|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
7-525 |
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: 802.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 7 VLVFKPSLKKESDRKAQLATIQASRALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPAAKSLIELSRS 86
Cdd:cd03337 2 VLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 87 QDEEVGDGTTSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDLNNEEAVKDVIQSSLETKFSS 166
Cdd:cd03337 82 QDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 167 RWGNLIASLALSAVQKVKLTRPDGRTVIDIKRYAKVEKLPGGMPEDSVVLDGILVNKDVTHPSMARRVENPRVLILDCTL 246
Cdd:cd03337 162 RWSDLMCNLALDAVKTVAVEENGRKKEIDIKRYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 247 EYkkgesqtivdisdeagwaklleqeeteifnmcqniiqtgcnVVVTEKGVSDLAQHFLSKAGISCIRRVRKTDANRLSR 326
Cdd:cd03337 242 EY-----------------------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIAR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 327 VTGATIVNRTEELLPSDVGTGCGLFEVKKIGDEYFSYFIQCKDPKACSIVLRGSSKDVLNEIERNLQDALNVCRNIMLEG 406
Cdd:cd03337 281 ACGATIVNRPEELTESDVGTGAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILNP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 407 KLLPGGGATEIEVACRLAAKLDSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHV-AGNVNAGLDGETG 485
Cdd:cd03337 361 KLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAqGENSTWGIDGETG 440
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1624722677 486 EICDTMKKRIFDTYTVKAQIFKSAIEAACMLLRIDMIVSG 525
Cdd:cd03337 441 DIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIVSG 480
|
|
| 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: 798.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 6 TVLVFKPSLKKESDRKAQLATIQASRALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPAAKSLIELSR 85
Cdd:TIGR02344 1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 86 SQDEEVGDGTTSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDLNNEEAVKDVIQSSLETKFS 165
Cdd:TIGR02344 81 TQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 166 SRWGNLIASLALSAVQKVKLTRpDGRTVIDIKRYAKVEKLPGGMPEDSVVLDGILVNKDVTHPSMARRVENPRVLILDCT 245
Cdd:TIGR02344 161 SRWSDLMCDLALDAVRTVQRDE-NGRKEIDIKRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 246 LEYKKGESQTIVDISDEAGWAKLLEQEETEIFNMCQNIIQTGCNVVVTEKGVSDLAQHFLSKAGISCIRRVRKTDANRLS 325
Cdd:TIGR02344 240 LEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 326 RVTGATIVNRTEELLPSDVGTGCGLFEVKKIGDEYFSYFIQCKDPKACSIVLRGSSKDVLNEIERNLQDALNVCRNIMLE 405
Cdd:TIGR02344 320 RACGATIVNRPEELRESDVGTGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 406 GKLLPGGGATEIEVACRLAAKLDSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHVAGNV-NAGLDGET 484
Cdd:TIGR02344 400 PKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNcTWGIDGET 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1624722677 485 GEICDTMKKRIFDTYTVKAQIFKSAIEAACMLLRIDMIVSGIGKR 529
Cdd:TIGR02344 480 GKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVSGVKKK 524
|
|
| 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: 558.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 33 LSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPAAKSLIELSRSQDEEVGDGTTSCVILSGQMLANSEPL 112
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 113 LKREIHPSKIVEGYMEALEDAL-AVMDAIATKIDLNNEEAVKDVIQSSLETKFSSRWGNLIASLALSAVQKVkltrPDGR 191
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALeILDSIISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAI----PKND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 192 TVIDIKRyAKVEKLPGGMPEDSVVLDGILVNKDVTHPSMARRVENPRVLILDCTLEYKKGESQTIVDISDEAGWAKLLEQ 271
Cdd:pfam00118 157 GSFDLGN-IGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 272 EETEIFNMCQNIIQTGCNVVVTEKGVSDLAQHFLSKAGISCIRRVRKTDANRLSRVTGATIVNRTEELLPSDVGTgCGLF 351
Cdd:pfam00118 236 EEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGT-AGKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 352 EVKKIGDEYFSYFIQCKDPKACSIVLRGSSKDVLNEIERNLQDALNVCRNIMLEGKLLPGGGATEIEVACRLAAKLDSKA 431
Cdd:pfam00118 315 EEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 432 GLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHVAGNVNAGLDGETGEICDTMKKRIFDTYTVKAQIFKSAIE 511
Cdd:pfam00118 395 GKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATE 474
|
490
....*....|...
gi 1624722677 512 AACMLLRIDMIVS 524
Cdd:pfam00118 475 AASTILRIDDIIK 487
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
15-524 |
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: 550.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 15 KKESDRKAQLATIQASRALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPAAKSLIELSRSQDEEVGDG 94
Cdd:cd00309 2 EREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 95 TTSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDLNNEEAVKDVIQSSLETKFSSRWGNLIAS 174
Cdd:cd00309 82 TTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 175 LALSAVQKVKLTRPDgrtviDIKRYAKVEKLPGGMPEDSVVLDGILVNKDVTHPSMARRVENPRVLILDCTLEYkkgesq 254
Cdd:cd00309 162 LVVDAVLKVGKENGD-----VDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 255 tivdisdeagwaklleqeeteifnmcqniiqtgcnVVVTEKGVSDLAQHFLSKAGISCIRRVRKTDANRLSRVTGATIVN 334
Cdd:cd00309 231 -----------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 335 RTEELLPSDVGTgCGLFEVKKIGDEYFSYFIQCKDPKACSIVLRGSSKDVLNEIERNLQDALNVCRNIMLEGKLLPGGGA 414
Cdd:cd00309 276 RLEDLTPEDLGT-AGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 415 TEIEVACRLAAKLDSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHVAGNVNAGLDGETGEICDTMKKR 494
Cdd:cd00309 355 AEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKEAG 434
|
490 500 510
....*....|....*....|....*....|
gi 1624722677 495 IFDTYTVKAQIFKSAIEAACMLLRIDMIVS 524
Cdd:cd00309 435 IIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
7-525 |
1.93e-178 |
|
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: 512.96 E-value: 1.93e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 7 VLVFKPSLKKESDRKAQLATIQASRALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPAAKSLIELSRS 86
Cdd:cd03343 1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 87 QDEEVGDGTTSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDLNNEEAVKDVIQSSLETKFSS 166
Cdd:cd03343 81 QDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 167 RWGNLIASLALSAVQKVKLTRpDGRTVIDIKrYAKVEKLPGGMPEDSVVLDGILVNKDVTHPSMARRVENPRVLILDCTL 246
Cdd:cd03343 161 AAKDKLADLVVDAVLQVAEKR-DGKYVVDLD-NIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 247 EYKKGESQTIVDISDEAGWAKLLEQEETEIFNMCQNIIQTGCNVVVTEKGVSDLAQHFLSKAGISCIRRVRKTDANRLSR 326
Cdd:cd03343 239 EVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 327 VTGATIVNRTEELLPSDVGTGcGLFEVKKIGDEYFSYFIQCKDPKACSIVLRGSSKDVLNEIERNLQDALNVCRNIMLEG 406
Cdd:cd03343 319 ATGAKIVTNIDDLTPEDLGEA-ELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 407 KLLPGGGATEIEVACRLAAKLDSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHVAGNVNAGLDGETGE 486
Cdd:cd03343 398 KVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGE 477
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1624722677 487 ICDTMKKRIFDTYTVKAQIFKSAIEAACMLLRID-MIVSG 525
Cdd:cd03343 478 VVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDdVIAAK 517
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
5-524 |
8.08e-176 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 506.35 E-value: 8.08e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 5 QTVLVFKPSLKKESDRKAQLATIQASRALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPAAKSLIELS 84
Cdd:NF041082 1 QPILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 85 RSQDEEVGDGTTSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDLNNEEAVKDVIQSSLETKF 164
Cdd:NF041082 81 KTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 165 SSRWGNLIASLALSAVQKVklTRPDGRTVIDIKrYAKVEKLPGGMPEDSVVLDGILVNKDVTHPSMARRVENPRVLILDC 244
Cdd:NF041082 161 AEAAKDKLADLVVDAVKAV--AEKDGGYNVDLD-NIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 245 TLEYKKGESQTIVDISDEAGWAKLLEQEETEIFNMCQNIIQTGCNVVVTEKGVSDLAQHFLSKAGISCIRRVRKTDANRL 324
Cdd:NF041082 238 PLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 325 SRVTGATIVNRTEELLPSDVGTGcGLFEVKKIGDEYFSYFIQCKDPKACSIVLRGSSKDVLNEIERNLQDALNVCRNIML 404
Cdd:NF041082 318 AKATGARIVTSIDDLSPEDLGYA-GLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 405 EGKLLPGGGATEIEVACRLAAKLDSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHVAGNVNAGLDGET 484
Cdd:NF041082 397 DGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYT 476
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1624722677 485 GEICDTMKKRIFDTYTVKAQIFKSAIEAACMLLRIDMIVS 524
Cdd:NF041082 477 GKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIA 516
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
5-524 |
2.58e-173 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 499.86 E-value: 2.58e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 5 QTVLVFKPSLKKESDRKAQLATIQASRALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPAAKSLIELS 84
Cdd:NF041083 1 QPVLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 85 RSQDEEVGDGTTSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDLNNEEAVKDVIQSSLETKF 164
Cdd:NF041083 81 KTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 165 SSRWGNLIASLALSAVQKVKLTRpDGRTVIDIKrYAKVEKLPGGMPEDSVVLDGILVNKDVTHPSMARRVENPRVLILDC 244
Cdd:NF041083 161 VEEARDYLAEIAVKAVKQVAEKR-DGKYYVDLD-NIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 245 TLEYKKGESQTIVDISDEAGWAKLLEQEETEIFNMCQNIIQTGCNVVVTEKGVSDLAQHFLSKAGISCIRRVRKTDANRL 324
Cdd:NF041083 239 PLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 325 SRVTGATIVNRTEELLPSDVGTGcGLFEVKKIGDEYFSYFIQCKDPKACSIVLRGSSKDVLNEIERNLQDALNVCRNIML 404
Cdd:NF041083 319 AKATGARIVTNIDDLTPEDLGYA-ELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 405 EGKLLPGGGATEIEVACRLAAKLDSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHVAGNVNAGLDGET 484
Cdd:NF041083 398 DGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFT 477
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1624722677 485 GEICDTMKKRIFDTYTVKAQIFKSAIEAACMLLRIDMIVS 524
Cdd:NF041083 478 GEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIA 517
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
7-524 |
8.46e-171 |
|
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: 493.43 E-value: 8.46e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 7 VLVFKPSLKKESDRKAQLATIQASRALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPAAKSLIELSRS 86
Cdd:TIGR02339 2 VFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 87 QDEEVGDGTTSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDLNNEEAVKDVIQSSLETKFSS 166
Cdd:TIGR02339 82 QDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 167 RWGN-LIASLALSAVQKVKLTRPDGRTVIDIKrYAKVEKLPGGMPEDSVVLDGILVNKDVTHPSMARRVENPRVLILDCT 245
Cdd:TIGR02339 162 EVAKdKLADLVVEAVKQVAELRGDGKYYVDLD-NIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 246 LEYKKGESQTIVDISDEAGWAKLLEQEETEIFNMCQNIIQTGCNVVVTEKGVSDLAQHFLSKAGISCIRRVRKTDANRLS 325
Cdd:TIGR02339 241 LEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 326 RVTGATIVNRTEELLPSDVGTGcGLFEVKKIGDEYFSYFIQCKDPKACSIVLRGSSKDVLNEIERNLQDALNVCRNIMLE 405
Cdd:TIGR02339 321 RATGARIVSSIDEITESDLGYA-ELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALED 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 406 GKLLPGGGATEIEVACRLAAKLDSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHVAGNVNAGLDGETG 485
Cdd:TIGR02339 400 GKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTG 479
|
490 500 510
....*....|....*....|....*....|....*....
gi 1624722677 486 EICDTMKKRIFDTYTVKAQIFKSAIEAACMLLRIDMIVS 524
Cdd:TIGR02339 480 EIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVIA 518
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
16-523 |
1.82e-128 |
|
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: 385.10 E-value: 1.82e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 16 KESDRKAQ--LATIQASRALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPAAKSLIELSRSQDEEVGD 93
Cdd:cd03338 1 TDKEKPADvrLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 94 GTTSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDLNNEEAVKDVIQSSLETKFSSRWGNLIA 173
Cdd:cd03338 81 GTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 174 SLALSAVQKVklTRPDGRTVIDIKRYAKVEKLpGGMPEDSVVLDGILVNKDVTH-PSMARRVENPRV-LILDCTLEYKKG 251
Cdd:cd03338 161 PIAVDAVLKV--IDPATATNVDLKDIRIVKKL-GGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIgLIQFCLSPPKTD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 252 ESQTIVdISDEAGWAKLLEQEETEIFNMCQNIIQTGCNVVVTEK-----GVSDLAQHFLSKAGISCIRRVRKTDANRLSR 326
Cdd:cd03338 238 MDNNIV-VNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQKsilrdAVSDLALHFLAKLKIMVVKDIEREEIEFICK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 327 VTGATIVNRTEELLPSDVGTGcGLFEVKKIGDEYFSYFIQCKDP-KACSIVLRGSSKDVLNEIERNLQDALNVCRNIMLE 405
Cdd:cd03338 317 TIGCKPVASIDHFTEDKLGSA-DLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 406 GKLLPGGGATEIEVACRLAAKLDSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHVAGNVNAGLDGETG 485
Cdd:cd03338 396 RALIPGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKG 475
|
490 500 510
....*....|....*....|....*....|....*...
gi 1624722677 486 EICDTMKKRIFDTYTVKAQIFKSAIEAACMLLRIDMIV 523
Cdd:cd03338 476 AITNILEENVVQPLLVSTSAITLATETVRMILKIDDIV 513
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
16-524 |
1.08e-111 |
|
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: 342.36 E-value: 1.08e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 16 KESDRK-------AQLATIQASRALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPAAKSLIELSRSQD 88
Cdd:cd03339 11 REQEKKkrlkgleAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 89 EEVGDGTTSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDL--NNEEAVKDVIQSSLETKFSS 166
Cdd:cd03339 91 DEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFspDNKEPLIQTAMTSLGSKIVS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 167 RWGNLIASLALSAVQkvkltrpdgrTVIDIKR------YAKVEKLPGGMPEDSVVLDGILVNKDVTHPSMARRVENPRVL 240
Cdd:cd03339 171 RCHRQFAEIAVDAVL----------SVADLERkdvnfeLIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 241 ILDCTLEYKKGESQTIVDISDEAGWAKLLEQEETEIFNMCQNIIQTGCNVVVTEKGVSDLAQHFLSKAGISCIRRVRKTD 320
Cdd:cd03339 241 ILTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 321 ANRLSRVTGATIVNRTEELLPSDVGTgCGLfeVKKIG-----DEYFsYFIQCKDPKACSIVLRGSSKDVLNEIERNLQDA 395
Cdd:cd03339 321 IELIAIATGGRIVPRFEDLSPEKLGK-AGL--VREISfgttkDKML-VIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 396 LNVCRNIMLEGKLLPGGGATEIEVACRLAAKLDSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHVA-G 474
Cdd:cd03339 397 LCVVRNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKeK 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1624722677 475 NVNAGLDGETGEICDTMKKRIFDTYTVKAQIFKSAIEAACMLLRIDMIVS 524
Cdd:cd03339 477 NPHLGIDCLGRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
15-523 |
9.39e-111 |
|
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: 339.84 E-value: 9.39e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 15 KKESDRKAQL--ATIQASRALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPAAKSLIELSRSQDEEVG 92
Cdd:TIGR02342 1 FQDKDKPQDVrtSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 93 DGTTSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDLNNEEAVKDVIQSSLETKFSSRWGNLI 172
Cdd:TIGR02342 81 DGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 173 ASLALSAVQKVklTRPDGRTVIDIKRYAKVEKLpGGMPEDSVVLDGILVNKDVTHPS-MARRVENPRVLILDCTLEYKKG 251
Cdd:TIGR02342 161 APLAVDAVLKV--IDPENAKNVDLNDIKVVKKL-GGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 252 ESQTIVDISDEAGWAKLLEQEETEIFNMCQNIIQTGCNVVVTEK-----GVSDLAQHFLSKAGISCIRRVRKTDANRLSR 326
Cdd:TIGR02342 238 DMENQIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKsilrdAVNDLALHFLAKMKIMVVKDIEREEIEFICK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 327 VTGATIVNRTEELLPSDVGTGcGLFEVKKIGDEYFSYFIQCKDP-KACSIVLRGSSKDVLNEIERNLQDALNVCRNIMLE 405
Cdd:TIGR02342 318 TIGCKPIASIDHFTADKLGSA-ELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 406 GKLLPGGGATEIEVACRLAAKLDSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHVAGNVNAGLDGETG 485
Cdd:TIGR02342 397 RGLIAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKG 476
|
490 500 510
....*....|....*....|....*....|....*...
gi 1624722677 486 EICDTMKKRIFDTYTVKAQIFKSAIEAACMLLRIDMIV 523
Cdd:TIGR02342 477 GITNMLEEHVLQPLLVTTSAITLASETVRSILKIDDIV 514
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
22-523 |
2.68e-108 |
|
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: 331.88 E-value: 2.68e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 22 AQLATIQASRALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPAAKSLIELSRSQDEEVGDGTTSCVIL 101
Cdd:cd03341 9 AVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 102 SGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMD--AIATKIDLNNEEAVKDVIQSSLETKFSsrwGN--LIASLAL 177
Cdd:cd03341 89 AGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEelVVYKIEDLRNKEEVSKALKTAIASKQY---GNedFLSPLVA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 178 SAVQKVKLTRPDGRTVIDIKryakVEKLPGGMPEDSVVLDGILVNKDVThpSMARRVENPRVLILDCTLEykkgesqtiv 257
Cdd:cd03341 166 EACISVLPENIGNFNVDNIR----VVKILGGSLEDSKVVRGMVFKREPE--GSVKRVKKAKVAVFSCPFD---------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 258 disdeagwaklleqeeteifnmcqniiqTGCNVVVTEKGVSDLAQHFLSKAGISCIRRVRKTDANRLSRVTGATIVNRTE 337
Cdd:cd03341 230 ----------------------------IGVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 338 ELLPSDVGTgCGLFEVKKIGDEYFSYFIQCK-DPKACSIVLRGSSKDVLNEIERNLQDALNVCRNIMLEGKLLPGGGATE 416
Cdd:cd03341 282 APTPEEIGY-CDSVYVEEIGDTKVVVFRQNKeDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 417 IEVACRLAAKLDSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHVAGNVNAGLDGETGE--ICDTMKKR 494
Cdd:cd03341 361 IELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDegTKDAKEAG 440
|
490 500
....*....|....*....|....*....
gi 1624722677 495 IFDTYTVKAQIFKSAIEAACMLLRIDMIV 523
Cdd:cd03341 441 IFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
14-520 |
2.80e-107 |
|
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: 330.79 E-value: 2.80e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 14 LKKESDR---KAQLAT-IQASRALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPAAKSLIELSRSQDE 89
Cdd:cd03340 5 LKEGTDTsqgKGQLISnINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 90 EVGDGTTSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDLNNEEAVKDVIQSSLETKFSSRwg 169
Cdd:cd03340 85 EVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKEEQRELLEKCAATALNSK-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 170 nLIAS-------LALSAVQkvKLTRPDGRTVIDIKryakveKLPGGMPEDSVVLDGILVNKDVT---HPSMARRVENPRV 239
Cdd:cd03340 163 -LIASekeffakMVVDAVL--SLDDDLDLDMIGIK------KVPGGSLEDSQLVNGVAFKKTFSyagFEQQPKKFKNPKI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 240 LILDCTLEYKKGESQTIVDISDEAGWAKLLEQEETEIFNMCQNIIQTGCNVVVTEKGVSDLAQHFLSKAGISCIRRVRKT 319
Cdd:cd03340 234 LLLNVELELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 320 DANRLSRVTGATIVNRTEELLPSDVGTgCGLFEVKKIGDEYFSYFIQCKDPKACSIVLRGSSKDVLNEIERNLQDALNVC 399
Cdd:cd03340 314 DLKRVAQATGGSIQTTVSNITDDVLGT-CGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 400 RNIMLEGKLLPGGGATEIEVACRLAAKLDSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHVAGNV-NA 478
Cdd:cd03340 393 RRAIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGkWY 472
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1624722677 479 GLDGETGEICDTMKKRIFDTYTVKAQIFKSAIEAACMLLRID 520
Cdd:cd03340 473 GVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLILSVD 514
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
16-524 |
5.82e-106 |
|
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: 327.91 E-value: 5.82e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 16 KESDRK-------AQLATIQASRALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPAAKSLIELSRSQD 88
Cdd:TIGR02343 15 KDQDNKkrlkgleAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 89 EEVGDGTTSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKI--DLNNEEAVKDVIQSSLETKFSS 166
Cdd:TIGR02343 95 DEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEIsaDNNNREPLIQAAKTSLGSKIVS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 167 RWGNLIASLALSAVQKV-KLTRPDgrtvIDIKrYAKVEKLPGGMPEDSVVLDGILVNKDVTHPSMARRVENPRVLILDCT 245
Cdd:TIGR02343 175 KCHRRFAEIAVDAVLNVaDMERRD----VDFD-LIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAILTCP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 246 LEYKKGESQTIVDISDEAGWAKLLEQEETEIFNMCQNIIQTGCNVVVTEKGVSDLAQHFLSKAGISCIRRVRKTDANRLS 325
Cdd:TIGR02343 250 FEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 326 RVTGATIVNRTEELLPSDVGTgCGLFEVKKIG--DEYFSYFIQCKDPKACSIVLRGSSKDVLNEIERNLQDALNVCRNIM 403
Cdd:TIGR02343 330 IATGGRIVPRFQELSKDKLGK-AGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 404 LEGKLLPGGGATEIEVACRLAAKLDSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHV-AGNVNAGLDG 482
Cdd:TIGR02343 409 KDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLkEKNPNLGVDC 488
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1624722677 483 ETGEICDTMKKRIFDTYTVKAQIFKSAIEAACMLLRIDMIVS 524
Cdd:TIGR02343 489 LGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVIS 530
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
4-520 |
2.73e-103 |
|
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: 320.55 E-value: 2.73e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 4 QQTVLVFKPSLKkESDRKAQLAT-IQASRALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPAAKSLIE 82
Cdd:TIGR02345 1 RPTIVLLKEGTD-TSQGKGQLISnINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 83 LSRSQDEEVGDGTTSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDLNN---EEAVKDVIQSS 159
Cdd:TIGR02345 80 IAKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqRELLEKCAATA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 160 LETKFSSRWGNLIASLALSAVQKVKLTRPDgRTVIDIKryakveKLPGGMPEDSVVLDGILVNKDVT---HPSMARRVEN 236
Cdd:TIGR02345 160 LSSKLISHNKEFFSKMIVDAVLSLDRDDLD-LKLIGIK------KVQGGALEDSQLVNGVAFKKTFSyagFEQQPKKFAN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 237 PRVLILDCTLEYKKGESQTIVDISDEAGWAKLLEQEETEIFNMCQNIIQTGCNVVVTEKGVSDLAQHFLSKAGISCIRRV 316
Cdd:TIGR02345 233 PKILLLNVELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 317 RKTDANRLSRVTGATIVNRTEELLPSDVGTgCGLFEVKKIGDEYFSYFIQCKDPKACSIVLRGSSKDVLNEIERNLQDAL 396
Cdd:TIGR02345 313 SAEDLKRVIKACGGSIQSTTSDLEADVLGT-CALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 397 NVCRNIMLEGKLLPGGGATEIEVACRLAAKLDSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHVAGNV 476
Cdd:TIGR02345 392 MIVRRALKNKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGK 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1624722677 477 NAGLDGETGEICDTMKKRIFDTYTVKAQIFKSAIEAACMLLRID 520
Cdd:TIGR02345 472 WYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVD 515
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
12-523 |
6.14e-99 |
|
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: 309.72 E-value: 6.14e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 12 PSLKKESDR------KAQLATIQASRALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPAAKSLIELSR 85
Cdd:TIGR02346 3 ASLLKEGYRhfsgleEAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 86 SQDEEVGDGTTSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDA-IATKI-DLNNEEAVKDVIQSSLETK 163
Cdd:TIGR02346 83 MQENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEElVVWEVkDLRDKDELIKALKASISSK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 164 FSSRWgNLIASLALSAVQKVKLTRPDGRTVIDIKryakVEKLPGGMPEDSVVLDGILVNKDVThpSMARRVENPRVLILD 243
Cdd:TIGR02346 163 QYGNE-DFLAQLVAQACSTVLPKNPQNFNVDNIR----VCKILGGSLSNSEVLKGMVFNREAE--GSVKSVKNAKVAVFS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 244 CTLEYKKGESQTIVDISDEAGWAKLLEQEETEIFNMCQNIIQTGCNVVVTEKGVSDLAQHFLSKAGISCIRRVRKTDANR 323
Cdd:TIGR02346 236 CPLDTATTETKGTVLIHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 324 LSRVTGATIVNRTEELLPSDVGTgCGLFEVKKIGDEYFSYFIQCK-DPKACSIVLRGSSKDVLNEIERNLQDALNVCRNI 402
Cdd:TIGR02346 316 LCKTVGATPLPRLGAPTPEEIGY-VDSVYVSEIGGDKVTVFKQENgDSKISTIILRGSTDNLLDDIERAIDDGVNTVKAL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 403 MLEGKLLPGGGATEIEVACRLAAKLDSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHVAGNVNAGLD- 481
Cdd:TIGR02346 395 VKDGRLLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDi 474
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1624722677 482 -GETGEICDTMKKRIFDTYTVKAQIFKSAIEAACMLLRIDMIV 523
Cdd:TIGR02346 475 eAESDGVKDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQII 517
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
19-532 |
5.50e-96 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 300.84 E-value: 5.50e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 19 DRKAQLATIQASRALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANP----AAKSLIELSRSQDEEVGDG 94
Cdd:COG0459 8 GEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 95 TTSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDlnNEEAVKDViqssleTKFSSRWGNLIAS 174
Cdd:COG0459 88 TTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVD--DKEELAQV------ATISANGDEEIGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 175 LALSAVQKVkltRPDGrtVIdikryaKVEKlPGGMPEDSVVLDGILVNKDVTHP-------SMARRVENPRVLILDctle 247
Cdd:COG0459 160 LIAEAMEKV---GKDG--VI------TVEE-GKGLETELEVVEGMQFDKGYLSPyfvtdpeKMPAELENAYILLTD---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 248 yKKgesqtivdISDEAGWAKLLEQeeteifnmcqnIIQTGCNVVVTEKGVSDLAQHFLSKAGISCIRRV----------- 316
Cdd:COG0459 224 -KK--------ISSIQDLLPLLEK-----------VAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgdr 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 317 RKTDANRLSRVTGATIVNR-----TEELLPSDVGTgCGLFEVkkiGDEYFSYFIQCKDPKACSIVLRGSSKDVLNEIERN 391
Cdd:COG0459 284 RKAMLEDIAILTGGRVISEdlglkLEDVTLDDLGR-AKRVEV---DKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 392 LQDALNVCRNImLEGKLLPGGGATEIEVACRLAAKLDSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSmh 471
Cdd:COG0459 360 VEDALHATRAA-VEEGIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRA-- 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1624722677 472 vAGNVNAGLDGETGEICDTMKKRIFDTYTVKAQIFKSAIEAACMLLRIDMIVSGIGKREEP 532
Cdd:COG0459 437 -AKDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEA 496
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
27-520 |
1.41e-95 |
|
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: 300.74 E-value: 1.41e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 27 IQASRALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPAAKSLIELSRSQDEEVGDGTTSCVILSGQML 106
Cdd:cd03335 14 VTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAELL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 107 ANSEPLLKREIHPSKIVEGYMEALEDALAVM-DAIATKIDLNNEEAVKDVIQSSLETKFSSRWGNLIASLALSAVQKVKL 185
Cdd:cd03335 94 KRANELVKQKIHPTTIISGYRLACKEAVKYIkEHLSISVDNLGKESLINVAKTSMSSKIIGADSDFFANMVVDAILAVKT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 186 TRPDGRTVIDIKRyAKVEKLPGGMPEDSVVLDGILVNKDVTHPSMARRVENPRVLILDCTLEYKKGESQTIVDISDEAGW 265
Cdd:cd03335 174 TNEKGKTKYPIKA-VNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKLGVQVVVTDPEKL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 266 AKlLEQEETEIF-NMCQNIIQTGCNVVVTEKGVSDLAQHFLSKAGISCIRRVRKTDANRLSRVTGATIV------NRTEE 338
Cdd:cd03335 253 EK-IRQRESDITkERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVstlanlEGEET 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 339 LLPSDVGTgCGLFEVKKIGDEYFSYFIQCKDPKACSIVLRGSSKDVLNEIERNLQDALNVCRNIMLEGKLLPGGGATEIE 418
Cdd:cd03335 332 FDPSYLGE-AEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGGAVETA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 419 VACRL---AAKLDSKAGLkrwSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHVAGNVNA--------GLDGETGEI 487
Cdd:cd03335 411 LSIYLenfATTLGSREQL---AIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKPdkkhlkwyGLDLINGKV 487
|
490 500 510
....*....|....*....|....*....|...
gi 1624722677 488 CDTMKKRIFDTYTVKAQIFKSAIEAACMLLRID 520
Cdd:cd03335 488 RDNLEAGVLEPTVSKIKSLKFATEAAITILRID 520
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
27-520 |
4.72e-95 |
|
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: 299.71 E-value: 4.72e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 27 IQASRALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPAAKSLIELSRSQDEEVGDGTTSCVILSGQML 106
Cdd:TIGR02340 18 VTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVIIAAELL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 107 ANSEPLLKREIHPSKIVEGYMEALEDALA-VMDAIATKIDLNNEEAVKDVIQSSLETKFSSRWGNLIASLALSAVQKVKL 185
Cdd:TIGR02340 98 KRADELVKNKIHPTSVISGYRLACKEAVKyIKENLSVSVDELGREALINVAKTSMSSKIIGLDSDFFSNIVVDAVLAVKT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 186 TRPDGRTVIDIKRyAKVEKLPGGMPEDSVVLDGILVNKDVTHPSMARRVENPRVLILDCTLEYKKGESQTIVDISDEAGW 265
Cdd:TIGR02340 178 TNENGETKYPIKA-INILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAKMALGVQIVVDDPEKL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 266 AKlLEQEETEIF-NMCQNIIQTGCNVVVTEKGVSDLAQHFLSKAGISCIRRVRKTDANRLSRVTGATIVNR------TEE 338
Cdd:TIGR02340 257 EQ-IRQREADITkERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVSTladlegEET 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 339 LLPSDVGTgCGLFEVKKIGDEYFSYFIQCKDPKACSIVLRGSSKDVLNEIERNLQDALNVCRNIMLEGKLLPGGGATEIE 418
Cdd:TIGR02340 336 FEASYLGF-ADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGGAVEAA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 419 VACRL---AAKLDSKAGLKRWSYraaAKAFEVIPKTLAQNCGANPVRIITELTSMHVA--------GNVNAGLDGETGEI 487
Cdd:TIGR02340 415 LSIYLenfATTLGSREQLAIAEF---ARALLIIPKTLAVNAAKDSTELVAKLRAYHAAaqlkpekkHLKWYGLDLVNGKI 491
|
490 500 510
....*....|....*....|....*....|...
gi 1624722677 488 CDTMKKRIFDTYTVKAQIFKSAIEAACMLLRID 520
Cdd:TIGR02340 492 RDNKEAGVLEPTVSKVKSLKFATEAAITILRID 524
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
15-523 |
5.68e-94 |
|
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: 295.32 E-value: 5.68e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 15 KKESDRKAQ-LAT-IQASRALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPAAKSLIELSRSQDEEVG 92
Cdd:cd03342 4 KAEVLRRGQaLAVnISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 93 DGTTSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKID-LNNEEAVKDVIQSSLETKFSSRWGNL 171
Cdd:cd03342 84 DGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEiDTDRELLLSVARTSLRTKLHADLADQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 172 IASLALSAVQKVKltRPDGRtvIDIKRyakVE--KLPGGMPEDSVVLDGILVNKDVTHPSMARRVENPRVLILDCTLEYK 249
Cdd:cd03342 164 LTEIVVDAVLAIY--KPDEP--IDLHM---VEimQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 250 KGEsqtivdisdeagwaklleqeeteifnmcqniIQTGC--NVVVTEKGVSDLAQHFLSKAGISCIRRVRKTDANRLSRV 327
Cdd:cd03342 237 KTE-------------------------------VNSGFfySVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 328 TGATIVNRTEELLPSDVGTgCGLFEVKKIGDEYFSYFIQCKDPKACSIVLRGSSKDVLNEIERNLQDALNVCRNIMLEGK 407
Cdd:cd03342 286 CGGVAMNSVDDLSPECLGY-AGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKC 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 408 LLPGGGATEIEVACRLAAKLDSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHVAGNVNAGLDGETGEI 487
Cdd:cd03342 365 VVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEP 444
|
490 500 510
....*....|....*....|....*....|....*.
gi 1624722677 488 CDTMKKRIFDTYTVKAQIFKSAIEAACMLLRIDMIV 523
Cdd:cd03342 445 MDPESEGIWDNYSVKRQILHSATVIASQLLLVDEII 480
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
22-532 |
8.81e-94 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 296.17 E-value: 8.81e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 22 AQLATIQASRALSEVIRTTLGPRAMLKMmLDPM------GGIVITNDGNAILREIDVANPAAKSLIELSRSQDEEVGDGT 95
Cdd:PTZ00212 23 ARLQSFVGAIAVADLVKTTLGPKGMDKI-LQPMsegprsGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGDGT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 96 TSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDLNNEEAVKDVI---QSSLETKFSSRWGNLI 172
Cdd:PTZ00212 102 TSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEKFKEDLLniaRTTLSSKLLTVEKDHF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 173 ASLALSAVQKVKltrpdGRTVIDikrYAKVEKLPGGMPEDSVVLDGILVNKDVThPSMARRVENPRVLILDCTLEYKK-- 250
Cdd:PTZ00212 182 AKLAVDAVLRLK-----GSGNLD---YIQIIKKPGGTLRDSYLEDGFILEKKIG-VGQPKRLENCKILVANTPMDTDKik 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 251 --GesqTIVDISDEAGWAKLLEQEETEIFNMCQNIIQTGCNVVVTEKGVSDLAQHFLSKAGISCIRRVRKTDANRLSRVT 328
Cdd:PTZ00212 253 iyG---AKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAAL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 329 GATIVNRTEELLPSDVGTgCGLFEVKKIGDEYFSYFIQCKDPKACSIVLRGSSKDVLNEIERNLQDALNVCRNIMLEGKL 408
Cdd:PTZ00212 330 GAEIVSTFDTPEKVKLGH-CDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKDTRV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 409 LPGGGATEIE--VACRLAAKldSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHVAGNVNAGLDGETGE 486
Cdd:PTZ00212 409 VLGGGCSEMLmaNAVEELAK--KVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGIDMEKGT 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1624722677 487 ICDTMKKRIFDTYTVKAQIFKSAIEAACMLLRIDMIVSGIGKREEP 532
Cdd:PTZ00212 487 VGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRCAPRQREQ 532
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
9-524 |
3.02e-92 |
|
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: 291.93 E-value: 3.02e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 9 VFKPSLKKESDRKAQLATIQASRALSEVIRTTLGPRAMLKMML--DPMGGIVITNDGNAILREIDVANPAAKSLIELSRS 86
Cdd:cd03336 1 ILKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILQsvGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 87 QDEEVGDGTTSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDLNNEEAVKDVI---QSSLETK 163
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEAFREDLLniaRTTLSSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 164 FSSRWGNLIASLALSAVQKVKltrpdGRTVIDikrYAKVEKLPGGMPEDSVVLDGILVNKD--VTHPsmaRRVENPRVLI 241
Cdd:cd03336 161 ILTQDKEHFAELAVDAVLRLK-----GSGNLD---AIQIIKKLGGSLKDSYLDEGFLLDKKigVNQP---KRIENAKILI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 242 LDCTLEYKKGE---SQTIVDisdeaGWAKLLEQEETE---IFNMCQNIIQTGCNVVVTEKGVSDLAQHFLSKAGISCIRR 315
Cdd:cd03336 230 ANTPMDTDKIKifgAKVRVD-----STAKVAEIEEAEkekMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 316 VRKTDANRLSRVTGATIVNRTEELLPSDVGTgCGLFEVKKIGDEYFSYFIQCKDPKACSIVLRGSSKDVLNEIERNLQDA 395
Cdd:cd03336 305 ADFDGVERLALVTGGEIASTFDHPELVKLGT-CKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 396 LNVCRNIMLEGKLLPGGGATEIEVACRLAAKLDSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHVAGN 475
Cdd:cd03336 384 LCVLAQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGN 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1624722677 476 VNAGLDGETGEICDTMKKRIFDTYTVKAQIFKSAIEAACMLLRIDMIVS 524
Cdd:cd03336 464 TTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIK 512
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
15-523 |
4.74e-87 |
|
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: 278.93 E-value: 4.74e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 15 KKESDRKAQ--LATIQASRALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPAAKSLIELSRSQDEEVG 92
Cdd:TIGR02347 8 KAESLRRDAalMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 93 DGTTSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDLNNE-EAVKDVIQSSLETKFSSrwgNL 171
Cdd:TIGR02347 88 DGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEVDrEFLLNVARTSLRTKLPA---DL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 172 IASLALSAVQKVKLTRPDGrTVIDIKRYAKVEkLPGGMPEDSVVLDGILVNKDVTHPSMARRVENPRVLILDCTLEYKKG 251
Cdd:TIGR02347 165 ADQLTEIVVDAVLAIKKDG-EDIDLFMVEIME-MKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 252 ESQTIVDISDEAGWAKLLEQEETEIFNMCQNIIQTG---CN-------VVVTEKGVSDLAQHFLSKAGISCIRRVRKTDA 321
Cdd:TIGR02347 243 EVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKkkvCGkspdkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 322 NRLSRVTGATIVNRTEELLPSDVGTGcGLFEVKKIGDEYFSYFIQCKDPKACSIVLRGSSKDVLNEIERNLQDALNVCRN 401
Cdd:TIGR02347 323 ERLTLACGGEALNSVEDLTPECLGWA-GLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 402 IMLEGKLLPGGGATEIEVACRLAAKLDSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHVAGNVNAGLD 481
Cdd:TIGR02347 402 AIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGVD 481
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1624722677 482 GETGEICDTMKKRIFDTYTVKAQIFKSAIEAACMLLRIDMIV 523
Cdd:TIGR02347 482 LNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVM 523
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
9-523 |
1.74e-76 |
|
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: 250.93 E-value: 1.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 9 VFKPSLKKESDRKAQLATIQASRALSEVIRTTLGPRAMLKMML--DPMGGIVITNDGNAILREIDVANPAAKSLIELSRS 86
Cdd:TIGR02341 2 IFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 87 QDEEVGDGTTSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDLNNEEAVKDVI---QSSLETK 163
Cdd:TIGR02341 82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVKFRQDLMniaRTTLSSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 164 FSSRWGNLIASLALSAVQKVKltrpdGRTVIDikrYAKVEKLPGGMPEDSVVLDGILVNK--DVTHPsmaRRVENPRVLI 241
Cdd:TIGR02341 162 ILSQHKDHFAQLAVDAVLRLK-----GSGNLE---AIQIIKKLGGSLADSYLDEGFLLDKkiGVNQP---KRIENAKILI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 242 LDCTLEYKKGE---SQTIVDisdeaGWAKLLEQEETEIFNM---CQNIIQTGCNVVVTEKGVSDLAQHFLSKAGISCIRR 315
Cdd:TIGR02341 231 ANTGMDTDKVKifgSRVRVD-----STAKVAELEHAEKEKMkekVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEH 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 316 VRKTDANRLSRVTGATIVNRTEEllPSDVGTG-CGLFEVKKIGDEYFSYFIQCKDPKACSIVLRGSSKDVLNEIERNLQD 394
Cdd:TIGR02341 306 ADFEGVERLALVTGGEIVSTFDH--PELVKLGsCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHD 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 395 ALNVCRNIMLEGKLLPGGGATEIEVACRLAAKLDSKAGLKRWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSMHVAG 474
Cdd:TIGR02341 384 ALCVLSQTVKESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNG 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1624722677 475 NVNAGLDGETGEICDTMKKRIFDTYTVKAQIFKSAIEAACMLLRIDMIV 523
Cdd:TIGR02341 464 NTTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNII 512
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
149-405 |
4.30e-72 |
|
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: 228.89 E-value: 4.30e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 149 EEAVKDVIQSSLETKFSSrWGNLIASLALSAVQKVKLTRPDgrtviDIKRYAKVEKLPGGMPEDSVVLDGILVNKDVTHP 228
Cdd:cd03333 1 RELLLQVATTSLNSKLSS-WDDFLGKLVVDAVLKVGPDNRM-----DDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 229 SMARRVENPRVLILDCTLEYkkgesqtivdisdeagwaklleqeeteifnmcqniiqtgcnVVVTEKGVSDLAQHFLSKA 308
Cdd:cd03333 75 YMPKRLENAKILLLDCPLEY-----------------------------------------VVIAEKGIDDLALHYLAKA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 309 GISCIRRVRKTDANRLSRVTGATIVNRTEELLPSDVGTgCGLFEVKKIGDEYFSYFIQCKDPKACSIVLRGSSKDVLNEI 388
Cdd:cd03333 114 GIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGT-AELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEV 192
|
250
....*....|....*..
gi 1624722677 389 ERNLQDALNVCRNIMLE 405
Cdd:cd03333 193 KRSLHDALCAVRAAVEE 209
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
165-409 |
1.88e-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: 160.85 E-value: 1.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 165 SSRWGNLIASLALSAVQKVKLTRPDGrTVIDIKRYAKVEKLPGGMPEDSVVLDGILVNKDVTHPSMARRVENPRVLILDC 244
Cdd:cd03334 16 DESWLDILLPLVWKAASNVKPDVRAG-DDMDIRQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 245 TLEYKKGESQTI-VDIsdeagwakLLEQEETEIFNMCQNIIQTGCNVVVTEKGVSDLAQHFLSKAGISCIRRVRKTDANR 323
Cdd:cd03334 95 PLEYQRVENKLLsLDP--------VILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLER 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 324 LSRVTGATIVNRTEELL-PSDVGTgCGLFEVKKIGDEY-----FSYFIQCKDPKACSIVLRGSSKDVLNEIERNLQDALN 397
Cdd:cd03334 167 ISRCTGADIISSMDDLLtSPKLGT-CESFRVRTYVEEHgrsktLMFFEGCPKELGCTILLRGGDLEELKKVKRVVEFMVF 245
|
250
....*....|..
gi 1624722677 398 VCRNIMLEGKLL 409
Cdd:cd03334 246 AAYHLKLETSFL 257
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
20-517 |
6.85e-12 |
|
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: 67.87 E-value: 6.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 20 RKAQLATIQAsraLSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANP----AAKSLIELSRSQDEEVGDGT 95
Cdd:cd03344 10 RKALLRGVNK---LADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 96 TSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIdlNNEEAVKDViqSSLETKFSSRWGNLIAsl 175
Cdd:cd03344 87 TTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPV--KTKEEIAQV--ATISANGDEEIGELIA-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 176 alSAVQKVKltrPDGrtVIDIKRyakveklpGGMPEDSV-VLDGILVNKD------VTHP-SMARRVENPRVLILDctle 247
Cdd:cd03344 161 --EAMEKVG---KDG--VITVEE--------GKTLETELeVVEGMQFDRGylspyfVTDPeKMEVELENPYILLTD---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 248 yKKGES-QTIVDISDEAGWAK--LL------EQE--ETEIFN----------------------MCQNI-IQTGCNVVVT 293
Cdd:cd03344 222 -KKISSiQELLPILELVAKAGrpLLiiaedvEGEalATLVVNklrgglkvcavkapgfgdrrkaMLEDIaILTGGTVISE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 294 EKGVSdlaqhfLSKAGISCIRRVRK--TDANRLSRVTGA----TIVNRTEEL------LPSDvgtgcglFEVKKIgDEYF 361
Cdd:cd03344 301 ELGLK------LEDVTLEDLGRAKKvvVTKDDTTIIGGAgdkaAIKARIAQIrkqieeTTSD-------YDKEKL-QERL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 362 SYFIQckdpKACSIVLRGSSKDVLNEIERNLQDALNVCRNIMLEGkLLPGGGATEIEVACRL----AAKLDSKAGlkrws 437
Cdd:cd03344 367 AKLSG----GVAVIKVGGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPALdklkALNGDEKLG----- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 438 YRAAAKAFEVIPKTLAQNCGANPVRIITELtsmhVAGNVNAGLDGETGEICDTMKKRIFDTYTVKAQIFKSAIEAACMLL 517
Cdd:cd03344 437 IEIVRRALEAPLRQIAENAGVDGSVVVEKV----LESPDGFGYDAATGEYVDMIEAGIIDPTKVVRSALQNAASVASLLL 512
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
31-535 |
1.92e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 56.74 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 31 RALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANP----AAKSLIELSRSQDEEVGDGTTSCVILSGQML 106
Cdd:PRK12849 20 NKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQALV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 107 --------ANSEPL-LKREIHpsKIVEGYMEAL-EDALAVMD-----AIATkIDLNNEEAVkdviqssletkfssrwGNL 171
Cdd:PRK12849 100 qeglknvaAGANPMdLKRGID--KAVEAVVEELkALARPVSGseeiaQVAT-ISANGDEEI----------------GEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 172 IASlALSAVQKvkltrpDGrtVIDIKrYAKveklpgGMPEDSVVLDGILVNKD------VTHP-SMARRVENPRVLILDC 244
Cdd:PRK12849 161 IAE-AMEKVGK------DG--VITVE-ESK------TLETELEVTEGMQFDRGylspyfVTDPeRMEAVLEDPLILLTDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 245 T----------LE--YKKGESQTIV--DISDEAgWAKLLEQEETEIFN---------------MCQNI-IQTGCNVVVTE 294
Cdd:PRK12849 225 KisslqdllplLEkvAQSGKPLLIIaeDVEGEA-LATLVVNKLRGGLKvaavkapgfgdrrkaMLEDIaILTGGTVISED 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 295 KGVSdlaqhfLSKAGISCIRRVRK--TDANRLSRVTGA----TIVNRTE------ELLPSDV--------------GTGc 348
Cdd:PRK12849 304 LGLK------LEEVTLDDLGRAKRvtITKDNTTIVDGAgdkeAIEARVAqirrqiEETTSDYdreklqerlaklagGVA- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 349 glfeVKKIGdeyfsyfiqckdpkacsivlrGSSKDVLNEIERNLQDALNVCRNIMLEGkLLPGGGATEIevacRLAAKLD 428
Cdd:PRK12849 377 ----VIKVG---------------------AATEVELKERKDRVEDALNATRAAVEEG-IVPGGGVALL----RAAKALD 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 429 SKAGLK---RWSYRAAAKAFEVIPKTLAQNCGANPVRIITELTSmhvaGNVNAGLDGETGEICDTMKKRIFDTYTVKAQI 505
Cdd:PRK12849 427 ELAGLNgdqAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLE----LEDGFGFNAATGEYGDLIAAGIIDPVKVTRSA 502
|
570 580 590
....*....|....*....|....*....|
gi 1624722677 506 FKSAIEAACMLLRIDMIVSGIGKREEPSTG 535
Cdd:PRK12849 503 LQNAASVAGLLLTTEALVADKPEEEDPPGG 532
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
20-514 |
3.16e-08 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 56.07 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 20 RKAQLATIQAsraLSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANPA----AKSLIELSRSQDEEVGDGT 95
Cdd:PTZ00114 24 RQSLLKGIER---LADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKAGDGT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 96 TSCVILSGQMLANSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDLNNEeaVKDV--IQSSLETKFssrwGNLIA 173
Cdd:PTZ00114 101 TTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKED--ILNVatISANGDVEI----GSLIA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 174 SlalsAVQKV----KLTRPDGRTVIDikryakveklpggmpEDSVVlDGILVNKDVTHP-----SMARRVE--NPRVLIL 242
Cdd:PTZ00114 175 D----AMDKVgkdgTITVEDGKTLED---------------ELEVV-EGMSFDRGYISPyfvtnEKTQKVEleNPLILVT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 243 DCT----------LEYKKGESQTIVDISDEAGWAKLleqeETEIFNMCQNIIQTGCnvvVTEKGVSDlaqhflskagisc 312
Cdd:PTZ00114 235 DKKissiqsilpiLEHAVKNKRPLLIIAEDVEGEAL----QTLIINKLRGGLKVCA---VKAPGFGD------------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 313 irrVRKTDANRLSRVTGATIVNRTEELLPSDVGTGCGLFEVKKIgdeyfsyfIQCKDpkACSIVLRGSSKDVLNE----- 387
Cdd:PTZ00114 295 ---NRKDILQDIAVLTGATVVSEDNVGLKLDDFDPSMLGSAKKV--------TVTKD--ETVILTGGGDKAEIKErvell 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 388 ---IERN---------------------------------------LQDALNVCRNIMLEGkLLPGGGATEIevacRLAA 425
Cdd:PTZ00114 362 rsqIERTtseydkeklkerlaklsggvavikvggasevevnekkdrIEDALNATRAAVEEG-IVPGGGVALL----RASK 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 426 KLDSKAGLKRWS--YRAAAK----AFEVIPKTLAQNCGANPVRIITELTSmhvAGNVNAGLDGETGEICDTMKKRIFDTY 499
Cdd:PTZ00114 437 LLDKLEEDNELTpdQRTGVKivrnALRLPTKQIAENAGVEGAVVVEKILE---KKDPSFGYDAQTGEYVNMFEAGIIDPT 513
|
570
....*....|....*
gi 1624722677 500 TVkaqiFKSAIEAAC 514
Cdd:PTZ00114 514 KV----VRSALVDAA 524
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
32-535 |
1.51e-06 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 50.87 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 32 ALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANP----AAKSLIELSRSQDEEVGDGTTSCVILSGQMLA 107
Cdd:PRK12850 22 ILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 108 NSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDLNNEEAVKDVIQSSLETKFssrwGNLIAslalSAVQKVK--- 184
Cdd:PRK12850 102 EGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESI----GEMIA----EAMDKVGkeg 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 185 -LTRPDGRTV---IDIkryakVEklpgGMPEDSVVLDGILvnkdVTHPSMARRV-ENPRVLIldctLEYKKGESQTIVDI 259
Cdd:PRK12850 174 vITVEEAKTLgteLDV-----VE----GMQFDRGYLSPYF----VTNPEKMRAElEDPYILL----HEKKISNLQDLLPI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 260 SD---EAGWAKLLEQEETE-------IFNMCQNIIQTgcnVVVTEKGVSD------------LAQHFLSK-AGIScIRRV 316
Cdd:PRK12850 237 LEavvQSGRPLLIIAEDVEgealatlVVNKLRGGLKS---VAVKAPGFGDrrkamlediavlTGGQVISEdLGIK-LENV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 317 RKTDANRLSRVT----GATIVNRTEEllPSDVGTGCGLFEVK--KIGDEYFSYFIQCKDPKACS--IVLR--GSSKDVLN 386
Cdd:PRK12850 313 TLDMLGRAKRVLitkeNTTIIDGAGD--KKNIEARVKQIRAQieETTSDYDREKLQERLAKLAGgvAVIRvgGATEVEVK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 387 EIERNLQDALNVCRNIMLEGkLLPGGGATEIEVACRLAAKL----DSKAGLKrwsyrAAAKAFEVIPKTLAQNCGANPVR 462
Cdd:PRK12850 391 EKKDRVDDALHATRAAVEEG-IVPGGGVALLRARSALRGLKganaDETAGID-----IVRRALEEPLRQIATNAGFEGSV 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624722677 463 IITELTSmhvaGNVNAGLDGETGEICDTMKKRIFDTYTVKAQIFKSAIEAACMLLRIDMIVSGIGKREEPSTG 535
Cdd:PRK12850 465 VVGKVAE----LPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAAAAAA 533
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
32-151 |
1.25e-05 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 47.81 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 32 ALSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANP----AAKSLIELSRSQDEEVGDGTTSCVILSGQMLA 107
Cdd:PRK12851 22 ILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAIVR 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1624722677 108 NSEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDLNNEEA 151
Cdd:PRK12851 102 EGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIA 145
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
33-535 |
8.45e-05 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 45.30 E-value: 8.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 33 LSEVIRTTLGPRAMLKMMLDPMGGIVITNDGNAILREIDVANP----AAKSLIELSRSQDEEVGDGTTSCVILSGQMLAN 108
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 109 SEPLLKREIHPSKIVEGYMEALEDALAVMDAIATKIDlnnEEAVKDVIQSSLETKFSSrwGNLIASlALSAV-QKVKLTR 187
Cdd:PLN03167 158 GVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVE---DSELADVAAVSAGNNYEV--GNMIAE-AMSKVgRKGVVTL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 188 PDGRTViDIKRYAkVEklpgGMPEDSvvldGILVNKDVTHPS-MARRVENPRVLILDctleYKKGESQTIVDISDEA--- 263
Cdd:PLN03167 232 EEGKSA-ENNLYV-VE----GMQFDR----GYISPYFVTDSEkMSVEYDNCKLLLVD----KKITNARDLIGILEDAirg 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 264 GW-----AKLLEQE--ETEIFNMCQNIIQ-----------------------TGCNVVVTEKGVSdlaqhfLSKAGisci 313
Cdd:PLN03167 298 GYplliiAEDIEQEalATLVVNKLRGSLKiaalkapgfgerksqylddiailTGGTVIREEVGLS------LDKVG---- 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 314 RRVRKTDANRLSRVTGATIV--NRTEELLPSDVGTGCGLFEV--KKIGDEYFSYFIQCKDPKACSIVLRGSSKDVLNEIE 389
Cdd:PLN03167 368 KEVLGTAAKVVLTKDTTTIVgdGSTQEAVNKRVAQIKNLIEAaeQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKK 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624722677 390 RNLQDALNVCRNIMLEGkLLPGGGATEIevacRLAAKLDS-KAGLKRWSYRAAA----KAFEVIPKTLAQNCGANPVRII 464
Cdd:PLN03167 448 LRVEDALNATKAAVEEG-IVVGGGCTLL----RLASKVDAiKDTLENDEQKVGAdivkRALSYPLKLIAKNAGVNGSVVS 522
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1624722677 465 TELTSmhvAGNVNAGLDGETGEICDTMKKRIFDTYTVKAQIFKSAIEAACMLLRIDMIVSGIGKREEPSTG 535
Cdd:PLN03167 523 EKVLS---NDNPKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPEPVPAG 590
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
32-101 |
9.36e-03 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 38.57 E-value: 9.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1624722677 32 ALSEVIRTTLGPRAmLKMMLD-PMGGIVITNDGNAILREIDVANP----AAKSLIELSRSQDEEVGDGTTSCVIL 101
Cdd:PRK00013 21 KLADAVKVTLGPKG-RNVVLEkSFGAPTITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVL 94
|
|
| |
