---ISTVTELRNRHaqgekttGINVRKGGISNILEEM 507
Cdd:PRK12850 421 R-ARSALRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGsvvVGKVAELPGNF-------GFNAQTGEYGDMVEAG 492
|
570 580
....*....|....*....|....*...
gi 33414505 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 |
4.83e-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: 74.64 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 30 PAQIRFSNISAAK------AVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVEL-----SKAQ 98
Cdd:TIGR02348 1 AKQIKFDEEARKAllrgvdKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLvkevaSKTN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33414505 99 DIeAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNS 173
Cdd:TIGR02348 81 DV-AGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPV--KGKKEIAQVATISANN 152
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
24-530 |
1.55e-11 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 66.67 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 24 YQDRDKPAQIRFSNIsaakaVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVEL-----SKAQ 98
Cdd:CHL00093 7 YQDNARRALERGMDI-----LAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALirqaaSKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 99 DIeAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQlsDRETLLNSATTSL-NSKVVS 177
Cdd:CHL00093 82 DV-AGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVE--DIQAITQVASISAgNDEEVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 178 QyssllspMSVNAVMKVidpatatsvdLRDIKIVKKLG-GTIDDCELVEGLvltqkvansgitRVEKAKIgliqfclsap 256
Cdd:CHL00093 159 S-------MIADAIEKV----------GREGVISLEEGkSTVTELEITEGM------------RFEKGFI---------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 257 ktdmdNQIVVSDYAQMDRVLreERAYIL------NLVKQ--------IKKTGCNVLLIQKSILRDALSDLalhFLNKMK- 321
Cdd:CHL00093 200 -----SPYFVTDTERMEVVQ--ENPYILltdkkiTLVQQdllpileqVTKTKRPLLIIAEDVEKEALATL---VLNKLRg 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 322 -IMVVK-------DIEREDIEFICKTIGTKPVAH-----IDQFTPDMLGSA--------------------------ELA 362
Cdd:CHL00093 270 iVNVVAvrapgfgDRRKAMLEDIAILTGGQVITEdaglsLETIQLDLLGQArriivtkdsttiiadgneeqvkarceQLR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 363 EEVSLNGSG--------KLFKITGctspGKTVtIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELAL 434
Cdd:CHL00093 350 KQIEIADSSyekeklqeRLAKLSG----GVAV-IKVGAATETEMKDKKLRLEDAINATKAAVEE-GIVPGGGATLVHLSE 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 435 RLTEYSRT-LSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRhaqgEKTTGINVRKGGISNILEEMVVQPLL 513
Cdd:CHL00093 424 NLKTWAKNnLKEDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQ----DFEIGYNAANNKFVNMYEAGIIDPAK 499
|
570
....*....|....*..
gi 33414505 514 VSVSALTLATETVRSIL 530
Cdd:CHL00093 500 VTRSALQNAASIASMIL 516
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
43-173 |
6.69e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 64.76 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 43 AVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVEL-----SKAQDIeAGDGTTSVVIIAGSLL 117
Cdd:PRK00013 21 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLvkevaSKTNDV-AGDGTTTATVLAQAIV 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 33414505 118 DSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNS 173
Cdd:PRK00013 100 REGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPV--EDKEEIAQVATISANG 153
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
44-524 |
8.15e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 64.48 E-value: 8.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 44 VADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVL----HPAARMLVEL-SKAQDIeAGDGTTSVVIIAGSLLD 118
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVaSKTNDL-AGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 119 SCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSdrETLLNSATTSLNSKVvsqyssllspmsvnAVMKVIDPA 198
Cdd:PRK12852 102 EGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASS--AEIAQVGTISANGDA--------------AIGKMIAQA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 199 tatsvdlrdikivkklggtiddcelveglvlTQKVANSGITRVEKAKigliqfclsapktDMDNQIVVSDYAQMDR---- 274
Cdd:PRK12852 166 -------------------------------MQKVGNEGVITVEENK-------------SLETEVDIVEGMKFDRgyls 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 275 ----------VLREERAYIL-------------NLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNK-MKIMVVK---- 326
Cdd:PRK12852 202 pyfvtnaekmTVELDDAYILlhekklsglqamlPVLEAVVQSGKPLLIIAEDVEGEALATLVVNRLRGgLKVAAVKapgf 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 327 -DIER---EDI------EFICKTIGTKpvahIDQFTPDMLGSAELAE-----EVSLNGSGKLFKITG-----------CT 380
Cdd:PRK12852 282 gDRRKamlEDIailtggQLISEDLGIK----LENVTLKMLGRAKKVVidkenTTIVNGAGKKADIEArvgqikaqieeTT 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 381 S--------------PGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKrALIAGGGAPeielALRLTEYSRTLSGM 446
Cdd:PRK12852 358 SdydreklqerlaklAGGVAVIRVGGATEVEVKEKKDRVEDALNATRAAVQE-GIVPGGGVA----LLRAKKAVGRINND 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 447 ES---YCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQgekTTGINVRKGGISNILEEMVVQPLLV--------- 514
Cdd:PRK12852 433 NAdvqAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSE---TFGFDAQTEEYVDMVAKGIIDPAKVvrtalqdaa 509
|
570
....*....|
gi 33414505 515 SVSALTLATE 524
Cdd:PRK12852 510 SVAGLLVTTE 519
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
44-159 |
1.76e-09 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 60.32 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 44 VADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVEL-----SKAQDIeAGDGTTSVVIIAGSLLD 118
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLvrqaaAKTNDL-AGDGTTTSVVLAQGLIA 156
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 33414505 119 SCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSD 159
Cdd:PLN03167 157 EGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE 197
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
44-526 |
1.47e-08 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 57.35 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 44 VADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQV----LHPAARMLVEL-SKAQDIeAGDGTTSVVIIAGSLLD 118
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVaSKSADA-AGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 119 SCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVqlSDRETLLNSATTSLNSKvvSQYSSLLSpmsvNAVMKVIDPA 198
Cdd:PRK14104 102 EGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKV--TSNDEIAQVGTISANGD--AEIGKFLA----DAMKKVGNEG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 199 TATSVDLRDIKIvkklggtidDCELVEGLVLTQK-VANSGITRVEKAKIgliqfclsapktDMDNQIVVSDYAQMDRvLR 277
Cdd:PRK14104 174 VITVEEAKSLET---------ELDVVEGMQFDRGyISPYFVTNADKMRV------------EMDDAYILINEKKLSS-LN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 278 EerayILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFL-NKMKIMVVK-----DIEREDIEFICKTIGTKPVAH---- 347
Cdd:PRK14104 232 E----LLPLLEAVVQTGKPLVIVAEDVEGEALATLVVNRLrGGLKVAAVKapgfgDRRKAMLQDIAILTGGQAISEdlgi 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 348 -IDQFTPDMLGSA-----ELAEEVSLNGSGKLFKITG-----------CTS--------------PGKTVTIVVRGSNKL 396
Cdd:PRK14104 308 kLENVTLQMLGRAkkvmiDKENTTIVNGAGKKADIEArvaqikaqieeTTSdydreklqerlaklAGGVAVIRVGGATEV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33414505 397 VIEEAERSIHDALCVIRCLVKKrALIAGGGAPEIELALRLTEYsRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPIST 476
Cdd:PRK14104 388 EVKERKDRVDDAMHATRAAVEE-GIVPGGGVALLRASEQLKGI-KTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVI 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 33414505 477 VTELRNRHaqgEKTTGINVRKGGISNILEEMVVQPLLV---------SVSALTLATETV 526
Cdd:PRK14104 466 VGKILEKE---QYSYGFDSQTGEYGNLVSKGIIDPTKVvrtaiqnaaSVAALLITTEAM 521
|
|
| |
