|
Name |
Accession |
Description |
Interval |
E-value |
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
6-529 |
0e+00 |
|
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: 1003.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:TIGR02344 1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVI 165
Cdd:TIGR02344 81 TQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 166 SRWSSLACNIALDAVKTVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSL 245
Cdd:TIGR02344 161 SRWSDLMCDLALDAVRTVQRDENGRKEIDIKRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 246 EYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIAR 325
Cdd:TIGR02344 241 EYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 326 ACGARIVSRPEELREDDVGTGAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDP 405
Cdd:TIGR02344 321 ACGATIVNRPEELRESDVGTGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 406 QLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCETWGVNGETG 485
Cdd:TIGR02344 401 KLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTWGIDGETG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 549059 486 TLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKK 529
Cdd:TIGR02344 481 KIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVSGVKKK 524
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
6-525 |
0e+00 |
|
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: 960.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:cd03337 1 PVLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVI 165
Cdd:cd03337 81 TQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 166 SRWSSLACNIALDAVKTVQFEENGR-KEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSS 244
Cdd:cd03337 161 SRWSDLMCNLALDAVKTVAVEENGRkKEIDIKRYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 245 LEYkkgesqtdieitreedftrilqmeeeyihqlcediiqlkpdVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIA 324
Cdd:cd03337 241 LEY-----------------------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 325 RACGARIVSRPEELREDDVGTGAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLD 404
Cdd:cd03337 280 RACGATIVNRPEELTESDVGTGAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 405 PQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCETWGVNGET 484
Cdd:cd03337 360 PKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTWGIDGET 439
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 549059 485 GTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSG 525
Cdd:cd03337 440 GDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIVSG 480
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
14-524 |
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: 607.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 14 TKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGD 93
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 94 GTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVISRWSSLAC 173
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 174 NIALDAVKTVQFEENgrkeIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYkkgesq 253
Cdd:cd00309 161 ELVVDAVLKVGKENG----DVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 254 tdieitreedftrilqmeeeyihqlcediiqlkpdVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARACGARIVS 333
Cdd:cd00309 231 -----------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 334 RPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGA 413
Cdd:cd00309 276 RLEDLTPEDLGT-AGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 414 SEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCeTWGVNGETGTLVDMKEL 493
Cdd:cd00309 355 AEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGG-NAGGDVETGEIVDMKEA 433
|
490 500 510
....*....|....*....|....*....|.
gi 549059 494 GIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:cd00309 434 GIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
33-524 |
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: 578.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 33 IADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSVAEHF 112
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 113 LEQQMHPTVVISAYRMALDDMISTLKKI-STPVDVNNREMMLSIINSSITTKVISRWSSLACNIALDAVKTVqfeENGRK 191
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAI---PKNDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 192 EIDIKKyARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGESQTDIEITREEDFTRILQME 271
Cdd:pfam00118 158 SFDLGN-IGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 272 EEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARACGARIVSRPEELREDDVGTgAGLLE 351
Cdd:pfam00118 237 EEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGT-AGKVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 352 IKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTG 431
Cdd:pfam00118 316 EEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 432 VEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHtQESCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVE 511
Cdd:pfam00118 396 KEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAH-ASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATE 474
|
490
....*....|...
gi 549059 512 TAVLLLRIDDIVS 524
Cdd:pfam00118 475 AASTILRIDDIIK 487
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
6-524 |
0e+00 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 544.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:NF041082 2 PILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVI 165
Cdd:NF041082 82 TQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 166 SRWSSLACNIALDAVKTVQfEENGRKEIDIkKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSL 245
Cdd:NF041082 162 EAAKDKLADLVVDAVKAVA-EKDGGYNVDL-DNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 246 EYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIAR 325
Cdd:NF041082 240 EVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 326 ACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDP 405
Cdd:NF041082 320 ATGARIVTSIDDLSPEDLGY-AGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 406 QLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHtQESCETWGVNGETG 485
Cdd:NF041082 399 KVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAH-EKGNKTAGLDVYTG 477
|
490 500 510
....*....|....*....|....*....|....*....
gi 549059 486 TLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:NF041082 478 KVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIA 516
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
6-524 |
0e+00 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 542.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:NF041083 2 PVLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVI 165
Cdd:NF041083 82 TQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 166 SRWSSLACNIALDAVKTVQFEENGRKEIDIkKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSL 245
Cdd:NF041083 162 EEARDYLAEIAVKAVKQVAEKRDGKYYVDL-DNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 246 EYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIAR 325
Cdd:NF041083 241 EVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 326 ACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDP 405
Cdd:NF041083 321 ATGARIVTNIDDLTPEDLGY-AELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 406 QLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHtQESCETWGVNGETG 485
Cdd:NF041083 400 KIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAH-EKGKKWAGINVFTG 478
|
490 500 510
....*....|....*....|....*....|....*....
gi 549059 486 TLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:NF041083 479 EVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIA 517
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
7-524 |
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: 530.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 7 VLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRT 86
Cdd:cd03343 1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 87 QDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVIS 166
Cdd:cd03343 81 QDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 167 RWSSLACNIALDAVKTVQFEENGRKEIDIkKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLE 246
Cdd:cd03343 161 AAKDKLADLVVDAVLQVAEKRDGKYVVDL-DNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 247 YKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARA 326
Cdd:cd03343 240 VKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 327 CGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQ 406
Cdd:cd03343 320 TGAKIVTNIDDLTPEDLGE-AELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 407 LVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQEScETWGVNGETGT 486
Cdd:cd03343 399 VVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGN-KNAGLDVYTGE 477
|
490 500 510
....*....|....*....|....*....|....*...
gi 549059 487 LVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:cd03343 478 VVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIA 515
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
6-524 |
2.40e-176 |
|
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: 507.69 E-value: 2.40e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:TIGR02339 1 PVFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVI 165
Cdd:TIGR02339 81 TQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 166 SRWS-SLACNIALDAVKTV-QFEENGRKEIDIKKyARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDS 243
Cdd:TIGR02339 161 AEVAkDKLADLVVEAVKQVaELRGDGKYYVDLDN-IKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 244 SLEYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRI 323
Cdd:TIGR02339 240 PLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 324 ARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLL 403
Cdd:TIGR02339 320 ARATGARIVSSIDEITESDLGY-AELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 404 DPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQEScETWGVNGE 483
Cdd:TIGR02339 399 DGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGN-KNAGINVF 477
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 549059 484 TGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:TIGR02339 478 TGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVIA 518
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
5-524 |
2.62e-128 |
|
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: 385.11 E-value: 2.62e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 5 RPVLVL--SQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIE 82
Cdd:cd03339 5 RPFIIVreQEKKKRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 83 ISRTQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKIST--PVDVNNREMMLSIINSSI 160
Cdd:cd03339 85 LSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADkiEFSPDNKEPLIQTAMTSL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 161 TTKVISRWSSLACNIALDAVKTVQFEEngRKEID---IKkyarVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPR 237
Cdd:cd03339 165 GSKIVSRCHRQFAEIAVDAVLSVADLE--RKDVNfelIK----VEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 238 IVLLDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRK 317
Cdd:cd03339 239 IAILTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 318 TDNNRIARACGARIVSRPEELREDDVGTgAGLLEIKKIG--DEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAM 395
Cdd:cd03339 319 VEIELIAIATGGRIVPRFEDLSPEKLGK-AGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDAL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 396 QVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESC 475
Cdd:cd03339 398 CVVRNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKN 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 549059 476 ETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:cd03339 478 PHLGIDCLGRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
14-523 |
1.34e-125 |
|
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: 377.78 E-value: 1.34e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 14 TKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGD 93
Cdd:cd03338 1 TDKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 94 GTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVISRWSSLAC 173
Cdd:cd03338 81 GTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 174 NIALDAVKTVqFEENGRKEIDIKKYARVEKIpGGIIEDSCVLRGVMINKDVTH-PRMRRYIKNPRIVLLDSSLEYKKGES 252
Cdd:cd03338 161 PIAVDAVLKV-IDPATATNVDLKDIRIVKKL-GGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 253 QTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGI-----SDLAQHYLMRANVTAIRRVRKTDNNRIARAC 327
Cdd:cd03338 239 DNNIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 328 GARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDP-KACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQ 406
Cdd:cd03338 319 GCKPVASIDHFTEDKLGS-ADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 407 LVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCeTWGVNGETGT 486
Cdd:cd03338 398 LIPGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEK-NAGINVRKGA 476
|
490 500 510
....*....|....*....|....*....|....*..
gi 549059 487 LVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:cd03338 477 ITNILEENVVQPLLVSTSAITLATETVRMILKIDDIV 513
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
6-523 |
1.58e-123 |
|
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: 372.78 E-value: 1.58e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:cd03340 1 PIILLKEGTDTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNN----REMMLSIINSSIT 161
Cdd:cd03340 81 SQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDkeeqRELLEKCAATALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 162 TKVISRWSSLACNIALDAVKTVQfEENGRKEIDIKKyarvekIPGGIIEDSCVLRGVMINKDVT---HPRMRRYIKNPRI 238
Cdd:cd03340 161 SKLIASEKEFFAKMVVDAVLSLD-DDLDLDMIGIKK------VPGGSLEDSQLVNGVAFKKTFSyagFEQQPKKFKNPKI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 239 VLLDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKT 318
Cdd:cd03340 234 LLLNVELELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 319 DNNRIARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVC 398
Cdd:cd03340 314 DLKRVAQATGGSIQTTVSNITDDVLGT-CGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 399 RNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCETW 478
Cdd:cd03340 393 RRAIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKWY 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 549059 479 GVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:cd03340 473 GVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLILSVDETI 517
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
5-524 |
2.91e-122 |
|
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: 369.90 E-value: 2.91e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 5 RPVLVLSQ--NTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIE 82
Cdd:TIGR02343 9 RPFIIIKDqdNKKRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 83 ISRTQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPV--DVNNREMMLSIINSSI 160
Cdd:TIGR02343 89 LSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEIsaDNNNREPLIQAAKTSL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 161 TTKVISRWSSLACNIALDAVKTVQFEEngRKEIDIkKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVL 240
Cdd:TIGR02343 169 GSKIVSKCHRRFAEIAVDAVLNVADME--RRDVDF-DLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 241 LDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDN 320
Cdd:TIGR02343 246 LTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQEL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 321 NRIARACGARIVSRPEELREDDVGTgAGLLEIKKIG--DEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVC 398
Cdd:TIGR02343 326 ELIAIATGGRIVPRFQELSKDKLGK-AGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 399 RNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCETW 478
Cdd:TIGR02343 405 RNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNL 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 549059 479 GVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:TIGR02343 485 GVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVIS 530
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
6-523 |
2.96e-121 |
|
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: 366.78 E-value: 2.96e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:TIGR02345 3 TIVLLKEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNN---REMMLSIINSSITT 162
Cdd:TIGR02345 83 SQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqRELLEKCAATALSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 163 KVISRWSSLACNIALDAVKTVQFEENGRKEIDIKkyarveKIPGGIIEDSCVLRGVMINKDVT---HPRMRRYIKNPRIV 239
Cdd:TIGR02345 163 KLISHNKEFFSKMIVDAVLSLDRDDLDLKLIGIK------KVQGGALEDSQLVNGVAFKKTFSyagFEQQPKKFANPKIL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 240 LLDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTD 319
Cdd:TIGR02345 237 LLNVELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 320 NNRIARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCR 399
Cdd:TIGR02345 317 LKRVIKACGGSIQSTTSDLEADVLGT-CALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 400 NVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCetW- 478
Cdd:TIGR02345 396 RALKNKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGK--Wy 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 549059 479 GVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:TIGR02345 474 GVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETI 518
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
15-523 |
1.10e-115 |
|
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: 352.74 E-value: 1.10e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 15 KRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDG 94
Cdd:cd03335 2 ERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 95 TTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKK-ISTPVDVNNREMMLSIINSSITTKVISRWSSLAC 173
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDNLGKESLINVAKTSMSSKIIGADSDFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 174 NIALDAVKTVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGESQ 253
Cdd:cd03335 162 NMVVDAILAVKTTNEKGKTKYPIKAVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 254 TDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARACGARIVS 333
Cdd:cd03335 242 VQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 334 RPEELREDDVGTGAGL-----LEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLV 408
Cdd:cd03335 322 TLANLEGEETFDPSYLgeaeeVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 409 PGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKH-------TQESCETWGVN 481
Cdd:cd03335 402 PGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHaaaqvkpDKKHLKWYGLD 481
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 549059 482 GETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:cd03335 482 LINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLI 523
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
15-532 |
5.32e-115 |
|
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: 351.33 E-value: 5.32e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 15 KRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDG 94
Cdd:TIGR02340 6 ERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 95 TTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKK-ISTPVDVNNREMMLSIINSSITTKVISRWSSLAC 173
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDELGREALINVAKTSMSSKIIGLDSDFFS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 174 NIALDAVKTVQFE-ENGRKEIDIKKyARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGES 252
Cdd:TIGR02340 166 NIVVDAVLAVKTTnENGETKYPIKA-INILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAKMAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 253 QTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARACGARIV 332
Cdd:TIGR02340 245 GVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 333 SRPEELREDDVGTGAGL-----LEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQL 407
Cdd:TIGR02340 325 STLADLEGEETFEASYLgfadeVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 408 VPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKH-------TQESCETWGV 480
Cdd:TIGR02340 405 VPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHaaaqlkpEKKHLKWYGL 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 549059 481 NGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGDD 532
Cdd:TIGR02340 485 DLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIKLNPEQSKG 536
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
16-523 |
3.59e-113 |
|
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: 346.00 E-value: 3.59e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 16 RESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGT 95
Cdd:TIGR02342 4 KDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 96 TSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVISRWSSLACNI 175
Cdd:TIGR02342 84 TSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 176 ALDAVKTVQFEENGrKEIDIKKYARVEKIpGGIIEDSCVLRGVMINKDVTHPR-MRRYIKNPRIVLLDSSLEYKKGESQT 254
Cdd:TIGR02342 164 AVDAVLKVIDPENA-KNVDLNDIKVVKKL-GGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDMEN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 255 DIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGI-----SDLAQHYLMRANVTAIRRVRKTDNNRIARACGA 329
Cdd:TIGR02342 242 QIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGC 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 330 RIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDP-KACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLV 408
Cdd:TIGR02342 322 KPIASIDHFTADKLGS-AELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 409 PGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQEScETWGVNGETGTLV 488
Cdd:TIGR02342 401 AGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGE-KTAGISVRKGGIT 479
|
490 500 510
....*....|....*....|....*....|....*
gi 549059 489 DMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:TIGR02342 480 NMLEEHVLQPLLVTTSAITLASETVRSILKIDDIV 514
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
19-533 |
6.76e-108 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 331.66 E-value: 6.76e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 19 GRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHP----AAKSMIEISRTQDEEVGDG 94
Cdd:COG0459 8 GEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 95 TTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDvnNREMMLSIINSSITTKvisrwSSLAcN 174
Cdd:COG0459 88 TTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVD--DKEELAQVATISANGD-----EEIG-E 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 175 IALDAVKTVqfeengRKEIDIKkyarVEKiPGGIIEDSCVLRGVMINKDVTHP-------RMRRYIKNPRIVLLDSsley 247
Cdd:COG0459 160 LIAEAMEKV------GKDGVIT----VEE-GKGLETELEVVEGMQFDKGYLSPyfvtdpeKMPAELENAYILLTDK---- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 248 kkgesqtdiEITREEDFTRILqmeeeyihqlcEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRV-----------R 316
Cdd:COG0459 225 ---------KISSIQDLLPLL-----------EKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgdrR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 317 KTDNNRIARACGARIVSR-----PEELREDDVGTgAGLLEikkIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNL 391
Cdd:COG0459 285 KAMLEDIAILTGGRVISEdlglkLEDVTLDDLGR-AKRVE---VDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 392 QDAMQVCRNVLLDpQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKht 471
Cdd:COG0459 361 EDALHATRAAVEE-GIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA-- 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549059 472 qeSCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGDDQ 533
Cdd:COG0459 438 --KDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
13-523 |
1.41e-104 |
|
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: 322.67 E-value: 1.41e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 13 NTKRESGRKVQS--GNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAkSMIEISRT-QDE 89
Cdd:cd03342 2 NPKAEVLRRGQAlaVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTA-SMIARAATaQDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 90 EVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDV-NNREMMLSIINSSITTKVISRW 168
Cdd:cd03342 81 ITGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIdTDRELLLSVARTSLRTKLHADL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 169 SSLACNIALDAVKTVQFEEngrKEIDIKkyaRVE--KIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLE 246
Cdd:cd03342 161 ADQLTEIVVDAVLAIYKPD---EPIDLH---MVEimQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 247 YKKGESQTdieitreedftrilqmeeeyihqlcediiQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARA 326
Cdd:cd03342 235 YEKTEVNS-----------------------------GFFYSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 327 CGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQ 406
Cdd:cd03342 286 CGGVAMNSVDDLSPECLGY-AGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKC 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 407 LVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTqESCETWGVNGETGT 486
Cdd:cd03342 365 VVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYA-EGGQVGGVDLDTGE 443
|
490 500 510
....*....|....*....|....*....|....*..
gi 549059 487 LVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:cd03342 444 PMDPESEGIWDNYSVKRQILHSATVIASQLLLVDEII 480
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
26-523 |
3.09e-103 |
|
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: 318.78 E-value: 3.09e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 26 NINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEM 105
Cdd:cd03341 13 NIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 106 LSVAEHFLEQQMHPTVVISAYRMALDDMISTLKK--ISTPVDVNNREMMLSIINSSITTKVISRwSSLACNIALDAVKTV 183
Cdd:cd03341 93 LEKAEELLRMGLHPSEIIEGYEKALKKALEILEElvVYKIEDLRNKEEVSKALKTAIASKQYGN-EDFLSPLVAEACISV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 184 QFEENGRKEIDikkYARVEKIPGGIIEDSCVLRGVMINKD----VTHprmrryIKNPRIVLLDSSLEykkgesqtdieit 259
Cdd:cd03341 172 LPENIGNFNVD---NIRVVKILGGSLEDSKVVRGMVFKREpegsVKR------VKKAKVAVFSCPFD------------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 260 reedftrilqmeeeyihqlcediiqLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARACGARIVSR----- 334
Cdd:cd03341 230 -------------------------IGVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRlgapt 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 335 PEELREDDVgtgaglLEIKKIGDEYFTFITDCK-DPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGA 413
Cdd:cd03341 285 PEEIGYCDS------VYVEEIGDTKVVVFRQNKeDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 414 SEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCETwGVNGETG--TLVDMK 491
Cdd:cd03341 359 TEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSA-GVDIESGdeGTKDAK 437
|
490 500 510
....*....|....*....|....*....|..
gi 549059 492 ELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:cd03341 438 EAGIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-524 |
4.36e-97 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 304.64 E-value: 4.36e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 1 MMGHRPVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKmLLDPM------GGIVMTNDGNAILREIQVQH 74
Cdd:PTZ00212 2 IMANVPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDK-ILQPMsegprsGNVTVTNDGATILKSVWLDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 75 PAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNN---REM 151
Cdd:PTZ00212 81 PAAKILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEekfKED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 152 MLSIINSSITTKVISRWSSLACNIALDAVKTVqfeeNGRKEIDikkYARVEKIPGGIIEDSCVLRGVMINKDVThPRMRR 231
Cdd:PTZ00212 161 LLNIARTTLSSKLLTVEKDHFAKLAVDAVLRL----KGSGNLD---YIQIIKKPGGTLRDSYLEDGFILEKKIG-VGQPK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 232 YIKNPRIVLLDSSLEYKKgesqtdIEI----TREEDFTRILQMEE---EYIHQLCEDIIQLKPDVVITEKGISDLAQHYL 304
Cdd:PTZ00212 233 RLENCKILVANTPMDTDK------IKIygakVKVDSMEKVAEIEAaekEKMKNKVDKILAHGCNVFINRQLIYNYPEQLF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 305 MRANVTAIRRVRKTDNNRIARACGARIVSRPEELREDDVGTGAGLLEIkKIGDEYFTFITDCKDPKACTILLRGASKEIL 384
Cdd:PTZ00212 307 AEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEI-MIGEDKLIRFSGCAKGEACTIVLRGASTHIL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 385 SEVERNLQDAMQVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLT 464
Cdd:PTZ00212 386 DEAERSLHDALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVS 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 465 SLRAKHTQEScETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:PTZ00212 466 KLRAEHYKGN-KTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIR 524
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
13-523 |
5.40e-97 |
|
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: 304.35 E-value: 5.40e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 13 NTKRESGRKVQS--GNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEE 90
Cdd:TIGR02347 6 NPKAESLRRDAAlmMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 91 VGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPV-DVNNREMMLSIINSSITTKVISRWS 169
Cdd:TIGR02347 86 TGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKeDEVDREFLLNVARTSLRTKLPADLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 170 SLACNIALDAVKTVQFEEngrKEID---IKKYARVEKIPggiiEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLE 246
Cdd:TIGR02347 166 DQLTEIVVDAVLAIKKDG---EDIDlfmVEIMEMKHKSA----TDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 247 YKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLK-------PD---VVITEKGISDLAQHYLMRANVTAIRRVR 316
Cdd:TIGR02347 239 YEKTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKkkvcgksPDkgfVVINQKGIDPPSLDLLAKEGIMALRRAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 317 KTDNNRIARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQ 396
Cdd:TIGR02347 319 RRNMERLTLACGGEALNSVEDLTPECLGW-AGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 397 VCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTqESCE 476
Cdd:TIGR02347 398 AVKNAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHD-EGGE 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 549059 477 TWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:TIGR02347 477 VVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVM 523
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
9-524 |
4.79e-95 |
|
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: 298.86 E-value: 4.79e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 9 VLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLL--DPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRT 86
Cdd:cd03336 1 ILKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILQsvGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 87 QDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNN---REMMLSIINSSITTK 163
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEeafREDLLNIARTTLSSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 164 VISRWSSLACNIALDAVktvqFEENGRKEIDikkYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRyIKNPRIVLLDS 243
Cdd:cd03336 161 ILTQDKEHFAELAVDAV----LRLKGSGNLD---AIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQPKR-IENAKILIANT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 244 SLEYKKgesqtdIEI----TREEDFTRILQMEE---EYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVR 316
Cdd:cd03336 233 PMDTDK------IKIfgakVRVDSTAKVAEIEEaekEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHAD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 317 KTDNNRIARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQ 396
Cdd:cd03336 307 FDGVERLALVTGGEIASTFDHPELVKLGT-CKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALC 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 397 VCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCe 476
Cdd:cd03336 386 VLAQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNT- 464
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 549059 477 TWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:cd03336 465 TAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIK 512
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
26-523 |
1.71e-92 |
|
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: 292.78 E-value: 1.71e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 26 NINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEM 105
Cdd:TIGR02346 23 NIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 106 LSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKIS--TPVDVNNREMMLSIINSSITTKVISRWSSLACNIAlDAVKTV 183
Cdd:TIGR02346 103 LNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVvwEVKDLRDKDELIKALKASISSKQYGNEDFLAQLVA-QACSTV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 184 QFEENGRKEIDikkYARVEKIPGGIIEDSCVLRGVMINKDvTHPRMRRyIKNPRIVLLDSSLEYKKGESQTDIEITREED 263
Cdd:TIGR02346 182 LPKNPQNFNVD---NIRVCKILGGSLSNSEVLKGMVFNRE-AEGSVKS-VKNAKVAVFSCPLDTATTETKGTVLIHNAEE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 264 FTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARACGARIVSR-----PEEL 338
Cdd:TIGR02346 257 LLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRlgaptPEEI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 339 REDDVgtgaglLEIKKIGDEYFT-FITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGASEMA 417
Cdd:TIGR02346 337 GYVDS------VYVSEIGGDKVTvFKQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 418 VAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHtQESCETWGVN--GETGTLVDMKELGI 495
Cdd:TIGR02346 411 LASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAH-KKGNKSKGIDieAESDGVKDASEAGI 489
|
490 500
....*....|....*....|....*...
gi 549059 496 WEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:TIGR02346 490 YDMLATKKWAIKLATEAAVTVLRVDQII 517
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
149-404 |
7.67e-78 |
|
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: 243.91 E-value: 7.67e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 149 REMMLSIINSSITTKvISRWSSLACNIALDAVKTVQFEENgrkeIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPR 228
Cdd:cd03333 1 RELLLQVATTSLNSK-LSSWDDFLGKLVVDAVLKVGPDNR----MDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 229 MRRYIKNPRIVLLDSSLEYkkgesqtdieitreedftrilqmeeeyihqlcediiqlkpdVVITEKGISDLAQHYLMRAN 308
Cdd:cd03333 76 MPKRLENAKILLLDCPLEY-----------------------------------------VVIAEKGIDDLALHYLAKAG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 309 VTAIRRVRKTDNNRIARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVE 388
Cdd:cd03333 115 IMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGT-AELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVK 193
|
250
....*....|....*.
gi 549059 389 RNLQDAMQVCRNVLLD 404
Cdd:cd03333 194 RSLHDALCAVRAAVEE 209
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
9-523 |
6.28e-71 |
|
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: 235.91 E-value: 6.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 9 VLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLL--DPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRT 86
Cdd:TIGR02341 2 IFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 87 QDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNN---REMMLSIINSSITTK 163
Cdd:TIGR02341 82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEvkfRQDLMNIARTTLSSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 164 VISRWSSLACNIALDAVKTVQfeenGRKEIDikkYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRyIKNPRIVLLDS 243
Cdd:TIGR02341 162 ILSQHKDHFAQLAVDAVLRLK----GSGNLE---AIQIIKKLGGSLADSYLDEGFLLDKKIGVNQPKR-IENAKILIANT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 244 SLEYKKGES-QTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNR 322
Cdd:TIGR02341 234 GMDTDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 323 IARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVL 402
Cdd:TIGR02341 314 LALVTGGEIVSTFDHPELVKLGS-CDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 403 LDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTqESCETWGVNG 482
Cdd:TIGR02341 393 KESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHY-NGNTTMGLDM 471
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 549059 483 ETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:TIGR02341 472 NEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNII 512
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
167-392 |
1.23e-45 |
|
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: 161.24 E-value: 1.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 167 RWSSLACNIALDAVKTVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLE 246
Cdd:cd03334 18 SWLDILLPLVWKAASNVKPDVRAGDDMDIRQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 247 YKKGESQ-TDIEItreedftrILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIAR 325
Cdd:cd03334 98 YQRVENKlLSLDP--------VILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549059 326 ACGARIVSRPEEL-REDDVGTgAGLLEIKKIGDEY-----FTFITDCKDPKACTILLRGASKEILSEVERNLQ 392
Cdd:cd03334 170 CTGADIISSMDDLlTSPKLGT-CESFRVRTYVEEHgrsktLMFFEGCPKELGCTILLRGGDLEELKKVKRVVE 241
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
30-517 |
9.50e-11 |
|
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: 64.01 E-value: 9.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 30 AKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHP----AAKSMIEISRTQDEEVGDGTTSVIILAGEM 105
Cdd:cd03344 17 VNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLARAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 106 LSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPvdVNNREMMLSI-INSSITTKVISRwsslacNIAlDAVKTVQ 184
Cdd:cd03344 97 IKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKP--VKTKEEIAQVaTISANGDEEIGE------LIA-EAMEKVG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 185 FE-----ENGRK---EIDIkkyarVEkipgGIIEDscvlRGVMINKDVTHP-RMRRYIKNPRIVLLDssleyKKgesqtd 255
Cdd:cd03344 168 KDgvitvEEGKTletELEV-----VE----GMQFD----RGYLSPYFVTDPeKMEVELENPYILLTD-----KK------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 256 ieITREEDFTRILqmeeeyihqlcEDIIQL-KPDVVITEkgisDLAQHYL-------MRA--NVTAIR-----RVRKTDN 320
Cdd:cd03344 224 --ISSIQELLPIL-----------ELVAKAgRPLLIIAE----DVEGEALatlvvnkLRGglKVCAVKapgfgDRRKAML 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 321 NRIARACGARIVS-----RPEELREDDVGTgAGLLEIKKigdEYFTFITDCKDPKActI-----LLRGASKEILSEVERN 390
Cdd:cd03344 287 EDIAILTGGTVISeelglKLEDVTLEDLGR-AKKVVVTK---DDTTIIGGAGDKAA--IkariaQIRKQIEETTSDYDKE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 391 --------------------------------LQDAMQVCRnVLLDPQLVPGGGASEMAVAHALtEKSKAMTGVEQWPYR 438
Cdd:cd03344 361 klqerlaklsggvavikvggatevelkekkdrVEDALNATR-AAVEEGIVPGGGVALLRASPAL-DKLKALNGDEKLGIE 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549059 439 AVAQALEVIPRTLIQNCGAStirllTSLRAKHTQESCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLL 517
Cdd:cd03344 439 IVRRALEAPLRQIAENAGVD-----GSVVVEKVLESPDGFGYDAATGEYVDMIEAGIIDPTKVVRSALQNAASVASLLL 512
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
32-545 |
1.37e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 63.58 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 32 TIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHP----AAKSMIEISRTQDEEVGDGTTSVIILAGEMLS 107
Cdd:PRK12850 22 ILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 108 VAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVISRWSSLACNIALDAVKTVQFEE 187
Cdd:PRK12850 102 EGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGEMIAEAMDKVGKEGVITVEEAK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 188 NGRKEIDIkkyarVEkipgGIIEDSCVLRGVMinkdVTHP-RMRRYIKNPRIVLldssleykkgesqTDIEITREEDFTR 266
Cdd:PRK12850 182 TLGTELDV-----VE----GMQFDRGYLSPYF----VTNPeKMRAELEDPYILL-------------HEKKISNLQDLLP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 267 ILqmeeeyihqlcEDIIQL-KPDVVITEkgisDLAQHYLMRANVTAIRRV--------------RKTDNNRIARACGARI 331
Cdd:PRK12850 236 IL-----------EAVVQSgRPLLIIAE----DVEGEALATLVVNKLRGGlksvavkapgfgdrRKAMLEDIAVLTGGQV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 332 VS-----RPEELREDDVGTGAGLLeikkIGDEYFTFITDCKDPK---ACTILLR-------------------------- 377
Cdd:PRK12850 301 ISedlgiKLENVTLDMLGRAKRVL----ITKENTTIIDGAGDKKnieARVKQIRaqieettsdydreklqerlaklaggv 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 378 -----GASKEI-LSEVERNLQDAMQVCRnVLLDPQLVPGGGASEMAVAHALTEKsKAMTGVEQWPYRAVAQALEVIPRTL 451
Cdd:PRK12850 377 avirvGGATEVeVKEKKDRVDDALHATR-AAVEEGIVPGGGVALLRARSALRGL-KGANADETAGIDIVRRALEEPLRQI 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 452 IQNCGAStirllTSLRAKHTQESCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGD 531
Cdd:PRK12850 455 ATNAGFE-----GSVVVGKVAELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAA 529
|
570
....*....|....
gi 549059 532 DQNRQTGAPDAGQE 545
Cdd:PRK12850 530 AAAAGPGPGMGGMG 543
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
17-530 |
1.64e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 57.06 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 17 ESGRKVQSGninaAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHP----AAKSMIEISRTQDEEVG 92
Cdd:PRK12851 11 EAREKMLRG----VNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 93 DGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIInSSITTKVISRWSSLA 172
Cdd:PRK12851 87 DGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATI-SANGDAEIGRLVAEA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 173 CN-IALDAVKTVQFEENGRKEIDIkkyarVEkipgGIIEDscvlRGVMINKDVTHP-RMRRYIKNPRIVLLDSsleykkg 250
Cdd:PRK12851 166 MEkVGNEGVITVEESKTAETELEV-----VE----GMQFD----RGYLSPYFVTDAdKMEAELEDPYILIHEK------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 251 esqtdiEITREEDFTRILqmeeeyihqlcEDIIQL-KPDVVITEkgisDLAQHYLMRANVTAIRRV-------------- 315
Cdd:PRK12851 226 ------KISNLQDLLPVL-----------EAVVQSgKPLLIIAE----DVEGEALATLVVNKLRGGlkvaavkapgfgdr 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 316 RKTDNNRIARACGARIVSRPEELREDDVgTGAGLLEIKK--IGDEYFTFITDCKDPKActilLRGASKEILSEVERN--- 390
Cdd:PRK12851 285 RKAMLEDIAILTGGTVISEDLGIKLENV-TLEQLGRAKKvvVEKENTTIIDGAGSKTE----IEGRVAQIRAQIEETtsd 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 391 ------------------------------------LQDAMQVCRnVLLDPQLVPGGGASEMAVAHALTEKsKAMTGVEQ 434
Cdd:PRK12851 360 ydreklqerlaklaggvavirvgastevevkekkdrVDDALHATR-AAVEEGIVPGGGVALLRAVKALDKL-ETANGDQR 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 435 WPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRakhtqESCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAV 514
Cdd:PRK12851 438 TGVEIVRRALEAPVRQIAENAGAEGSVVVGKLR-----EKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAG 512
|
570
....*....|....*.
gi 549059 515 LLLRIDDIVSGHKKKG 530
Cdd:PRK12851 513 LLLTTEAMVAEKPKKE 528
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
33-543 |
2.09e-08 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 56.96 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 33 IADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQV----QHPAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSV 108
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 109 AEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVISRWSSLACNIALDAVKTVQFEEN 188
Cdd:PRK14104 103 GAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFLADAMKKVGNEGVITVEEAKS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 189 GRKEIDIKKYARVEK--IPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKK----------GESQTDI 256
Cdd:PRK14104 183 LETELDVVEGMQFDRgyISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQTGKplvivaedveGEALATL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 257 EITREEDFTRILQMEEEYIHQLCEDIIQlkpDVVITEKG--ISDLAQHYLMRANVTAIRRVRKT----DNNRIARACG-- 328
Cdd:PRK14104 263 VVNRLRGGLKVAAVKAPGFGDRRKAMLQ---DIAILTGGqaISEDLGIKLENVTLQMLGRAKKVmidkENTTIVNGAGkk 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 329 ARIVSRPEELREddvgtgagllEIKKIGDEYFTFITDCKDPK----ACTILLRGASKEILSEVERNLQDAMQVCRnVLLD 404
Cdd:PRK14104 340 ADIEARVAQIKA----------QIEETTSDYDREKLQERLAKlaggVAVIRVGGATEVEVKERKDRVDDAMHATR-AAVE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 405 PQLVPGGGASEMAVAHAL----TEKSKAMTGVEqwpyrAVAQALEVIPRTLIQNCGASTirllTSLRAKHTQESCETWGV 480
Cdd:PRK14104 409 EGIVPGGGVALLRASEQLkgikTKNDDQKTGVE-----IVRKALSAPARQIAINAGEDG----SVIVGKILEKEQYSYGF 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549059 481 NGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGDDQNRQTGAPDAG 543
Cdd:PRK14104 480 DSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGGAGPAMPPGGGMG 542
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
27-542 |
4.23e-08 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 55.69 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 27 INAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPA----AKSMIEISRTQDEEVGDGTTSVIILA 102
Cdd:PTZ00114 28 LKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKAGDGTTTATILA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 103 GEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPvdVNNREMMLSII-----NSSITTKVISRwsslacniAL 177
Cdd:PTZ00114 108 RAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRP--VKTKEDILNVAtisanGDVEIGSLIAD--------AM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 178 DAV---KTVQFEENGRKEIDIKkyarvekipggIIEDSCVLRGVMINKDVTHPRMRRYI-KNPRIVLLDssleyKKGESQ 253
Cdd:PTZ00114 178 DKVgkdGTITVEDGKTLEDELE-----------VVEGMSFDRGYISPYFVTNEKTQKVElENPLILVTD-----KKISSI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 254 TDIeitreedfTRILqmeeEYIHQlcediiQLKPDVVITEKGISDLAQHYL---MRAN--VTAIR-----RVRKTDNNRI 323
Cdd:PTZ00114 242 QSI--------LPIL----EHAVK------NKRPLLIIAEDVEGEALQTLIinkLRGGlkVCAVKapgfgDNRKDILQDI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 324 ARACGARIVSRPEELREDDVGTGAGLLEIKKI---GDEyfTFIT----DCKDPKACTILLRGA--------SKEIL---- 384
Cdd:PTZ00114 304 AVLTGATVVSEDNVGLKLDDFDPSMLGSAKKVtvtKDE--TVILtgggDKAEIKERVELLRSQierttseyDKEKLkerl 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 385 ---------------SEVERN-----LQDAMQVCRNVlLDPQLVPGGGAsemavahALTEKSKAMTGVEQWPYR------ 438
Cdd:PTZ00114 382 aklsggvavikvggaSEVEVNekkdrIEDALNATRAA-VEEGIVPGGGV-------ALLRASKLLDKLEEDNELtpdqrt 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 439 ---AVAQALEVIPRTLIQNCG---ASTIRLLtsLRAKHtqescETWGVNGETGTLVDMKELGIWEPLAVklqtYKTAVET 512
Cdd:PTZ00114 454 gvkIVRNALRLPTKQIAENAGvegAVVVEKI--LEKKD-----PSFGYDAQTGEYVNMFEAGIIDPTKV----VRSALVD 522
|
570 580 590
....*....|....*....|....*....|....
gi 549059 513 AV----LLLRIDDIVSGHKKKgDDQNRQTGAPDA 542
Cdd:PTZ00114 523 AAsvasLMLTTEAAIVDLPKE-KKKNKNSAAPPM 555
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
32-529 |
1.25e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 54.47 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 32 TIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQV----QHPAAKSMIEISRTQDEEVGDGTTSVIILAGEMLS 107
Cdd:PRK12852 22 ILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 108 VAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVISRWSSLACNIALDAVKTVqfEE 187
Cdd:PRK12852 102 EGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGKMIAQAMQKVGNEGVITV--EE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 188 NGRKEIDIKkyarvekipggIIEDSCVLRGVMINKDVTHP-RMRRYIKNPRIVLLDSSL--------------------- 245
Cdd:PRK12852 180 NKSLETEVD-----------IVEGMKFDRGYLSPYFVTNAeKMTVELDDAYILLHEKKLsglqamlpvleavvqsgkpll 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 246 ---EYKKGESQTDIEITREEDFTRILQMEE----EYIHQLCEDIIQLKPDVVITEK-GISdlaqhyLMRANVTAIRRVRK 317
Cdd:PRK12852 249 iiaEDVEGEALATLVVNRLRGGLKVAAVKApgfgDRRKAMLEDIAILTGGQLISEDlGIK------LENVTLKMLGRAKK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 318 T----DNNRIARACG--ARIVSRPEELREddvgtgagllEIKKIGDEYftfitD--------CKDPKACTILLRGASKEI 383
Cdd:PRK12852 323 VvidkENTTIVNGAGkkADIEARVGQIKA----------QIEETTSDY-----DreklqerlAKLAGGVAVIRVGGATEV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 384 -LSEVERNLQDAMQVCRnVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVeQWPYRAVAQALEVIPRTLIQNCGASTIRL 462
Cdd:PRK12852 388 eVKEKKDRVEDALNATR-AAVQEGIVPGGGVALLRAKKAVGRINNDNADV-QAGINIVLKALEAPIRQIAENAGVEGSIV 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549059 463 LTSLRAKHTqescETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKK 529
Cdd:PRK12852 466 VGKILENKS----ETFGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKK 528
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
32-543 |
1.80e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 53.66 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 32 TIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHP----AAKSMIEISRTQDEEVGDGTTSVIILAGEMLS 107
Cdd:PRK12849 21 KLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQALVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 108 VAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDvNNREM----MLSIINSSITTKVISRwsslacniALDAVKT- 182
Cdd:PRK12849 101 EGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVS-GSEEIaqvaTISANGDEEIGELIAE--------AMEKVGKd 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 183 --VQFEENGRKEIDIKkyarvekipggiiedscVLRGVMINKD------VTHP-RMRRYIKNPRIVLLDssleyKKgesq 253
Cdd:PRK12849 172 gvITVEESKTLETELE-----------------VTEGMQFDRGylspyfVTDPeRMEAVLEDPLILLTD-----KK---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 254 tdieITREEDFTRILqmeeeyihqlcEDIIQL-KPDVVITEkgisDLAQHYLMRANVTAIRRV--------------RKT 318
Cdd:PRK12849 226 ----ISSLQDLLPLL-----------EKVAQSgKPLLIIAE----DVEGEALATLVVNKLRGGlkvaavkapgfgdrRKA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 319 DNNRIARACGARIVSRP-----EELREDDVGTgAGLLEIKKigdEYFTFITDCKDPKA---------------------- 371
Cdd:PRK12849 287 MLEDIAILTGGTVISEDlglklEEVTLDDLGR-AKRVTITK---DNTTIVDGAGDKEAiearvaqirrqieettsdydre 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 372 -------------CTILLRGAskeilSEVERN-----LQDAMQVCRnVLLDPQLVPGGGASEMAVAHALTEKSKA----M 429
Cdd:PRK12849 363 klqerlaklaggvAVIKVGAA-----TEVELKerkdrVEDALNATR-AAVEEGIVPGGGVALLRAAKALDELAGLngdqA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 430 TGVeqwpyRAVAQALEVIPRTLIQNCGAStirllTSLRAKHTQESCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTA 509
Cdd:PRK12849 437 AGV-----EIVRRALEAPLRQIAENAGLD-----GSVVVAKVLELEDGFGFNAATGEYGDLIAAGIIDPVKVTRSALQNA 506
|
570 580 590
....*....|....*....|....*....|....
gi 549059 510 VETAVLLLRIDDIVSGHKKKGDDQNRQTGAPDAG 543
Cdd:PRK12849 507 ASVAGLLLTTEALVADKPEEEDPPGGMGGMGGMG 540
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
20-145 |
5.82e-05 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 45.69 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549059 20 RKVQSGninaAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHP----AAKSMIEISRTQDEEVGDGT 95
Cdd:PLN03167 69 KKLQAG----VNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGT 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 549059 96 TSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVD 145
Cdd:PLN03167 145 TTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVE 194
|
|
| |
