|
Name |
Accession |
Description |
Interval |
E-value |
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
2-533 |
0e+00 |
|
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: 956.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 2 SVRVLNPNAEVLNKSAALHMTINAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIARTAV 81
Cdd:TIGR02347 1 SVKLLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 82 AQDDISGDGTTSTVIFIGELMKQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKtpVVMGDEPDKEILKMVARTTLRT 161
Cdd:TIGR02347 81 AQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFK--VKKEDEVDREFLLNVARTSLRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 162 KLYEGLADQLTDIVVNSVLCIRKPQEPIDLFMVEIMHMRHKFDVDTRLVEGLVLDHGSRHPDMKRRAENCHILTCNVSLE 241
Cdd:TIGR02347 159 KLPADLADQLTEIVVDAVLAIKKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 242 YEKSEINAGFFYSNAEQREAMVTAERRSVDERVQKIIELKNKVCA-GNDNSFVILNQKGIDPPSLDLLAREGIIALRRAK 320
Cdd:TIGR02347 239 YEKTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCGkSPDKGFVVINQKGIDPPSLDLLAKEGIMALRRAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 321 RRNMERLVLACGGEAVNSVDDLTPDCLGWAGLVYEHVLGEEKYTFVEQVKNPHSCTILIKGPNDHTIAQIKDAVRDGLRS 400
Cdd:TIGR02347 319 RRNMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 401 VKNTLEDECVVLGAGAFEVAARQHLiNEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKG-NI 479
Cdd:TIGR02347 399 VKNAIEDKCVVPGAGAFEIAAYRHL-KEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGgEV 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1780591515 480 VGLDLQDGEPVDPQLAGIFDNYSVKRQLINSGPVIASQLLLVDEVIRAGRNMRK 533
Cdd:TIGR02347 478 VGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSMLK 531
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
6-529 |
0e+00 |
|
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: 897.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 6 LNPNAEVLNKSAALHMTINAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIARTAVAQDD 85
Cdd:cd03342 1 LNPKAEVLRRGQALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 86 ISGDGTTSTVIFIGELMKQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVVMgdEPDKEILKMVARTTLRTKLYE 165
Cdd:cd03342 81 ITGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEI--DTDRELLLSVARTSLRTKLHA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 166 GLADQLTDIVVNSVLCIRKPQEPIDLFMVEIMHMRHKFDVDTRLVEGLVLDHGSRHPDMKRRAENCHILTCNVSLEYEKS 245
Cdd:cd03342 159 DLADQLTEIVVDAVLAIYKPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEKT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 246 EINAGFFYSnaeqreamvtaerrsvdervqkiielknkvcagndnsfVILNQKGIDPPSLDLLAREGIIALRRAKRRNME 325
Cdd:cd03342 239 EVNSGFFYS--------------------------------------VVINQKGIDPPSLDMLAKEGILALRRAKRRNME 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 326 RLVLACGGEAVNSVDDLTPDCLGWAGLVYEHVLGEEKYTFVEQVKNPHSCTILIKGPNDHTIAQIKDAVRDGLRSVKNTL 405
Cdd:cd03342 281 RLTLACGGVAMNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 406 EDECVVLGAGAFEVAARQHLINEvKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKGNIVGL-DL 484
Cdd:cd03342 361 EDKCVVPGAGAFEVALYAHLKEF-KKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGvDL 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1780591515 485 QDGEPVDPQLAGIFDNYSVKRQLINSGPVIASQLLLVDEVIRAGR 529
Cdd:cd03342 440 DTGEPMDPESEGIWDNYSVKRQILHSATVIASQLLLVDEIIRAGR 484
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
29-528 |
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: 588.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 29 LQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIARTAVAQDDISGDGTTSTVIFIGELMKQSERC 108
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 109 IDEGMHPRVLVDGFEIAKRATLQFLD-TFKTPVvmgDEPDKEILKMVARTTLRTKLYEGLADQLTDIVVNSVLCIRKPQE 187
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDsIISIPV---EDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 188 PIDLFMVEIMHMRHKFDVDTRLVEGLVLDHGSRHPDMKRRAENCHILTCNVSLEYEKSEINAGFFYSNAEQREAMVTAER 267
Cdd:pfam00118 158 SFDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 268 RSVDERVQKIIELKNKVcagndnsfvILNQKGIDPPSLDLLAREGIIALRRAKRRNMERLVLACGGEAVNSVDDLTPDCL 347
Cdd:pfam00118 238 EQILEIVEKIIDSGVNV---------VVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 348 GWAGLVYEHVLGEEKYTFVEQVKNPHSCTILIKGPNDHTIAQIKDAVRDGLRSVKNTLEDECVVLGAGAFEVAARQHLiN 427
Cdd:pfam00118 309 GTAGKVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARAL-R 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 428 EVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKGNI-VGLDLQDGEPVDPQLAGIFDNYSVKRQ 506
Cdd:pfam00118 388 EYAKSVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKhAGIDVETGEIIDMKEAGVVDPLKVKRQ 467
|
490 500
....*....|....*....|..
gi 1780591515 507 LINSGPVIASQLLLVDEVIRAG 528
Cdd:pfam00118 468 ALKSATEAASTILRIDDIIKAK 489
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
10-526 |
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: 539.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 10 AEVLNKSAALHMTINAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIARTAVAQDDISGD 89
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 90 GTTSTVIFIGELMKQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVvmgDEPDKEILKMVARTTLRTKLYEGLAD 169
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPI---DVEDREELLKVATTSLNSKLVSGGDD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 170 QLTDIVVNSVLCIRKPQEPIDLFMVEIMHMRHKFDVDTRLVEGLVLDHGSRHPDMKRRAENCHILTCNVSLEYekseina 249
Cdd:cd00309 158 FLGELVVDAVLKVGKENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 250 gffysnaeqreamvtaerrsvdervqkiielknkvcagndnsfVILNQKGIDPPSLDLLAREGIIALRRAKRRNMERLVL 329
Cdd:cd00309 231 -------------------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAK 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 330 ACGGEAVNSVDDLTPDCLGWAGLVYEHVLGEEKYTFVEQVKNPHSCTILIKGPNDHTIAQIKDAVRDGLRSVKNTLEDEC 409
Cdd:cd00309 268 ATGATIVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGG 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 410 VVLGAGAFEVAARQHLiNEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKGNI-VGLDLQDGE 488
Cdd:cd00309 348 IVPGGGAAEIELSKAL-EELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGnAGGDVETGE 426
|
490 500 510
....*....|....*....|....*....|....*...
gi 1780591515 489 PVDPQLAGIFDNYSVKRQLINSGPVIASQLLLVDEVIR 526
Cdd:cd00309 427 IVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
18-528 |
1.09e-141 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 418.52 E-value: 1.09e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 18 ALHMTINAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIARTAVAQDDISGDGTTSTVIF 97
Cdd:NF041082 18 AQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 98 IGELMKQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVvmgDEPDKEILKMVARTTLRTKLYEGLADQLTDIVVN 177
Cdd:NF041082 98 AGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKV---DPDDKETLKKIAATAMTGKGAEAAKDKLADLVVD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 178 SVLCIRKPQEP--IDLFMVEIMHMRHKFDVDTRLVEGLVLDHGSRHPDMKRRAENCHILTCNVSLEYEKSEINAGFFYSN 255
Cdd:NF041082 175 AVKAVAEKDGGynVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDAKISITD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 256 AEQREAMVTAERRSVDERVQKIIElknkvcAGNDnsfVILNQKGIDPPSLDLLAREGIIALRRAKRRNMERLVLACGGEA 335
Cdd:NF041082 255 PDQLQAFLDQEEKMLKEMVDKIAD------SGAN---VVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 336 VNSVDDLTPDCLGWAGLVYEHVLGEEKYTFVEQVKNPHSCTILIKGPNDHTIAQIKDAVRDGLRSVKNTLEDECVVLGAG 415
Cdd:NF041082 326 VTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 416 AFEVA-ARQhlINEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKGNI-VGLDLQDGEPVDPQ 493
Cdd:NF041082 406 APEVElALR--LREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKtAGLDVYTGKVVDML 483
|
490 500 510
....*....|....*....|....*....|....*
gi 1780591515 494 LAGIFDNYSVKRQLINSGPVIASQLLLVDEVIRAG 528
Cdd:NF041082 484 EIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
18-528 |
1.16e-139 |
|
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: 413.58 E-value: 1.16e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 18 ALHMTINAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIARTAVAQDDISGDGTTSTVIF 97
Cdd:cd03343 16 AQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 98 IGELMKQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVvmgDEPDKEILKMVARTTLRTKLYEGLADQLTDIVVN 177
Cdd:cd03343 96 AGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKV---DPDDKDTLRKIAKTSLTGKGAEAAKDKLADLVVD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 178 SVLCI---RKPQEPIDLFMVEIMHMRHKFDVDTRLVEGLVLDHGSRHPDMKRRAENCHILTCNVSLEYEKSEINAGFFYS 254
Cdd:cd03343 173 AVLQVaekRDGKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAKIRIT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 255 NAEQREAMVTAERRSVDERVQKIIElknkvcAGNDnsfVILNQKGIDPPSLDLLAREGIIALRRAKRRNMERLVLACGGE 334
Cdd:cd03343 253 SPDQLQAFLEQEEAMLKEMVDKIAD------TGAN---VVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 335 AVNSVDDLTPDCLGWAGLVYEHVLGEEKYTFVEQVKNPHSCTILIKGPNDHTIAQIKDAVRDGLRSVKNTLEDECVVLGA 414
Cdd:cd03343 324 IVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 415 GAFEVAARQHLiNEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKGNI-VGLDLQDGEPVDPQ 493
Cdd:cd03343 404 GAVEIELAKRL-REYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKnAGLDVYTGEVVDML 482
|
490 500 510
....*....|....*....|....*....|....*
gi 1780591515 494 LAGIFDNYSVKRQLINSGPVIASQLLLVDEVIRAG 528
Cdd:cd03343 483 EKGVIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
18-528 |
2.24e-135 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 402.41 E-value: 2.24e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 18 ALHMTINAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIARTAVAQDDISGDGTTSTVIF 97
Cdd:NF041083 18 AQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAVVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 98 IGELMKQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVvmgDEPDKEILKMVARTTLRTKLYEGLADQLTDIVVN 177
Cdd:NF041083 98 AGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKV---DPDDRETLKKIAETSLTSKGVEEARDYLAEIAVK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 178 SVLCIrkpqepidlfmVEIMHMRHKFDV--------------DTRLVEGLVLDHGSRHPDMKRRAENCHILTCNVSLEYE 243
Cdd:NF041083 175 AVKQV-----------AEKRDGKYYVDLdniqiekkhggsieDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 244 KSEINAGFFYSNAEQREAMVTAERRSVDERVQKIIElknkvcAGNDnsfVILNQKGIDPPSLDLLAREGIIALRRAKRRN 323
Cdd:NF041083 244 KTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKA------TGAN---VVFCQKGIDDLAQHYLAKAGILAVRRVKKSD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 324 MERLVLACGGEAVNSVDDLTPDCLGWAGLVYEHVLGEEKYTFVEQVKNPHSCTILIKGPNDHTIAQIKDAVRDGLRSVKN 403
Cdd:NF041083 315 MEKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVAD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 404 TLEDECVVLGAGAFEVAARQHLiNEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKGNI-VGL 482
Cdd:NF041083 395 AVEDGKIVAGGGAPEVELAKRL-REYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKwAGI 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1780591515 483 DLQDGEPVDPQLAGIFDNYSVKRQLINSGPVIASQLLLVDEVIRAG 528
Cdd:NF041083 474 NVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
3-525 |
1.46e-82 |
|
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: 264.93 E-value: 1.46e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 3 VRVLNPNAEVLNKSAALHMTINAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTA---IMIART 79
Cdd:cd03337 2 VLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAksmIELSRT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 80 avaQDDISGDGTTSTVIFIGELMKQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVvmgDEPDKEILKMVARTTL 159
Cdd:cd03337 82 ---QDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPV---DVNDRAQMLKIIKSCI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 160 RTKLYEGLADQLTDIVVNSVLCIRKPQE----PIDL--FM-VE------IMhmrhkfdvDTRLVEGLVLDHGSRHPDMKR 226
Cdd:cd03337 156 GTKFVSRWSDLMCNLALDAVKTVAVEENgrkkEIDIkrYAkVEkipggeIE--------DSRVLDGVMLNKDVTHPKMRR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 227 RAENCHILTCNVSLEYekseinagffysnaeqreamvtaerrsvdervqkiielknkvcagndnsfVILNQKGIDPPSLD 306
Cdd:cd03337 228 RIENPRIVLLDCPLEY--------------------------------------------------LVITEKGVSDLAQH 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 307 LLAREGIIALRRAKRRNMERLVLACGGEAVNSVDDLTPDCLGWAGLVYEHVL-GEEKYTFVEQVKNPHSCTILIKGPNDH 385
Cdd:cd03337 258 YLVKAGITALRRVRKTDNNRIARACGATIVNRPEELTESDVGTGAGLFEVKKiGDEYFTFITECKDPKACTILLRGASKD 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 386 TIAQIKDAVRDGLRSVKNTLEDECVVLGAGAFEVAARQHLiNEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQD 465
Cdd:cd03337 338 VLNEVERNLQDAMAVARNIILNPKLVPGGGATEMAVSHAL-SEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIR 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1780591515 466 VIISLTSEH--DKGNIVGLDLQDGEPVDPQLAGIFDNYSVKRQLINSGPVIASQLLLVDEVI 525
Cdd:cd03337 417 TLTELRAKHaqGENSTWGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
23-526 |
1.95e-82 |
|
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: 266.07 E-value: 1.95e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 23 INAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIARTAVAQDDISGDGTTSTVIFIGELM 102
Cdd:cd03335 14 VTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAELL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 103 KQSERCIDEGMHPRVLVDGFEIAKRATLQFL-DTFKTPVvmgDEPDKEILKMVARTTLRTKLYEGLADQLTDIVVNSVLC 181
Cdd:cd03335 94 KRANELVKQKIHPTTIISGYRLACKEAVKYIkEHLSISV---DNLGKESLINVAKTSMSSKIIGADSDFFANMVVDAILA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 182 IR------KPQEPIDlfMVEIMHMRHKFDVDTRLVEGLVLDHGSRHPDMKRRAENCHILTCNVSLEYEKSEINAGFFYSN 255
Cdd:cd03335 171 VKttnekgKTKYPIK--AVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKLGVQVVVTD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 256 AEQREAMVTAERRSVDERVQKIIElknkvcAGNDnsfVILNQKGIDPPSLDLLAREGIIALRRAKRRNMERLVLACGGEA 335
Cdd:cd03335 249 PEKLEKIRQRESDITKERIKKILA------AGAN---VVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 336 VNSVDDL------TPDCLGWAGLVYEHVLGEEKYTFVEQVKNPHSCTILIKGPNDHTIAQIKDAVRDGLRSVKNTLEDEC 409
Cdd:cd03335 320 VSTLANLegeetfDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 410 VVLGAGAFEVAARQHLiNEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKGNI---------V 480
Cdd:cd03335 400 VVPGGGAVETALSIYL-ENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVkpdkkhlkwY 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1780591515 481 GLDLQDGEPVDPQLAGIFDNYSVKRQLINSGPVIASQLLLVDEVIR 526
Cdd:cd03335 479 GLDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
23-526 |
7.09e-81 |
|
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: 262.35 E-value: 7.09e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 23 INAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIARTAVAQDDISGDGTTSTVIFIGELM 102
Cdd:TIGR02340 18 VTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVIIAAELL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 103 KQSERCIDEGMHPRVLVDGFEIAKRATLQFLDtfKTPVVMGDEPDKEILKMVARTTLRTKLYEGLADQLTDIVVNSVLCI 182
Cdd:TIGR02340 98 KRADELVKNKIHPTSVISGYRLACKEAVKYIK--ENLSVSVDELGREALINVAKTSMSSKIIGLDSDFFSNIVVDAVLAV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 183 R------KPQEPIDlfMVEIMHMRHKFDVDTRLVEGLVLDHGSRHPDMKRRAENCHILTCNVSLEYEKSEINAGFFYSNA 256
Cdd:TIGR02340 176 KttnengETKYPIK--AINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAKMALGVQIVVDDP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 257 EQREAMVTAERRSVDERVQKIIElknkvcAGNDnsfVILNQKGIDPPSLDLLAREGIIALRRAKRRNMERLVLACGGEAV 336
Cdd:TIGR02340 254 EKLEQIRQREADITKERIKKILD------AGAN---VVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 337 NSVDDLT------PDCLGWAGLVYEHVLGEEKYTFVEQVKNPHSCTILIKGPNDHTIAQIKDAVRDGLRSVKNTLEDECV 410
Cdd:TIGR02340 325 STLADLEgeetfeASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 411 VLGAGAFEVAARQHLiNEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKGNI---------VG 481
Cdd:TIGR02340 405 VPGGGAVEAALSIYL-ENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAQLkpekkhlkwYG 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1780591515 482 LDLQDGEPVDPQLAGIFDNYSVKRQLINSGPVIASQLLLVDEVIR 526
Cdd:TIGR02340 484 LDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIK 528
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
23-526 |
2.12e-80 |
|
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: 260.69 E-value: 2.12e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 23 INAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIARTAVAQDDISGDGTTSTVIFIGELM 102
Cdd:cd03339 29 ILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGALL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 103 KQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVVMgDEPDKEILKMVARTTLRTKLYEGLADQLTDIVVNSVLCI 182
Cdd:cd03339 109 EQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEF-SPDNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAVLSV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 183 ----RKpqePIDLfmvEIMHMRHKFD---VDTRLVEGLVLDHGSRHPDMKRRAENCHI--LTCnvSLEYEKSEINAGFFY 253
Cdd:cd03339 188 adleRK---DVNF---ELIKVEGKVGgrlEDTKLVKGIVIDKDFSHPQMPKEVKDAKIaiLTC--PFEPPKPKTKHKLDI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 254 SNAEQREAMVTAERRSVDERVQKIIElknkvcAGNDnsFVILnQKGIDPPSLDLLAREGIIALRRAKRRNMERLVLACGG 333
Cdd:cd03339 260 TSVEDYKKLQEYEQKYFREMVEQVKD------AGAN--LVIC-QWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 334 EAVNSVDDLTPDCLGWAGLVYEHVLG--EEKYTFVEQVKNPHSCTILIKGPNDHTIAQIKDAVRDGLRSVKNTLEDECVV 411
Cdd:cd03339 331 RIVPRFEDLSPEKLGKAGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIV 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 412 LGAGAFEVAARQHlINEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKGNI--VGLDLQDGEP 489
Cdd:cd03339 411 YGGGAAEISCSLA-VEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNphLGIDCLGRGT 489
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1780591515 490 VDPQLAGIFDNYSVKRQLINsgpvIASQL----LLVDEVIR 526
Cdd:cd03339 490 NDMKEQKVFETLISKKQQIL----LATQVvkmiLKIDDVIV 526
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
3-525 |
3.16e-80 |
|
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: 260.44 E-value: 3.16e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 3 VRVLNPNAEVLNKSAALHMTINAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTA---IMIART 79
Cdd:TIGR02344 2 VLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAksmIELSRT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 80 avaQDDISGDGTTSTVIFIGELMKQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVvmgDEPDKEILKMVARTTL 159
Cdd:TIGR02344 82 ---QDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPV---DVNDDAAMLKLIQSCI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 160 RTKLYEGLADQLTDIVVNSVLCIRKPQEPIdlFMVEIMHMRHKFDV------DTRLVEGLVLDHGSRHPDMKRRAENCHI 233
Cdd:TIGR02344 156 GTKFVSRWSDLMCDLALDAVRTVQRDENGR--KEIDIKRYAKVEKIpggdieDSCVLKGVMINKDVTHPKMRRYIENPRI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 234 LTCNVSLEYEKSEINAGFFYSNAEQREAMVTAERRSVDERVQKIIELKNKvcagndnsfVILNQKGIDPPSLDLLAREGI 313
Cdd:TIGR02344 234 VLLDCPLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPD---------LVITEKGVSDLAQHYLLKANI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 314 IALRRAKRRNMERLVLACGGEAVNSVDDLTPDCLGW-AGLVYEHVLGEEKYTFVEQVKNPHSCTILIKGPNDHTIAQIKD 392
Cdd:TIGR02344 305 TAIRRVRKTDNNRIARACGATIVNRPEELRESDVGTgCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVER 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 393 AVRDGLRSVKNTLEDECVVLGAGAFEVAARQHLINEVKKtVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTS 472
Cdd:TIGR02344 385 NLQDAMAVARNVLLDPKLVPGGGATEMAVSVALTEKSKK-LEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRA 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1780591515 473 EHDKGNI--VGLDLQDGEPVDPQLAGIFDNYSVKRQLINSGPVIASQLLLVDEVI 525
Cdd:TIGR02344 464 KHAQENNctWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
18-527 |
6.45e-80 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 258.47 E-value: 6.45e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 18 ALHMTINAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIAR----TAVAQDDISGDGTTS 93
Cdd:COG0459 11 ARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQlvkeVASKTNDEAGDGTTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 94 TVIFIGELMKQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVvmgdePDKEILKMVARTTLRTKlyeglaDQLTD 173
Cdd:COG0459 91 ATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPV-----DDKEELAQVATISANGD------EEIGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 174 IVVNSVLCIRKpqEPIdlFMVEimhmRHK-FDVDTRLVEGLVLDHGSRHPD-------MKRRAENCHILTCNVSLeyeks 245
Cdd:COG0459 160 LIAEAMEKVGK--DGV--ITVE----EGKgLETELEVVEGMQFDKGYLSPYfvtdpekMPAELENAYILLTDKKI----- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 246 einagffySNAEQREAMvtaerrsvderVQKIIELKNKVcagndnsfVILnQKGIDPPSLDLLAREGIIALRRA------ 319
Cdd:COG0459 227 --------SSIQDLLPL-----------LEKVAQSGKPL--------LII-AEDIDGEALATLVVNGIRGVLRVvavkap 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 320 ---KRRN--MERLVLACGGEAVN-----SVDDLTPDCLGWAGLVYEhvlGEEKYTFVEQVKNPHSCTILIKGPNDHTIAQ 389
Cdd:COG0459 279 gfgDRRKamLEDIAILTGGRVISedlglKLEDVTLDDLGRAKRVEV---DKDNTTIVEGAGNPKAIVILVGAATEVEVKE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 390 IKDAVRDGLRSVKNTLEDEcVVLGAGAFEVAARQHLiNEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIIS 469
Cdd:COG0459 356 RKRRVEDALHATRAAVEEG-IVPGGGAALLRAARAL-RELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEK 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1780591515 470 LTSEHDKGniVGLDLQDGEPVDPQLAGIFDNYSVKRQLINSGPVIASQLLLVDEVIRA 527
Cdd:COG0459 434 VRAAKDKG--FGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIAD 489
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-534 |
2.10e-78 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 255.72 E-value: 2.10e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 1 MSVRVLNPNAEVLNKSAALHMTINAAKGLQDVLKSNLGPKGTIKMLVG-----GSGDIKLTKDGNTLLKEMQIQNPTAIM 75
Cdd:PTZ00212 6 VPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQPmsegpRSGNVTVTNDGATILKSVWLDNPAAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 76 IARTAVAQDDISGDGTTSTVIFIGELMKQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVVMGDEPDKEILKMVA 155
Cdd:PTZ00212 86 LVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEKFKEDLLNIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 156 RTTLRTKLYEGLADQLTDIVVNSVLCIRkpqEPIDLFMVEIMH-----MRhkfdvDTRLVEGLVLDH--GSRHPdmkRRA 228
Cdd:PTZ00212 166 RTTLSSKLLTVEKDHFAKLAVDAVLRLK---GSGNLDYIQIIKkpggtLR-----DSYLEDGFILEKkiGVGQP---KRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 229 ENCHILTCNVSLEYEKSEINAGFFYSNA-EQREAMVTAERRSVDERVQKIIelknkvcAGNDNSFVilNQKGIDPPSLDL 307
Cdd:PTZ00212 235 ENCKILVANTPMDTDKIKIYGAKVKVDSmEKVAEIEAAEKEKMKNKVDKIL-------AHGCNVFI--NRQLIYNYPEQL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 308 LAREGIIALRRAKRRNMERLVLACGGEAVNSVDDLTPDCLGWAGLVYEHVLGEEKYTFVEQVKNPHSCTILIKGPNDHTI 387
Cdd:PTZ00212 306 FAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHIL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 388 AQIKDAVRDGLRSVKNTLEDECVVLGAGAFEVAArQHLINEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVI 467
Cdd:PTZ00212 386 DEAERSLHDALCVLSQTVKDTRVVLGGGCSEMLM-ANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELV 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1780591515 468 ISLTSEHDKGNI-VGLDLQDGEPVDPQLAGIFDNYSVKRQLINSGPVIASQLLLVDEVIRAGRNMRKP 534
Cdd:PTZ00212 465 SKLRAEHYKGNKtAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRCAPRQREQ 532
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
18-528 |
3.83e-78 |
|
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: 255.11 E-value: 3.83e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 18 ALHMTINAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIARTAVAQDDISGDGTTSTVIF 97
Cdd:TIGR02343 28 AKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVVVL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 98 IGELMKQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVVMgDEPDKEILKMVARTTLRTKLYEGLADQLTDIVVN 177
Cdd:TIGR02343 108 AGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISA-DNNNREPLIQAAKTSLGSKIVSKCHRRFAEIAVD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 178 SVLCIR-KPQEPIDLFMVEIMHMRHKFDVDTRLVEGLVLDHGSRHPDMKRRAENCH--ILTCnvSLEYEKSEINAGFFYS 254
Cdd:TIGR02343 187 AVLNVAdMERRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKiaILTC--PFEPPKPKTKHKLDIS 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 255 NAEQREAMVTAERRSVDERVQKIIElknkvcAGNDnsfVILNQKGIDPPSLDLLAREGIIALRRAKRRNMERLVLACGGE 334
Cdd:TIGR02343 265 SVEEYKKLQKYEQQKFKEMIDDIKK------SGAN---LVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 335 AVNSVDDLTPDCLGWAGLVYEHVLG--EEKYTFVEQVKNPHSCTILIKGPNDHTIAQIKDAVRDGLRSVKNTLEDECVVL 412
Cdd:TIGR02343 336 IVPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVY 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 413 GAGAFEVAARQHLINEVKKtVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKGNI--VGLDLQDGEPV 490
Cdd:TIGR02343 416 GGGAAEISCSLAVSQEADK-YPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNpnLGVDCLGYGTN 494
|
490 500 510
....*....|....*....|....*....|....*...
gi 1780591515 491 DPQLAGIFDNYSVKRQLINSGPVIASQLLLVDEVIRAG 528
Cdd:TIGR02343 495 DMKEQFVFETLIGKKQQILLATQLVRMILKIDDVISPG 532
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
31-527 |
5.46e-76 |
|
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: 248.78 E-value: 5.46e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 31 DVLKSNLGPKGTIKML--VGGSGDIKLTKDGNTLLKEMQIQNPTAIMIARTAVAQDDISGDGTTSTVIFIGELMKQSERC 108
Cdd:cd03336 27 DLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDGTTSVTVLAAELLREAEKL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 109 IDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVVMGDEPDKEILKMVARTTLRTKLYEGLADQLTDIVVNSVLCIRkpqEP 188
Cdd:cd03336 107 VAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEAFREDLLNIARTTLSSKILTQDKEHFAELAVDAVLRLK---GS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 189 IDLFMVEIMHMRHKFDVDTRLVEGLVLDH--GSRHPdmkRRAENCHILTCNVSLEYEKSEINAGFFYSNA-EQREAMVTA 265
Cdd:cd03336 184 GNLDAIQIIKKLGGSLKDSYLDEGFLLDKkiGVNQP---KRIENAKILIANTPMDTDKIKIFGAKVRVDStAKVAEIEEA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 266 ERRSVDERVQKIieLKNKVcagndNSFVilNQKGIDPPSLDLLAREGIIALRRAKRRNMERLVLACGGEAVNSVDDLTPD 345
Cdd:cd03336 261 EKEKMKNKVEKI--LKHGI-----NCFI--NRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTGGEIASTFDHPELV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 346 CLGWAGLVYEHVLGEEKYTFVEQVKNPHSCTILIKGPNDHTIAQIKDAVRDGLRSVKNTLEDECVVLGAGAFEVAArQHL 425
Cdd:cd03336 332 KLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRVVLGGGCSEMLM-AKA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 426 INEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKGN-IVGLDLQDGEPVDPQLAGIFDNYSVK 504
Cdd:cd03336 411 VEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNtTAGLDMRKGTVGDMKELGITESFKVK 490
|
490 500
....*....|....*....|...
gi 1780591515 505 RQLINSGPVIASQLLLVDEVIRA 527
Cdd:cd03336 491 RQVLLSASEAAEMILRVDDIIKC 513
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
23-527 |
1.94e-74 |
|
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: 244.89 E-value: 1.94e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 23 INAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIARTAVAQDDISGDGTTSTVIFIGELM 102
Cdd:cd03340 22 INACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEFL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 103 KQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVVMGDEPDK-EILKMVARTTLRTKLYEGLADQLTDIVVNSVLC 181
Cdd:cd03340 102 KEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKEEQrELLEKCAATALNSKLIASEKEFFAKMVVDAVLS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 182 IrkpQEPIDLFMVEIMHMRHKFDVDTRLVEGLVLDHG---SRHPDMKRRAENCHILTCNVSLEYEKSEINAGFFYSNAEQ 258
Cdd:cd03340 182 L---DDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTfsyAGFEQQPKKFKNPKILLLNVELELKAEKDNAEVRVEDPEE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 259 REAMVTAERRSVDERVQKIIElknkvCAGNdnsfVILNQKGIDPPSLDLLAREGIIALRRAKRRNMERLVLACGGEAVNS 338
Cdd:cd03340 259 YQAIVDAEWKIIYDKLEKIVK-----SGAN----VVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQTT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 339 VDDLTPDCLGWAGLVYEHVLGEEKYTFVEQVKNPHSCTILIKGPNDHTIAQIKDAVRDGLRSVKNTLEDECVVLGAGAFE 418
Cdd:cd03340 330 VSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAIE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 419 VAARQHLiNEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKGNIV--GLDLQDGEPVDPQLAG 496
Cdd:cd03340 410 MELSKYL-RDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKwyGVDINNEGIADNFEAF 488
|
490 500 510
....*....|....*....|....*....|.
gi 1780591515 497 IFDNYSVKRQLINSGPVIASQLLLVDEVIRA 527
Cdd:cd03340 489 VWEPSLVKINALTAATEAACLILSVDETIKN 519
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
23-527 |
2.57e-73 |
|
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: 241.97 E-value: 2.57e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 23 INAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIARTAVAQDDISGDGTTSTVIFIGELM 102
Cdd:TIGR02345 24 INACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGELL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 103 KQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVVMGDEPDKEILKMVARTTLRTKLYEGLADQLTDIVVNSVLCI 182
Cdd:TIGR02345 104 KEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKGEQRELLEKCAATALSSKLISHNKEFFSKMIVDAVLSL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 183 RKpqEPIDLFMVEIMHMRHKFDVDTRLVEGLVLDHG---SRHPDMKRRAENCHILTCNVSLEYEKSEINAGFFYSNAEQR 259
Cdd:TIGR02345 184 DR--DDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTfsyAGFEQQPKKFANPKILLLNVELELKAEKDNAEIRVEDVEDY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 260 EAMVTAERRSVDERVQKIIElknkvcAGNDnsfVILNQKGIDPPSLDLLAREGIIALRRAKRRNMERLVLACGGEAVNSV 339
Cdd:TIGR02345 262 QAIVDAEWAIIFRKLEKIVE------SGAN---VVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 340 DDLTPDCLGWAGLVYEHVLGEEKYTFVEQVKNPHSCTILIKGPNDHTIAQIKDAVRDGLRSVKNTLEDECVVLGAGAFEV 419
Cdd:TIGR02345 333 SDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIEM 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 420 AARQHLiNEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKGNI-VGLDLQDGEPVDPQLAGIF 498
Cdd:TIGR02345 413 ELSKCL-RDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKwYGVDINTEDIGDNFEAFVW 491
|
490 500
....*....|....*....|....*....
gi 1780591515 499 DNYSVKRQLINSGPVIASQLLLVDEVIRA 527
Cdd:TIGR02345 492 EPALVKINALKAAFEAACTILSVDETITN 520
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
31-527 |
8.32e-70 |
|
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: 232.83 E-value: 8.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 31 DVLKSNLGPKGTIKMLVGGS--GDIKLTKDGNTLLKEMQIQNPTAIMIARTAVAQDDISGDGTTSTVIFIGELMKQSERC 108
Cdd:TIGR02341 28 DLVKSTLGPKGMDKILQSSSsdASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEVGDGTTSVTVLAAELLREAEKL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 109 IDEGMHPRVLVDGFEIAKRATLQFLDtfKTPVVMGDEPDK--EILKMVARTTLRTKLYEGLADQLTDIVVNSVLCIRKPQ 186
Cdd:TIGR02341 108 INQKIHPQTIIAGYREATKAARDALL--KSAVDNGSDEVKfrQDLMNIARTTLSSKILSQHKDHFAQLAVDAVLRLKGSG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 187 epiDLFMVEIMHMRHKFDVDTRLVEGLVLDH--GSRHPdmkRRAENCHILTCNVSLEYEKSEINAGFFYSNAEQREAMV- 263
Cdd:TIGR02341 186 ---NLEAIQIIKKLGGSLADSYLDEGFLLDKkiGVNQP---KRIENAKILIANTGMDTDKVKIFGSRVRVDSTAKVAELe 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 264 TAERRSVDERVQKIIelknkvcAGNDNSFVilNQKGIDPPSLDLLAREGIIALRRAKRRNMERLVLACGGEAVNSVDDLT 343
Cdd:TIGR02341 260 HAEKEKMKEKVEKIL-------KHGINCFI--NRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIVSTFDHPE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 344 PDCLGWAGLVYEHVLGEEKYTFVEQVKNPHSCTILIKGPNDHTIAQIKDAVRDGLRSVKNTLEDECVVLGAGAFEVAArQ 423
Cdd:TIGR02341 331 LVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGGGCSEMLM-S 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 424 HLINEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKGN-IVGLDLQDGEPVDPQLAGIFDNYS 502
Cdd:TIGR02341 410 KAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNtTMGLDMNEGTIADMRQLGITESYK 489
|
490 500
....*....|....*....|....*
gi 1780591515 503 VKRQLINSGPVIASQLLLVDEVIRA 527
Cdd:TIGR02341 490 VKRAVVSSAAEAAEVILRVDNIIKA 514
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
23-491 |
3.52e-69 |
|
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: 231.02 E-value: 3.52e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 23 INAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIARTAVAQDDISGDGTTSTVIFIGELM 102
Cdd:cd03338 14 IQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGALL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 103 KQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVvmgDEPDKEILKMVARTTLRTKLYEGLADQLTDIVVNSVLCI 182
Cdd:cd03338 94 SACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPV---DLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 183 RKPQEP--IDLFMVEIMHMRHKFDVDTRLVEGLVLDH-GSRHPDMKRRAENCHILTCNVSLEYEKSEINAGFFYSNAEQR 259
Cdd:cd03338 171 IDPATAtnVDLKDIRIVKKLGGTIEDTELVDGLVFTQkASKKAGGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVNDYAQM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 260 EAMVTAERrsvdervQKIIELKNKVCAGNDNsfVILNQKGI-----DPPSLDLLAREGIIALRRAKRRNMERLVLACGGE 334
Cdd:cd03338 251 DRILREER-------KYILNMCKKIKKSGCN--VLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 335 AVNSVDDLTPDCLGWAGLVYEHVLGEEKYTFVEQVKNP-HSCTILIKGPNDHTIAQIKDAVRDGLRSVKNTLEDECVVLG 413
Cdd:cd03338 322 PVASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPG 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1780591515 414 AGAFEVAARQHLiNEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKGNI-VGLDLQDGEPVD 491
Cdd:cd03338 402 GGAPEIEIALQL-SEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKnAGINVRKGAITN 479
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
148-407 |
1.60e-68 |
|
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: 219.26 E-value: 1.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 148 KEILKMVARTTLRTKLYEGlADQLTDIVVNSVLCIRKPQEPIDLFMVEIMHMRHKFDVDTRLVEGLVLDHGSRHPDMKRR 227
Cdd:cd03333 1 RELLLQVATTSLNSKLSSW-DDFLGKLVVDAVLKVGPDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYMPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 228 AENCHILTCNVSLEYekseinagffysnaeqreamvtaerrsvdervqkiielknkvcagndnsfVILNQKGIDPPSLDL 307
Cdd:cd03333 80 LENAKILLLDCPLEY--------------------------------------------------VVIAEKGIDDLALHY 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 308 LAREGIIALRRAKRRNMERLVLACGGEAVNSVDDLTPDCLGWAGLVYEHVLGEEKYTFVEQVKNPHSCTILIKGPNDHTI 387
Cdd:cd03333 110 LAKAGIMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVEL 189
|
250 260
....*....|....*....|
gi 1780591515 388 AQIKDAVRDGLRSVKNTLED 407
Cdd:cd03333 190 DEVKRSLHDALCAVRAAVEE 209
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
23-491 |
1.59e-67 |
|
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: 226.59 E-value: 1.59e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 23 INAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIARTAVAQDDISGDGTTSTVIFIGELM 102
Cdd:TIGR02342 15 IVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGALL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 103 KQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVvmgDEPDKEILKMVARTTLRTKLYEGLADQLTDIVVNSVLCI 182
Cdd:TIGR02342 95 GACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPV---DLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVLKV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 183 RKPQEP--IDLFMVEIMHMRHKFDVDTRLVEGLVLD-HGSRHPDMKRRAENCHILTCNVSLEYEKSEINAGFFYSNAEQR 259
Cdd:TIGR02342 172 IDPENAknVDLNDIKVVKKLGGTIDDTELIEGLVFTqKASKSAGGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDYAQM 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 260 EAMVTAERrsvdervQKIIELKNKVCAGNDNsfVILNQKGI-----DPPSLDLLAREGIIALRRAKRRNMERLVLACGGE 334
Cdd:TIGR02342 252 DRVLKEER-------AYILNIVKKIKKTGCN--VLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 335 AVNSVDDLTPDCLGWAGLVYEHVLGEEKYTFVEQVKNP-HSCTILIKGPNDHTIAQIKDAVRDGLRSVKNTLEDECVVLG 413
Cdd:TIGR02342 323 PIASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAG 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1780591515 414 AGAFEVAARQHLINEvKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKGNI-VGLDLQDGEPVD 491
Cdd:TIGR02342 403 GGAPEIEIARRLSKY-ARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKtAGISVRKGGITN 480
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
23-527 |
1.79e-59 |
|
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: 203.99 E-value: 1.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 23 INAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIARTAVAQDDISGDGTTSTVIFIGELM 102
Cdd:cd03341 14 IEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGELL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 103 KQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVVmGDEPDKEILKMVARTTLRTKLYeGLADQLTDIVVNSVLCI 182
Cdd:cd03341 94 EKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKI-EDLRNKEEVSKALKTAIASKQY-GNEDFLSPLVAEACISV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 183 rKPQEPidlfmveimhmrHKFDVD--------------TRLVEGLVLdhgSRHP--DMKRrAENCHI--LTCNVsleyek 244
Cdd:cd03341 172 -LPENI------------GNFNVDnirvvkilggsledSKVVRGMVF---KREPegSVKR-VKKAKVavFSCPF------ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 245 seinagffysnaeqreamvtaerrsvDERVQKIielknkVCAGNdnsfvilnqkgIDPPSLDLLAREGIIALRRAKRRNM 324
Cdd:cd03341 229 --------------------------DIGVNVI------VAGGS-----------VGDLALHYCNKYGIMVIKINSKFEL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 325 ERLVLACGGEAVNSVDDLTPDCLGWAGLVYEHVLGEEKYTFVEQVKNPHS-CTILIKGPNDHTIAQIKDAVRDGLRSVKN 403
Cdd:cd03341 266 RRLCRTVGATPLPRLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDSKiATIVLRGATQNILDDVERAIDDGVNVFKS 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 404 TLEDECVVLGAGAFEVAArQHLINEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKGNI-VGL 482
Cdd:cd03341 346 LTKDGRFVPGAGATEIEL-AKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKsAGV 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1780591515 483 DLQDGEP--VDPQLAGIFDNYSVKRQLINSGPVIASQLLLVDEVIRA 527
Cdd:cd03341 425 DIESGDEgtKDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMA 471
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
18-534 |
3.97e-58 |
|
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: 201.87 E-value: 3.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 18 ALHMTINAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIARTAVAQDDISGDGTTSTVIF 97
Cdd:TIGR02346 19 AVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 98 IGELMKQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVVMGDEPDKEILKMVaRTTLRTKLYeGLADQLTDIVVN 177
Cdd:TIGR02346 99 AGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDLRDKDELIKAL-KASISSKQY-GNEDFLAQLVAQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 178 SVLCIR-KPQEPIDLFMVEIMHMRHKFDVDTRLVEGLVLdhgSRHPDMK-RRAENCHILTCNVSLEYEKSEINAGFFYSN 255
Cdd:TIGR02346 177 ACSTVLpKNPQNFNVDNIRVCKILGGSLSNSEVLKGMVF---NREAEGSvKSVKNAKVAVFSCPLDTATTETKGTVLIHN 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 256 AEQREAMVTAERRSVDERVQKIIElknkvcAGNDnsfVILNQKGIDPPSLDLLAREGIIALRRAKRRNMERLVLACGGEA 335
Cdd:TIGR02346 254 AEELLNYSKGEENQIEAMIKAIAD------SGVN---VIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 336 VNSVDDLTPDCLGWAGLVYEHVLGEEKYTFVEQVKNPHSC-TILIKGPNDHTIAQIKDAVRDGLRSVKNTLEDECVVLGA 414
Cdd:TIGR02346 325 LPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGDSKIsTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 415 GAFEVAARQHLInEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKGNI-VGLDLQDGEP--VD 491
Cdd:TIGR02346 405 GATEIELASRLT-KYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKsKGIDIEAESDgvKD 483
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1780591515 492 PQLAGIFDNYSVKRQLINSGPVIASQLLLVDEVIragrnMRKP 534
Cdd:TIGR02346 484 ASEAGIYDMLATKKWAIKLATEAAVTVLRVDQII-----MAKP 521
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
29-524 |
2.71e-15 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 78.42 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 29 LQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPT----AIMIARTAVAQDDISGDGTTSTVIFIGELMKQ 104
Cdd:PTZ00114 34 LADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKAGDGTTTATILARAIFRE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 105 SERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVvmgdEPDKEILKmVArtTLRT----KLYEGLADQLTDIVVNSVL 180
Cdd:PTZ00114 114 GCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPV----KTKEDILN-VA--TISAngdvEIGSLIADAMDKVGKDGTI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 181 CIrkpqepidlfmVEIMHMRHKFDVdtrlVEGLVLDHGSRHP-------DMKRRAENCHILTCNVSLEYEKSEINAgFFY 253
Cdd:PTZ00114 187 TV-----------EDGKTLEDELEV----VEGMSFDRGYISPyfvtnekTQKVELENPLILVTDKKISSIQSILPI-LEH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 254 SNAEQREAMVTAErrSVDERV-QKII--ELKN--KVCAgndnsfvilnqkgIDPPSLDllaregiialrRAKRRNMERLV 328
Cdd:PTZ00114 251 AVKNKRPLLIIAE--DVEGEAlQTLIinKLRGglKVCA-------------VKAPGFG-----------DNRKDILQDIA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 329 LACGGEAVNSV------DDLTPDCLGWAGLV--------------YEHVLGEEKYTFVEQVKNPHS-------------- 374
Cdd:PTZ00114 305 VLTGATVVSEDnvglklDDFDPSMLGSAKKVtvtkdetviltgggDKAEIKERVELLRSQIERTTSeydkeklkerlakl 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 375 ----CTILIKGPNDHTIAQIKDAVRDGLRSVKNTLEdECVVLGAG-AFEVAARQHLINEVKKTVQGRAQLGVEAFANALL 449
Cdd:PTZ00114 385 sggvAVIKVGGASEVEVNEKKDRIEDALNATRAAVE-EGIVPGGGvALLRASKLLDKLEEDNELTPDQRTGVKIVRNALR 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1780591515 450 VVPKTLAENAGLDTQDVIISLTSEHDKGniVGLDLQDGEPVDPQLAGIFDNYSVKRQLINSGPVIASqLLLVDEV 524
Cdd:PTZ00114 464 LPTKQIAENAGVEGAVVVEKILEKKDPS--FGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVAS-LMLTTEA 535
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
11-525 |
1.79e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 66.69 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 11 EVLNKSAALHMTINAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNP----TAIMIARTAVAQDDI 86
Cdd:PRK12851 5 EVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 87 SGDGTTSTVIFIGELMKQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVvmgdEPDKEILKMVARTTLR-TKLYE 165
Cdd:PRK12851 85 AGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPV----TTNAEIAQVATISANGdAEIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 166 GLADQLTDIVVNSVLCIRKPQepidlfmveimhmrhKFDVDTRLVEGLVLDHGSRHPdmkrraenchiltcnvsleyeks 245
Cdd:PRK12851 161 LVAEAMEKVGNEGVITVEESK---------------TAETELEVVEGMQFDRGYLSP----------------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 246 einagFFYSNAEQREAMVTAERRSVDER----VQKIIELKNKVCAGNDNSFVIlnQKGIDPPSLDLLAREGI-----IAL 316
Cdd:PRK12851 203 -----YFVTDADKMEAELEDPYILIHEKkisnLQDLLPVLEAVVQSGKPLLII--AEDVEGEALATLVVNKLrgglkVAA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 317 RRA-----KRRNM-ERLVLACGGEAVN-----SVDDLTPDCLGWAGLVyehVLGEEKYTFV------------------- 366
Cdd:PRK12851 276 VKApgfgdRRKAMlEDIAILTGGTVISedlgiKLENVTLEQLGRAKKV---VVEKENTTIIdgagskteiegrvaqiraq 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 367 -EQVKNPHS---------------CTILIKGPNDHTIAQIKDAVRDGLRSVKNTLEdECVVLGAGAFEVAARQHLINEvk 430
Cdd:PRK12851 353 iEETTSDYDreklqerlaklaggvAVIRVGASTEVEVKEKKDRVDDALHATRAAVE-EGIVPGGGVALLRAVKALDKL-- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 431 KTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEhdKGNIvGLDLQDGEPVDPQLAGIFDNYSVKRQLINS 510
Cdd:PRK12851 430 ETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREK--PGGY-GFNAATNEYGDLYAQGVIDPVKVVRTALQN 506
|
570
....*....|....*
gi 1780591515 511 GPVIASQLLLVDEVI 525
Cdd:PRK12851 507 AASVAGLLLTTEAMV 521
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
29-525 |
4.16e-10 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 62.36 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 29 LQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQI----QNPTAIMIARTAVAQDDISGDGTTSTVIFIGELMKQ 104
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 105 SERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVVMGDEpdkeiLKMVARTTLR--TKLYEGLADQLTDIVVNSVLCI 182
Cdd:PRK14104 103 GAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDE-----IAQVGTISANgdAEIGKFLADAMKKVGNEGVITV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 183 RKPQEpidlfmveimhmrhkFDVDTRLVEGLVLDHGSRHPdmkrraenchiltcnvsleyekseinagFFYSNA-----E 257
Cdd:PRK14104 178 EEAKS---------------LETELDVVEGMQFDRGYISP----------------------------YFVTNAdkmrvE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 258 QREAMVTAERRSVDERVQKIIELKNKVCAGNDNSFVILNQKGIDPPSLDLLAREGIIALRRAK------RRN--MERLVL 329
Cdd:PRK14104 215 MDDAYILINEKKLSSLNELLPLLEAVVQTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKapgfgdRRKamLQDIAI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 330 ACGGEAVNS-----VDDLTPDCLGWAGLVyehVLGEEKYTFVE-----------------QVKNPHS------------- 374
Cdd:PRK14104 295 LTGGQAISEdlgikLENVTLQMLGRAKKV---MIDKENTTIVNgagkkadiearvaqikaQIEETTSdydreklqerlak 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 375 -----CTILIKGPNDHTIAQIKDAVRDGLRSVKNTLEdECVVLGAGAFEVAARQHLinEVKKTVQGRAQLGVEAFANALL 449
Cdd:PRK14104 372 laggvAVIRVGGATEVEVKERKDRVDDAMHATRAAVE-EGIVPGGGVALLRASEQL--KGIKTKNDDQKTGVEIVRKALS 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1780591515 450 VVPKTLAENAGLDTQdVIISLTSEHDKGNIvGLDLQDGEPVDPQLAGIFDNYSVKRQLINSGPVIASQLLLVDEVI 525
Cdd:PRK14104 449 APARQIAINAGEDGS-VIVGKILEKEQYSY-GFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMV 522
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
29-156 |
1.67e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 60.24 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 29 LQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQI----QNPTAIMIARTAVAQDDISGDGTTSTVIFIGELMKQ 104
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1780591515 105 SERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVVMGDE----------PDKEILKMVAR 156
Cdd:PRK12852 103 GAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEiaqvgtisanGDAAIGKMIAQ 164
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
29-155 |
1.72e-09 |
|
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: 60.16 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 29 LQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIAR----TAVAQDDISGDGTTSTVIFIGELMKQ 104
Cdd:cd03344 20 LADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQlvkeVASKTNDVAGDGTTTATVLARAIIKE 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1780591515 105 SERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVVMGDE----------PDKEILKMVA 155
Cdd:cd03344 100 GLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEiaqvatisanGDEEIGELIA 160
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
205-428 |
2.92e-09 |
|
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: 58.00 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 205 VDTRLVEGLVLDHGSRHPDMKRRAENCHILTCNVSLEYEKSEinaGFFYSnaeqREAMVTAERRSVDERVQKIIELKNKV 284
Cdd:cd03334 61 SDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQRVE---NKLLS----LDPVILQEKEYLKNLVSRIVALRPDV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 285 cagndnsfvILNQKGIDPPSLDLLAREGIIALRRAKRRNMERLVLACGGEAVNSVDDL-TPDCLGWAGLVYEHVLGEEK- 362
Cdd:cd03334 134 ---------ILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDLlTSPKLGTCESFRVRTYVEEHg 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 363 ----YTFVEQVKNPHSCTILIKGPNdhtiaqikdavRDGLRSVKNTLEdecvvlgagaFEVAARQHLINE 428
Cdd:cd03334 205 rsktLMFFEGCPKELGCTILLRGGD-----------LEELKKVKRVVE----------FMVFAAYHLKLE 253
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
29-140 |
8.86e-07 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 51.46 E-value: 8.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 29 LQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPT----AIMIARTAVAQDDISGDGTTSTVIFIGELMKQ 104
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVenigAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAE 157
|
90 100 110
....*....|....*....|....*....|....*.
gi 1780591515 105 SERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPV 140
Cdd:PLN03167 158 GVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEV 193
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
37-140 |
7.30e-05 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 45.48 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 37 LGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNP---TAIMIARTAVAQ-DDISGDGTTSTVIFIGELMKQSERCIDEG 112
Cdd:CHL00093 30 LGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHienTGVALIRQAASKtNDVAGDGTTTATVLAYAIVKQGMKNVAAG 109
|
90 100
....*....|....*....|....*...
gi 1780591515 113 MHPRVLVDGFEIAKRATLQFLDTFKTPV 140
Cdd:CHL00093 110 ANPISLKRGIEKATQYVVSQIAEYARPV 137
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
396-519 |
5.75e-03 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 39.32 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780591515 396 DGLRSVKNTLEdECVVLGAGAFEVAARQHLINEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGlDTQDVIISLTSEHD 475
Cdd:CHL00093 397 DAINATKAAVE-EGIVPGGGATLVHLSENLKTWAKNNLKEDELIGALIVARAILAPLKRIAENAG-KNGSVIIEKVQEQD 474
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1780591515 476 KGniVGLDLQDGEPVDPQLAGIFDNYSVKRQLINSGPVIASQLL 519
Cdd:CHL00093 475 FE--IGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMIL 516
|
|
| |
