|
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: 1005.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:TIGR02344 1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDISDSDMMLNIINSSITTKAI 165
Cdd:TIGR02344 81 TQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 166 SRWSSLACNIALDAVKMVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSL 245
Cdd:TIGR02344 161 SRWSDLMCDLALDAVRTVQRDENGRKEIDIKRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 246 EYKKGESQTDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRVRKTDNNRIAR 325
Cdd:TIGR02344 241 EYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 326 ACGARIVSRPEELREDDVGTGAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDP 405
Cdd:TIGR02344 321 ACGATIVNRPEELRESDVGTGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 406 QLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENCETWGVNGETG 485
Cdd:TIGR02344 401 KLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTWGIDGETG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....
7X0A_g 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: 959.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:cd03337 1 PVLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDISDSDMMLNIINSSITTKAI 165
Cdd:cd03337 81 TQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 166 SRWSSLACNIALDAVKMVQFEENGR-KEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSS 244
Cdd:cd03337 161 SRWSDLMCNLALDAVKTVAVEENGRkKEIDIKRYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 245 LEYkkgesqtdieitreedftrilqmeeeyiqqlcediiqlkpdVVITEKGISDLAQHYLMRANITAIRRVRKTDNNRIA 324
Cdd:cd03337 241 LEY-----------------------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 325 RACGARIVSRPEELREDDVGTGAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLD 404
Cdd:cd03337 280 RACGATIVNRPEELTESDVGTGAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 405 PQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENCETWGVNGET 484
Cdd:cd03337 360 PKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTWGIDGET 439
|
490 500 510 520
....*....|....*....|....*....|....*....|.
7X0A_g 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: 605.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 14 TKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGD 93
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 94 GTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDISDSDMMLNIINSSITTKAISRWSSLAC 173
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 174 NIALDAVKMVQFEENgrkeIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYkkgesq 253
Cdd:cd00309 161 ELVVDAVLKVGKENG----DVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 254 tdieitreedftrilqmeeeyiqqlcediiqlkpdVVITEKGISDLAQHYLMRANITAIRRVRKTDNNRIARACGARIVS 333
Cdd:cd00309 231 -----------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 334 RPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGA 413
Cdd:cd00309 276 RLEDLTPEDLGT-AGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 414 SEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENCeTWGVNGETGTLVDMKEL 493
Cdd:cd00309 355 AEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGG-NAGGDVETGEIVDMKEA 433
|
490 500 510
....*....|....*....|....*....|.
7X0A_g 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: 581.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 33 IADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSVAEHF 112
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 113 LEQQMHPTVVISAYRKALDDMISTLKKI-SIPVDISDSDMMLNIINSSITTKAISRWSSLACNIALDAVKMVqfeENGRK 191
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAI---PKNDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 192 EIDIKKyARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGESQTDIEITREEDFTRILQME 271
Cdd:pfam00118 158 SFDLGN-IGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 272 EEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRVRKTDNNRIARACGARIVSRPEELREDDVGTgAGLLE 351
Cdd:pfam00118 237 EEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGT-AGKVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 352 IKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTG 431
Cdd:pfam00118 316 EEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 432 VEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHtQENCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVE 511
Cdd:pfam00118 396 KEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAH-ASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATE 474
|
490
....*....|...
7X0A_g 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:NF041082 2 PILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDISDSDMMLNIINSSITTKAI 165
Cdd:NF041082 82 TQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 166 SRWSSLACNIALDAVKMVQfEENGRKEIDIkKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSL 245
Cdd:NF041082 162 EAAKDKLADLVVDAVKAVA-EKDGGYNVDL-DNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 246 EYKKGESQTDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRVRKTDNNRIAR 325
Cdd:NF041082 240 EVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 326 ACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDP 405
Cdd:NF041082 320 ATGARIVTSIDDLSPEDLGY-AGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 406 QLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENcETWGVNGETG 485
Cdd:NF041082 399 KVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGN-KTAGLDVYTG 477
|
490 500 510
....*....|....*....|....*....|....*....
7X0A_g 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: 541.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:NF041083 2 PVLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDISDSDMMLNIINSSITTKAI 165
Cdd:NF041083 82 TQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 166 SRWSSLACNIALDAVKMVQFEENGRKEIDIkKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSL 245
Cdd:NF041083 162 EEARDYLAEIAVKAVKQVAEKRDGKYYVDL-DNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 246 EYKKGESQTDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRVRKTDNNRIAR 325
Cdd:NF041083 241 EVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 326 ACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDP 405
Cdd:NF041083 321 ATGARIVTNIDDLTPEDLGY-AELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 406 QLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHtQENCETWGVNGETG 485
Cdd:NF041083 400 KIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAH-EKGKKWAGINVFTG 478
|
490 500 510
....*....|....*....|....*....|....*....
7X0A_g 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: 536.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 7 VLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRT 86
Cdd:cd03343 1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 87 QDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDISDSDMMLNIINSSITTKAIS 166
Cdd:cd03343 81 QDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 167 RWSSLACNIALDAVKMVQFEENGRKEIDIkKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLE 246
Cdd:cd03343 161 AAKDKLADLVVDAVLQVAEKRDGKYVVDL-DNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 247 YKKGESQTDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRVRKTDNNRIARA 326
Cdd:cd03343 240 VKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 327 CGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQ 406
Cdd:cd03343 320 TGAKIVTNIDDLTPEDLGE-AELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 407 LVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENcETWGVNGETGT 486
Cdd:cd03343 399 VVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGN-KNAGLDVYTGE 477
|
490 500 510
....*....|....*....|....*....|....*...
7X0A_g 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 |
8.20e-178 |
|
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: 511.15 E-value: 8.20e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:TIGR02339 1 PVFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDISDSDMMLNIINSSITTKAI 165
Cdd:TIGR02339 81 TQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 166 SRWS-SLACNIALDAVK-MVQFEENGRKEIDIKKyARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDS 243
Cdd:TIGR02339 161 AEVAkDKLADLVVEAVKqVAELRGDGKYYVDLDN-IKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 244 SLEYKKGESQTDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRVRKTDNNRI 323
Cdd:TIGR02339 240 PLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 324 ARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLL 403
Cdd:TIGR02339 320 ARATGARIVSSIDEITESDLGY-AELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 404 DPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENcETWGVNGE 483
Cdd:TIGR02339 399 DGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGN-KNAGINVF 477
|
490 500 510 520
....*....|....*....|....*....|....*....|.
7X0A_g 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 |
6.63e-127 |
|
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: 381.26 E-value: 6.63e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 5 RPVLVL--SQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIE 82
Cdd:cd03339 5 RPFIIVreQEKKKRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 83 ISRTQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDIS--DSDMMLNIINSSI 160
Cdd:cd03339 85 LSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSpdNKEPLIQTAMTSL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 161 TTKAISRWSSLACNIALDAVKMVQFEEngRKEID---IKkyarVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPR 237
Cdd:cd03339 165 GSKIVSRCHRQFAEIAVDAVLSVADLE--RKDVNfelIK----VEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 238 IVLLDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRVRK 317
Cdd:cd03339 239 IAILTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 318 TDNNRIARACGARIVSRPEELREDDVGTgAGLLEIKKIG--DEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAM 395
Cdd:cd03339 319 VEIELIAIATGGRIVPRFEDLSPEKLGK-AGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDAL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 396 QVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENC 475
Cdd:cd03339 398 CVVRNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKN 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
7X0A_g 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 |
1.77e-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: 377.40 E-value: 1.77e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 14 TKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGD 93
Cdd:cd03338 1 TDKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 94 GTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDISDSDMMLNIINSSITTKAISRWSSLAC 173
Cdd:cd03338 81 GTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 174 NIALDAVKMVqFEENGRKEIDIKKYARVEKIpGGIIEDSCVLRGVMINKDVTH-PRMRRYIKNPRIVLLDSSLEYKKGES 252
Cdd:cd03338 161 PIAVDAVLKV-IDPATATNVDLKDIRIVKKL-GGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 253 QTDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGI-----SDLAQHYLMRANITAIRRVRKTDNNRIARAC 327
Cdd:cd03338 239 DNNIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 328 GARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDP-KACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQ 406
Cdd:cd03338 319 GCKPVASIDHFTEDKLGS-ADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 407 LVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENCeTWGVNGETGT 486
Cdd:cd03338 398 LIPGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEK-NAGINVRKGA 476
|
490 500 510
....*....|....*....|....*....|....*..
7X0A_g 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 |
1.00e-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: 373.16 E-value: 1.00e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:cd03340 1 PIILLKEGTDTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDISDSD----MMLNIINSSIT 161
Cdd:cd03340 81 SQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKEeqreLLEKCAATALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 162 TKAISRWSSLACNIALDAVKMVQfEENGRKEIDIKKyarvekIPGGIIEDSCVLRGVMINKDVT---HPRMRRYIKNPRI 238
Cdd:cd03340 161 SKLIASEKEFFAKMVVDAVLSLD-DDLDLDMIGIKK------VPGGSLEDSQLVNGVAFKKTFSyagFEQQPKKFKNPKI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 239 VLLDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRVRKT 318
Cdd:cd03340 234 LLLNVELELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 319 DNNRIARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVC 398
Cdd:cd03340 314 DLKRVAQATGGSIQTTVSNITDDVLGT-CGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 399 RNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENCETW 478
Cdd:cd03340 393 RRAIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKWY 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
7X0A_g 479 GVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:cd03340 473 GVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLILSVDETI 517
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
6-523 |
1.00e-120 |
|
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: 365.62 E-value: 1.00e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:TIGR02345 3 TIVLLKEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDISDSD---MMLNIINSSITT 162
Cdd:TIGR02345 83 SQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKGEqreLLEKCAATALSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 163 KAISRWSSLACNIALDAVKMVQFEENGRKEIDIKkyarveKIPGGIIEDSCVLRGVMINKDVT---HPRMRRYIKNPRIV 239
Cdd:TIGR02345 163 KLISHNKEFFSKMIVDAVLSLDRDDLDLKLIGIK------KVQGGALEDSQLVNGVAFKKTFSyagFEQQPKKFANPKIL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 240 LLDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRVRKTD 319
Cdd:TIGR02345 237 LLNVELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 320 NNRIARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCR 399
Cdd:TIGR02345 317 LKRVIKACGGSIQSTTSDLEADVLGT-CALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 400 NVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENCetW- 478
Cdd:TIGR02345 396 RALKNKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGK--Wy 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
7X0A_g 479 GVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:TIGR02345 474 GVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETI 518
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
5-524 |
7.49e-120 |
|
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: 363.74 E-value: 7.49e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 5 RPVLVLSQ--NTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIE 82
Cdd:TIGR02343 9 RPFIIIKDqdNKKRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 83 ISRTQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKIS--IPVDISDSDMMLNIINSSI 160
Cdd:TIGR02343 89 LSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISdeISADNNNREPLIQAAKTSL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 161 TTKAISRWSSLACNIALDAVKMVQFEEngRKEIDIkKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVL 240
Cdd:TIGR02343 169 GSKIVSKCHRRFAEIAVDAVLNVADME--RRDVDF-DLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 241 LDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRVRKTDN 320
Cdd:TIGR02343 246 LTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQEL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 321 NRIARACGARIVSRPEELREDDVGTgAGLLEIKKIG--DEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVC 398
Cdd:TIGR02343 326 ELIAIATGGRIVPRFQELSKDKLGK-AGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 399 RNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENCETW 478
Cdd:TIGR02343 405 RNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNL 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
7X0A_g 479 GVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:TIGR02343 485 GVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVIS 530
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
15-523 |
1.21e-113 |
|
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: 347.35 E-value: 1.21e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 15 KRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDG 94
Cdd:cd03335 2 ERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 95 TTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKK-ISIPVDISDSDMMLNIINSSITTKAISRWSSLAC 173
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDNLGKESLINVAKTSMSSKIIGADSDFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 174 NIALDAVKMVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGESQ 253
Cdd:cd03335 162 NMVVDAILAVKTTNEKGKTKYPIKAVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 254 TDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRVRKTDNNRIARACGARIVS 333
Cdd:cd03335 242 VQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 334 RPEELREDDVGTGAGL-----LEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLV 408
Cdd:cd03335 322 TLANLEGEETFDPSYLgeaeeVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 409 PGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKH-------TQENCETWGVN 481
Cdd:cd03335 402 PGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHaaaqvkpDKKHLKWYGLD 481
|
490 500 510 520
....*....|....*....|....*....|....*....|..
7X0A_g 482 GETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:cd03335 482 LINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLI 523
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
16-523 |
1.28e-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: 347.16 E-value: 1.28e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 16 RESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGT 95
Cdd:TIGR02342 4 KDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 96 TSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDISDSDMMLNIINSSITTKAISRWSSLACNI 175
Cdd:TIGR02342 84 TSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 176 ALDAVKMVQFEENGrKEIDIKKYARVEKIpGGIIEDSCVLRGVMINKDVTHPR-MRRYIKNPRIVLLDSSLEYKKGESQT 254
Cdd:TIGR02342 164 AVDAVLKVIDPENA-KNVDLNDIKVVKKL-GGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDMEN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 255 DIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGI-----SDLAQHYLMRANITAIRRVRKTDNNRIARACGA 329
Cdd:TIGR02342 242 QIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGC 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 330 RIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDP-KACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLV 408
Cdd:TIGR02342 322 KPIASIDHFTADKLGS-AELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 409 PGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENcETWGVNGETGTLV 488
Cdd:TIGR02342 401 AGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGE-KTAGISVRKGGIT 479
|
490 500 510
....*....|....*....|....*....|....*
7X0A_g 489 DMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:TIGR02342 480 NMLEEHVLQPLLVTTSAITLASETVRSILKIDDIV 514
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
15-532 |
1.48e-113 |
|
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: 347.48 E-value: 1.48e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 15 KRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDG 94
Cdd:TIGR02340 6 ERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 95 TTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKK-ISIPVDISDSDMMLNIINSSITTKAISRWSSLAC 173
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDELGREALINVAKTSMSSKIIGLDSDFFS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 174 NIALDAVKMVQFE-ENGRKEIDIKKyARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGES 252
Cdd:TIGR02340 166 NIVVDAVLAVKTTnENGETKYPIKA-INILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAKMAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 253 QTDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRVRKTDNNRIARACGARIV 332
Cdd:TIGR02340 245 GVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 333 SRPEELREDDVGTGAGL-----LEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQL 407
Cdd:TIGR02340 325 STLADLEGEETFEASYLgfadeVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 408 VPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKH-------TQENCETWGV 480
Cdd:TIGR02340 405 VPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHaaaqlkpEKKHLKWYGL 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
7X0A_g 481 NGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGDD 532
Cdd:TIGR02340 485 DLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIKLNPEQSKG 536
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
19-533 |
1.55e-109 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 335.89 E-value: 1.55e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 19 GRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHP----AAKSMIEISRTQDEEVGDG 94
Cdd:COG0459 8 GEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 95 TTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDisDSDMMLNIINSSITTKAisrwsSLAcN 174
Cdd:COG0459 88 TTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVD--DKEELAQVATISANGDE-----EIG-E 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 175 IALDAVKMVqfeengRKEIDIKkyarVEKiPGGIIEDSCVLRGVMINKDVTHP-------RMRRYIKNPRIVLLDSsley 247
Cdd:COG0459 160 LIAEAMEKV------GKDGVIT----VEE-GKGLETELEVVEGMQFDKGYLSPyfvtdpeKMPAELENAYILLTDK---- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 248 kkgesqtdiEITREEDFTRILqmeeeyiqqlcEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRV-----------R 316
Cdd:COG0459 225 ---------KISSIQDLLPLL-----------EKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgdrR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 317 KTDNNRIARACGARIVSR-----PEELREDDVGTgAGLLEikkIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNL 391
Cdd:COG0459 285 KAMLEDIAILTGGRVISEdlglkLEDVTLDDLGR-AKRVE---VDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 392 QDAMQVCRNVLLDpQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKht 471
Cdd:COG0459 361 EDALHATRAAVEE-GIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA-- 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
7X0A_g 472 qeNCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGDDQ 533
Cdd:COG0459 438 --KDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
26-523 |
4.79e-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: 318.01 E-value: 4.79e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 26 NINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEM 105
Cdd:cd03341 13 NIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 106 LSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIP--VDISDSDMMLNIINSSITTKAISRwSSLACNIALDAVKMV 183
Cdd:cd03341 93 LEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYkiEDLRNKEEVSKALKTAIASKQYGN-EDFLSPLVAEACISV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 184 QFEENGRKEIDikkYARVEKIPGGIIEDSCVLRGVMINKD----VTHprmrryIKNPRIVLLDSSLEykkgesqtdieit 259
Cdd:cd03341 172 LPENIGNFNVD---NIRVVKILGGSLEDSKVVRGMVFKREpegsVKR------VKKAKVAVFSCPFD------------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 260 reedftrilqmeeeyiqqlcediiqLKPDVVITEKGISDLAQHYLMRANITAIRRVRKTDNNRIARACGARIVSR----- 334
Cdd:cd03341 230 -------------------------IGVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRlgapt 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 335 PEELREDDVgtgaglLEIKKIGDEYFTFITDCK-DPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGA 413
Cdd:cd03341 285 PEEIGYCDS------VYVEEIGDTKVVVFRQNKeDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 414 SEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENCETwGVNGETG--TLVDMK 491
Cdd:cd03341 359 TEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSA-GVDIESGdeGTKDAK 437
|
490 500 510
....*....|....*....|....*....|..
7X0A_g 492 ELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:cd03341 438 EAGIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
13-523 |
2.16e-101 |
|
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: 314.20 E-value: 2.16e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 13 NTKRESGRKVQS--GNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAkSMIEISRT-QDE 89
Cdd:cd03342 2 NPKAEVLRRGQAlaVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTA-SMIARAATaQDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 90 EVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDIS-DSDMMLNIINSSITTKAISRW 168
Cdd:cd03342 81 ITGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDtDRELLLSVARTSLRTKLHADL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 169 SSLACNIALDAVKMVQFEEngrKEIDIKKyarVE--KIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLE 246
Cdd:cd03342 161 ADQLTEIVVDAVLAIYKPD---EPIDLHM---VEimQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 247 YKKGESQTdieitreedftrilqmeeeyiqqlcediiQLKPDVVITEKGISDLAQHYLMRANITAIRRVRKTDNNRIARA 326
Cdd:cd03342 235 YEKTEVNS-----------------------------GFFYSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 327 CGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQ 406
Cdd:cd03342 286 CGGVAMNSVDDLSPECLGY-AGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKC 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 407 LVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTqENCETWGVNGETGT 486
Cdd:cd03342 365 VVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYA-EGGQVGGVDLDTGE 443
|
490 500 510
....*....|....*....|....*....|....*..
7X0A_g 487 LVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:cd03342 444 PMDPESEGIWDNYSVKRQILHSATVIASQLLLVDEII 480
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-524 |
9.94e-97 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 303.87 E-value: 9.94e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 1 MMGHRPVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKmLLDPM------GGIVMTNDGNAILREIQVQH 74
Cdd:PTZ00212 2 IMANVPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDK-ILQPMsegprsGNVTVTNDGATILKSVWLDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 75 PAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDiSDSDM--- 151
Cdd:PTZ00212 81 PAAKILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHG-SDEEKfke 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 152 -MLNIINSSITTKAISRWSSLACNIALDAVKMVqfeeNGRKEIDikkYARVEKIPGGIIEDSCVLRGVMINKDVThPRMR 230
Cdd:PTZ00212 160 dLLNIARTTLSSKLLTVEKDHFAKLAVDAVLRL----KGSGNLD---YIQIIKKPGGTLRDSYLEDGFILEKKIG-VGQP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 231 RYIKNPRIVLLDSSLEYKKgesqtdIEI----TREEDFTRILQMEE---EYIQQLCEDIIQLKPDVVITEKGISDLAQHY 303
Cdd:PTZ00212 232 KRLENCKILVANTPMDTDK------IKIygakVKVDSMEKVAEIEAaekEKMKNKVDKILAHGCNVFINRQLIYNYPEQL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 304 LMRANITAIRRVRKTDNNRIARACGARIVSRPEELREDDVGTGAGLLEIkKIGDEYFTFITDCKDPKACTILLRGASKEI 383
Cdd:PTZ00212 306 FAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEI-MIGEDKLIRFSGCAKGEACTIVLRGASTHI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 384 LSEVERNLQDAMQVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLL 463
Cdd:PTZ00212 385 LDEAERSLHDALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELV 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
7X0A_g 464 TSLRAKHTQENcETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:PTZ00212 465 SKLRAEHYKGN-KTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIR 524
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
13-523 |
7.01e-96 |
|
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: 301.65 E-value: 7.01e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 13 NTKRESGRKVQS--GNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEE 90
Cdd:TIGR02347 6 NPKAESLRRDAAlmMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 91 VGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPV-DISDSDMMLNIINSSITTKAISRWS 169
Cdd:TIGR02347 86 TGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKeDEVDREFLLNVARTSLRTKLPADLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 170 SLACNIALDAVKMVQFEEngrKEID---IKKYARVEKIPggiiEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLE 246
Cdd:TIGR02347 166 DQLTEIVVDAVLAIKKDG---EDIDlfmVEIMEMKHKSA----TDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 247 YKKGESQTDIEITREEDFTRILQMEEEYIQQLCEDIIQLK-------PD---VVITEKGISDLAQHYLMRANITAIRRVR 316
Cdd:TIGR02347 239 YEKTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKkkvcgksPDkgfVVINQKGIDPPSLDLLAKEGIMALRRAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 317 KTDNNRIARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQ 396
Cdd:TIGR02347 319 RRNMERLTLACGGEALNSVEDLTPECLGW-AGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 397 VCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTqENCE 476
Cdd:TIGR02347 398 AVKNAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHD-EGGE 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
7X0A_g 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 |
1.23e-94 |
|
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: 298.09 E-value: 1.23e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 9 VLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLL--DPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRT 86
Cdd:cd03336 1 ILKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILQsvGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 87 QDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDiSDSDM----MLNIINSSITT 162
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHS-SDEEAfredLLNIARTTLSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 163 KAISRWSSLACNIALDAVkmvqFEENGRKEIDikkYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRyIKNPRIVLLD 242
Cdd:cd03336 160 KILTQDKEHFAELAVDAV----LRLKGSGNLD---AIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQPKR-IENAKILIAN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 243 SSLEYKKgesqtdIEI----TREEDFTRILQMEE---EYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRV 315
Cdd:cd03336 232 TPMDTDK------IKIfgakVRVDSTAKVAEIEEaekEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 316 RKTDNNRIARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAM 395
Cdd:cd03336 306 DFDGVERLALVTGGEIASTFDHPELVKLGT-CKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 396 QVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENC 475
Cdd:cd03336 385 CVLAQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNT 464
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
7X0A_g 476 eTWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 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 ... |
26-544 |
2.89e-91 |
|
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: 289.69 E-value: 2.89e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 26 NINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEM 105
Cdd:TIGR02346 23 NIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 106 LSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISI--PVDISDSDMMLNIINSSITTKAISRWSSLACNIAlDAVKMV 183
Cdd:TIGR02346 103 LNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVweVKDLRDKDELIKALKASISSKQYGNEDFLAQLVA-QACSTV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 184 QFEENGRKEIDikkYARVEKIPGGIIEDSCVLRGVMINKDvTHPRMRRyIKNPRIVLLDSSLEYKKGESQTDIEITREED 263
Cdd:TIGR02346 182 LPKNPQNFNVD---NIRVCKILGGSLSNSEVLKGMVFNRE-AEGSVKS-VKNAKVAVFSCPLDTATTETKGTVLIHNAEE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 264 FTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRVRKTDNNRIARACGARIVSR-----PEEL 338
Cdd:TIGR02346 257 LLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRlgaptPEEI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 339 REDDVgtgaglLEIKKIGDEYFT-FITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGASEMA 417
Cdd:TIGR02346 337 GYVDS------VYVSEIGGDKVTvFKQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 418 VAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHtQENCETWGVN--GETGTLVDMKELGI 495
Cdd:TIGR02346 411 LASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAH-KKGNKSKGIDieAESDGVKDASEAGI 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
7X0A_g 496 WEPLAVKLQTYKTAVETAVLLLRIDDIVsghkkkgddQSRQGGAPDAGQ 544
Cdd:TIGR02346 490 YDMLATKKWAIKLATEAAVTVLRVDQII---------MAKPAGGPKPPQ 529
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
150-404 |
1.56e-77 |
|
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: 243.14 E-value: 1.56e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 150 DMMLNIINSSITTKaISRWSSLACNIALDAVKMVQFEENgrkeIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRM 229
Cdd:cd03333 2 ELLLQVATTSLNSK-LSSWDDFLGKLVVDAVLKVGPDNR----MDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 230 RRYIKNPRIVLLDSSLEYkkgesqtdieitreedftrilqmeeeyiqqlcediiqlkpdVVITEKGISDLAQHYLMRANI 309
Cdd:cd03333 77 PKRLENAKILLLDCPLEY-----------------------------------------VVIAEKGIDDLALHYLAKAGI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 310 TAIRRVRKTDNNRIARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVER 389
Cdd:cd03333 116 MAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGT-AELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKR 194
|
250
....*....|....*
7X0A_g 390 NLQDAMQVCRNVLLD 404
Cdd:cd03333 195 SLHDALCAVRAAVEE 209
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
9-523 |
2.65e-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: 237.06 E-value: 2.65e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 9 VLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLL--DPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRT 86
Cdd:TIGR02341 2 IFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 87 QDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIpvDISDSDMM-----LNIINSSIT 161
Cdd:TIGR02341 82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAV--DNGSDEVKfrqdlMNIARTTLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 162 TKAISRWSSLACNIALDAVKMVQfeenGRKEIDikkYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRyIKNPRIVLL 241
Cdd:TIGR02341 160 SKILSQHKDHFAQLAVDAVLRLK----GSGNLE---AIQIIKKLGGSLADSYLDEGFLLDKKIGVNQPKR-IENAKILIA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 242 DSSLEYKKGES-QTDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRVRKTDN 320
Cdd:TIGR02341 232 NTGMDTDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 321 NRIARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRN 400
Cdd:TIGR02341 312 ERLALVTGGEIVSTFDHPELVKLGS-CDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 401 VLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENcETWGV 480
Cdd:TIGR02341 391 TVKESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGN-TTMGL 469
|
490 500 510 520
....*....|....*....|....*....|....*....|...
7X0A_g 481 NGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:TIGR02341 470 DMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNII 512
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
167-392 |
2.78e-46 |
|
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: 162.78 E-value: 2.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 167 RWSSLACNIALDAVKMVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLE 246
Cdd:cd03334 18 SWLDILLPLVWKAASNVKPDVRAGDDMDIRQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 247 YKKGESQ-TDIEItreedftrILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRVRKTDNNRIAR 325
Cdd:cd03334 98 YQRVENKlLSLDP--------VILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
7X0A_g 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 |
2.60e-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: 65.94 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 30 AKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHP----AAKSMIEISRTQDEEVGDGTTSVIILAGEM 105
Cdd:cd03344 17 VNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLARAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 106 LSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVdiSDSDMMLNI-INSSITTKAISRwsslacNIAlDAVKMVQ 184
Cdd:cd03344 97 IKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPV--KTKEEIAQVaTISANGDEEIGE------LIA-EAMEKVG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 185 FE-----ENGRK---EIDIkkyarVEkipgGIIEDscvlRGVMINKDVTHP-RMRRYIKNPRIVLLDssleyKKgesqtd 255
Cdd:cd03344 168 KDgvitvEEGKTletELEV-----VE----GMQFD----RGYLSPYFVTDPeKMEVELENPYILLTD-----KK------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 256 ieITREEDFTRILqmeeeyiqqlcEDIIQL-KPDVVITEkgisDLAQHYL-------MRA--NITAIR-----RVRKTDN 320
Cdd:cd03344 224 --ISSIQELLPIL-----------ELVAKAgRPLLIIAE----DVEGEALatlvvnkLRGglKVCAVKapgfgDRRKAML 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 321 NRIARACGARIVS-----RPEELREDDVGTgAGLLEIKKigdEYFTFITDCKDPKActI-----LLRGASKEILSEVERN 390
Cdd:cd03344 287 EDIAILTGGTVISeelglKLEDVTLEDLGR-AKKVVVTK---DDTTIIGGAGDKAA--IkariaQIRKQIEETTSDYDKE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 391 --------------------------------LQDAMQVCRnVLLDPQLVPGGGASEMAVAHALtEKSKAMTGVEQWPYR 438
Cdd:cd03344 361 klqerlaklsggvavikvggatevelkekkdrVEDALNATR-AAVEEGIVPGGGVALLRASPAL-DKLKALNGDEKLGIE 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7X0A_g 439 AVAQALEVIPRTLIQNCGAStirllTSLRAKHTQENCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLL 517
Cdd:cd03344 439 IVRRALEAPLRQIAENAGVD-----GSVVVEKVLESPDGFGYDAATGEYVDMIEAGIIDPTKVVRSALQNAASVASLLL 512
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
32-545 |
1.27e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 63.97 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 32 TIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHP----AAKSMIEISRTQDEEVGDGTTSVIILAGEMLS 107
Cdd:PRK12850 22 ILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 108 VAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDisdsdmmlniinssiTTKAISRWSSLACN--------IAlDA 179
Cdd:PRK12850 102 EGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVT---------------SSKEIAQVATISANgdesigemIA-EA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 180 VKMVQFE-----ENGRK---EIDIkkyarVEkipgGIIEDSCVLRGVMinkdVTHP-RMRRYIKNPRIVLldssleykkg 250
Cdd:PRK12850 166 MDKVGKEgvitvEEAKTlgtELDV-----VE----GMQFDRGYLSPYF----VTNPeKMRAELEDPYILL---------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 251 esqTDIEITREEDFTRILqmeeeyiqqlcEDIIQL-KPDVVITEKgISDLAQHYLMRANITAIRRV-----------RKT 318
Cdd:PRK12850 223 ---HEKKISNLQDLLPIL-----------EAVVQSgRPLLIIAED-VEGEALATLVVNKLRGGLKSvavkapgfgdrRKA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 319 DNNRIARACGARIVS-----RPEELREDDVGTGAGLLeikkIGDEYFTFITDCKDPK---ACTILLR------------- 377
Cdd:PRK12850 288 MLEDIAVLTGGQVISedlgiKLENVTLDMLGRAKRVL----ITKENTTIIDGAGDKKnieARVKQIRaqieettsdydre 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 378 ------------------GASKEI-LSEVERNLQDAMQVCRnVLLDPQLVPGGGASEMAVAHALTEKsKAMTGVEQWPYR 438
Cdd:PRK12850 364 klqerlaklaggvavirvGGATEVeVKEKKDRVDDALHATR-AAVEEGIVPGGGVALLRARSALRGL-KGANADETAGID 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 439 AVAQALEVIPRTLIQNCGAStirllTSLRAKHTQENCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLR 518
Cdd:PRK12850 442 IVRRALEEPLRQIATNAGFE-----GSVVVGKVAELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLIT 516
|
570 580
....*....|....*....|....*..
7X0A_g 519 IDDIVSGHKKKGDDQSRQGGAPDAGQE 545
Cdd:PRK12850 517 TEAMVAEAPKKAAAAAAGPGPGMGGMG 543
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
32-543 |
1.37e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 57.51 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 32 TIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHP----AAKSMIEISRTQDEEVGDGTTSVIILAGEMLS 107
Cdd:PRK12849 21 KLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQALVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 108 VAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVdiSDSDMMLNIINSS---------ITTKAISRwsslacnIALD 178
Cdd:PRK12849 101 EGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPV--SGSEEIAQVATISangdeeigeLIAEAMEK-------VGKD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 179 AVKMVqfEENGRKEIDIKkyarvekipggiiedscVLRGVMINKD------VTHP-RMRRYIKNPRIVLLDssleyKKge 251
Cdd:PRK12849 172 GVITV--EESKTLETELE-----------------VTEGMQFDRGylspyfVTDPeRMEAVLEDPLILLTD-----KK-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 252 sqtdieITREEDFTRILqmeeEYIQQlcediiQLKPDVVITEkgisDLAQHYLMRANITAIRRV--------------RK 317
Cdd:PRK12849 226 ------ISSLQDLLPLL----EKVAQ------SGKPLLIIAE----DVEGEALATLVVNKLRGGlkvaavkapgfgdrRK 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 318 TDNNRIARACGARIVSRP-----EELREDDVGTgAGLLEIKKigdEYFTFITDCKDPKA--------------------- 371
Cdd:PRK12849 286 AMLEDIAILTGGTVISEDlglklEEVTLDDLGR-AKRVTITK---DNTTIVDGAGDKEAiearvaqirrqieettsdydr 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 372 --------------CTILLRGAskeilSEVERN-----LQDAMQVCRnVLLDPQLVPGGGASEMAVAHALTEKSKA---- 428
Cdd:PRK12849 362 eklqerlaklaggvAVIKVGAA-----TEVELKerkdrVEDALNATR-AAVEEGIVPGGGVALLRAAKALDELAGLngdq 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 429 MTGVeqwpyRAVAQALEVIPRTLIQNCGAStirllTSLRAKHTQENCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKT 508
Cdd:PRK12849 436 AAGV-----EIVRRALEAPLRQIAENAGLD-----GSVVVAKVLELEDGFGFNAATGEYGDLIAAGIIDPVKVTRSALQN 505
|
570 580 590
....*....|....*....|....*....|....*
7X0A_g 509 AVETAVLLLRIDDIVSGHKKKGDDQSRQGGAPDAG 543
Cdd:PRK12849 506 AASVAGLLLTTEALVADKPEEEDPPGGMGGMGGMG 540
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
27-155 |
1.82e-08 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 56.84 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 27 INAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPA----AKSMIEISRTQDEEVGDGTTSVIILA 102
Cdd:PTZ00114 28 LKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKAGDGTTTATILA 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
7X0A_g 103 GEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVdiSDSDMMLNI 155
Cdd:PTZ00114 108 RAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPV--KTKEDILNV 158
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
17-545 |
1.51e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 53.98 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 17 ESGRKVQSGninaAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHP----AAKSMIEISRTQDEEVG 92
Cdd:PRK12851 11 EAREKMLRG----VNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 93 DGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDISDSDMMLNIInSSITTKAISRWSSLA 172
Cdd:PRK12851 87 DGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATI-SANGDAEIGRLVAEA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 173 CN-IALDAVKMVQFEENGRKEIDIkkyarVEkipgGIIEDscvlRGVMINKDVTHP-RMRRYIKNPRIVLLDSsleykkg 250
Cdd:PRK12851 166 MEkVGNEGVITVEESKTAETELEV-----VE----GMQFD----RGYLSPYFVTDAdKMEAELEDPYILIHEK------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 251 esqtdiEITREEDFTRILqmeeeyiqqlcEDIIQL-KPDVVITEKgISDLAQHYLMRANITAIRRV-----------RKT 318
Cdd:PRK12851 226 ------KISNLQDLLPVL-----------EAVVQSgKPLLIIAED-VEGEALATLVVNKLRGGLKVaavkapgfgdrRKA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 319 DNNRIARACGARIVSRPEELREDDVgTGAGLLEIKK--IGDEYFTFITDCKDPKActilLRGASKEILSEVERN------ 390
Cdd:PRK12851 288 MLEDIAILTGGTVISEDLGIKLENV-TLEQLGRAKKvvVEKENTTIIDGAGSKTE----IEGRVAQIRAQIEETtsdydr 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 391 ---------------------------------LQDAMQVCRnVLLDPQLVPGGGASEMAVAHALTEKsKAMTGVEQWPY 437
Cdd:PRK12851 363 eklqerlaklaggvavirvgastevevkekkdrVDDALHATR-AAVEEGIVPGGGVALLRAVKALDKL-ETANGDQRTGV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 438 RAVAQALEVIPRTLIQNCGASTIRLLTSLRakhtqENCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLL 517
Cdd:PRK12851 441 EIVRRALEAPVRQIAENAGAEGSVVVGKLR-----EKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLL 515
|
570 580
....*....|....*....|....*...
7X0A_g 518 RIDDIVSGHKKKGDDQSRQggaPDAGQE 545
Cdd:PRK12851 516 TTEAMVAEKPKKEPAPPAP---PGGGMD 540
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
32-545 |
2.70e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 53.31 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 32 TIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQV----QHPAAKSMIEISRTQDEEVGDGTTSVIILAGEMLS 107
Cdd:PRK12852 22 ILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 108 VAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDISDSDMMLNIInSSITTKAISRWSSLACN-IALDAVKMVqfE 186
Cdd:PRK12852 102 EGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTI-SANGDAAIGKMIAQAMQkVGNEGVITV--E 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 187 ENGRKEIDIKkyarvekipggIIEDSCVLRGVMINKDVTHP-RMRRYIKNPRIVLLDSSL-------------------- 245
Cdd:PRK12852 179 ENKSLETEVD-----------IVEGMKFDRGYLSPYFVTNAeKMTVELDDAYILLHEKKLsglqamlpvleavvqsgkpl 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 246 ----EYKKGESQTDIEITREEDFTRILQMEE----EYIQQLCEDIIQLKPDVVITEK-GISdlaqhyLMRANITAIRRVR 316
Cdd:PRK12852 248 liiaEDVEGEALATLVVNRLRGGLKVAAVKApgfgDRRKAMLEDIAILTGGQLISEDlGIK------LENVTLKMLGRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 317 KT----DNNRIARACG--ARIVSRPEELREddvgtgagllEIKKIGDEYftfitD--------CKDPKACTILLRGASKE 382
Cdd:PRK12852 322 KVvidkENTTIVNGAGkkADIEARVGQIKA----------QIEETTSDY-----DreklqerlAKLAGGVAVIRVGGATE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 383 I-LSEVERNLQDAMQVCRnVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVeQWPYRAVAQALEVIPRTLIQNCGASTIR 461
Cdd:PRK12852 387 VeVKEKKDRVEDALNATR-AAVQEGIVPGGGVALLRAKKAVGRINNDNADV-QAGINIVLKALEAPIRQIAENAGVEGSI 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 462 LLTSLRAKHTqencETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGDDQSRQGGAPD 541
Cdd:PRK12852 465 VVGKILENKS----ETFGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDAAPAMPAGGGM 540
|
....
7X0A_g 542 AGQE 545
Cdd:PRK12852 541 GGMG 544
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
33-543 |
4.01e-06 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 49.64 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 33 IADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQV----QHPAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSV 108
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 109 AEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDISDSDMMLNIINSSITTKAISRWSSLACNIALDAVKMVQFEEN 188
Cdd:PRK14104 103 GAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFLADAMKKVGNEGVITVEEAKS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 189 GRKEIDIKKYARVEK--IPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKK----------GESQTDI 256
Cdd:PRK14104 183 LETELDVVEGMQFDRgyISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQTGKplvivaedveGEALATL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 257 EITREEDFTRILQMEEEYIQQLCEDIIQlkpDVVITEKG--ISDLAQHYLMRANITAIRRVRKT----DNNRIARACG-- 328
Cdd:PRK14104 263 VVNRLRGGLKVAAVKAPGFGDRRKAMLQ---DIAILTGGqaISEDLGIKLENVTLQMLGRAKKVmidkENTTIVNGAGkk 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 329 ARIVSRPEELREddvgtgagllEIKKIGDEYFTFITDCKDPK----ACTILLRGASKEILSEVERNLQDAMQVCRnVLLD 404
Cdd:PRK14104 340 ADIEARVAQIKA----------QIEETTSDYDREKLQERLAKlaggVAVIRVGGATEVEVKERKDRVDDAMHATR-AAVE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 405 PQLVPGGGASEMAVAHAL----TEKSKAMTGVEqwpyrAVAQALEVIPRTLIQNCGASTirllTSLRAKHTQENCETWGV 480
Cdd:PRK14104 409 EGIVPGGGVALLRASEQLkgikTKNDDQKTGVE-----IVRKALSAPARQIAINAGEDG----SVIVGKILEKEQYSYGF 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
7X0A_g 481 NGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGDdqsrQGGAPDAG 543
Cdd:PRK14104 480 DSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGG----AGPAMPPG 538
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
20-148 |
7.58e-06 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 48.77 E-value: 7.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 20 RKVQSGninaAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHP----AAKSMIEISRTQDEEVGDGT 95
Cdd:PLN03167 69 KKLQAG----VNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGT 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
7X0A_g 96 TSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDISD 148
Cdd:PLN03167 145 TTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSE 197
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
408-543 |
6.97e-03 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 38.95 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7X0A_g 408 VPGGGASEMAVAHALtEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCG--ASTIrlltslRAKHTQENCETWGVNGETG 485
Cdd:PRK00013 411 VPGGGVALLRAAPAL-EALKGLNGDEATGINIVLRALEAPLRQIAENAGleGSVV------VEKVKNGKGKGYGYNAATG 483
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
7X0A_g 486 TLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGDDQSRQGGAPDAG 543
Cdd:PRK00013 484 EYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAAAPPMGGGGMGG 541
|
|
| |
