|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
20-529 |
0e+00 |
|
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: 754.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 20 RMYSGLEEAVFRNISACKEFAQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHPAAKLIVMASQMQDAEVGD 99
Cdd:cd03341 1 RHYSGLEEAVLRNIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 100 GTNFVVVLAGALLESAEELLRLGITTAEISDGYEKALEKALEILPNLVSHKIEDYRNVEKVKEVLRTSIMSKQYGQEDFL 179
Cdd:cd03341 81 GTNLVVVLAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLRNKEEVSKALKTAIASKQYGNEDFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 180 NDLVSKACVSILPDE-GTFNVDNIRICKILGSGLTKSEVVRGMVFKRFVEGDVTYAEKAKIVIFSCPVDIiqtetkGTVL 258
Cdd:cd03341 161 SPLVAEACISVLPENiGNFNVDNIRVVKILGGSLEDSKVVRGMVFKREPEGSVKRVKKAKVAVFSCPFDI------GVNV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 259 IksadellsFSSGEESllesqikaiadagvkvvvaggkvgDMALHFLNKYGLMAVRLNSKFDLRRLSRSVNATVLPRITT 338
Cdd:cd03341 235 I--------VAGGSVG------------------------DLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 339 PSQEELGYCDKVCIEELGDTTIVAFRNEGKDSRIATVVIRGATDNFMDDIERALDDAINNFKCLTRDGRYLPGAGATEIE 418
Cdd:cd03341 283 PTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 419 LATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHNNEaGKTIGFDIEAEKASTIDTTKAKL 498
Cdd:cd03341 363 LAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKG-NKSAGVDIESGDEGTKDAKEAGI 441
|
490 500 510
....*....|....*....|....*....|.
gi 19921848 499 FDLYQSKFWGLKYAVGAAATILKVDQIIMAK 529
Cdd:cd03341 442 FDHLATKKWAIKLATEAAVTVLRVDQIIMAK 472
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
10-539 |
0e+00 |
|
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: 730.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 10 GVSQMLKDGARMYSGLEEAVFRNISACKEFAQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHPAAKLIVMA 89
Cdd:TIGR02346 1 GIASLLKEGYRHFSGLEEAVIKNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 90 SQMQDAEVGDGTNFVVVLAGALLESAEELLRLGITTAEISDGYEKALEKALEILPNLVSHKIEDYRNVEKVKEVLRTSIM 169
Cdd:TIGR02346 81 SEMQENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDLRDKDELIKALKASIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 170 SKQYGQEDFLNDLVSKACVSILP-DEGTFNVDNIRICKILGSGLTKSEVVRGMVFKRFVEGDVTYAEKAKIVIFSCPVDI 248
Cdd:TIGR02346 161 SKQYGNEDFLAQLVAQACSTVLPkNPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNREAEGSVKSVKNAKVAVFSCPLDT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 249 IQTETKGTVLIKSADELLSFSSGEESLLESQIKAIADAGVKVVVAGGKVGDMALHFLNKYGLMAVRLNSKFDLRRLSRSV 328
Cdd:TIGR02346 241 ATTETKGTVLIHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 329 NATVLPRITTPSQEELGYCDKVCIEELGDTTIVAFRNEGKDSRIATVVIRGATDNFMDDIERALDDAINNFKCLTRDGRY 408
Cdd:TIGR02346 321 GATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 409 LPGAGATEIELATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHnNEAGKTIGFDIEAEKA 488
Cdd:TIGR02346 401 LPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAH-KKGNKSKGIDIEAESD 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 19921848 489 STIDTTKAKLFDLYQSKFWGLKYAVGAAATILKVDQIIMAKRAGGPKVRQA 539
Cdd:TIGR02346 480 GVKDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKPAGGPKPPQG 530
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
40-529 |
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: 524.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 40 AQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHPAAKLIVMASQMQDAEVGDGTNFVVVLAGALLESAEELL 119
Cdd:pfam00118 2 ADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 120 RLGITTAEISDGYEKALEKALEILPNLVSHKIEDYrNVEKVKEVLRTSIMSKQYGQE-DFLNDLVSKACVSILPDEGTFN 198
Cdd:pfam00118 82 AAGVHPTTIIEGYEKALEKALEILDSIISIPVEDV-DREDLLKVARTSLSSKIISREsDFLAKLVVDAVLAIPKNDGSFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 199 VDNIRICKILGSGLTKSEVVRGMVFKRFVEGD--VTYAEKAKIVIFSCPVDIIQTETKGTVLIKSADELLSFSSGEESLL 276
Cdd:pfam00118 161 LGNIGVVKILGGSLEDSELVDGVVLDKGPLHPdmPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 277 ESQIKAIADAGVKVVVAGGKVGDMALHFLNKYGLMAVRLNSKFDLRRLSRSVNATVLPRITTPSQEELGYCDKVCIEELG 356
Cdd:pfam00118 241 LEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEKIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 357 DTTIVAFRNeGKDSRIATVVIRGATDNFMDDIERALDDAINNFKCLTRDGRYLPGAGATEIELATQLSAYADTLPGLDQY 436
Cdd:pfam00118 321 DEKYTFIEG-CKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGKEQL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 437 AVRKFANALEVFPKALAENSGINGTEIVNQLYLAHNNeAGKTIGFDIeaEKASTIDTTKAKLFDLYQSKFWGLKYAVGAA 516
Cdd:pfam00118 400 AIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHAS-GEKHAGIDV--ETGEIIDMKEAGVVDPLKVKRQALKSATEAA 476
|
490
....*....|...
gi 19921848 517 ATILKVDQIIMAK 529
Cdd:pfam00118 477 STILRIDDIIKAK 489
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
23-527 |
3.90e-168 |
|
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: 484.62 E-value: 3.90e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 23 SGLEEAVFRNISACKEFAQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHPAAKLIVMASQMQDAEVGDGTN 102
Cdd:cd00309 4 EFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDGTT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 103 FVVVLAGALLESAEELLRLGITTAEISDGYEKALEKALEILPNLVSHKIEDyrNVEKVKEVLRTSIMSKQ-YGQEDFLND 181
Cdd:cd00309 84 TVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVE--DREELLKVATTSLNSKLvSGGDDFLGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 182 LVSKACVSILPDEGTFNVDNIRICKILGSGLTKSEVVRGMVFKRFVEGDV--TYAEKAKIVIFSCPVDiiqtetkgTVLI 259
Cdd:cd00309 162 LVVDAVLKVGKENGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYmpKRLENAKILLLDCKLE--------YVVI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 260 ksadellsfssgeeslleSQiKAIADagvkvvvaggkvgdMALHFLNKYGLMAVRLNSKFDLRRLSRSVNATVLPRITTP 339
Cdd:cd00309 234 ------------------AE-KGIDD--------------EALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLEDL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 340 SQEELGYCDKVCIEELGDTTIVAFRnEGKDSRIATVVIRGATDNFMDDIERALDDAINNFKCLTRDGRYLPGAGATEIEL 419
Cdd:cd00309 281 TPEDLGTAGLVEETKIGDEKYTFIE-GCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGAAEIEL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 420 ATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHNNEaGKTIGFDIEAEKasTIDTTKAKLF 499
Cdd:cd00309 360 SKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEG-GGNAGGDVETGE--IVDMKEAGII 436
|
490 500
....*....|....*....|....*...
gi 19921848 500 DLYQSKFWGLKYAVGAAATILKVDQIIM 527
Cdd:cd00309 437 DPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
15-529 |
1.43e-119 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 362.28 E-value: 1.43e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 15 LKDGARMYSGlEEAVFRNISACKEFAQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHPAAKLIVMASQMQD 94
Cdd:NF041082 6 LKEGTQRTSG-RDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 95 AEVGDGTNFVVVLAGALLESAEELLRLGITTAEISDGYEKALEKALEILpNLVSHKIEDyRNVEKVKEVLRTSIMSKQYG 174
Cdd:NF041082 85 DEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEIL-DEIAIKVDP-DDKETLKKIAATAMTGKGAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 175 Q-EDFLNDLVSKACVSILPDEGTFNVD--NIRICKILGSGLTKSEVVRGMVF--KRFVEGDVTYAEKAKIVIFSCPVDII 249
Cdd:NF041082 163 AaKDKLADLVVDAVKAVAEKDGGYNVDldNIKVEKKVGGSIEDSELVEGVVIdkERVHPGMPKRVENAKIALLDAPLEVK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 250 QTETKGTVLIKSADELLSFSSGEESLLESQIKAIADAGVKVVVAGGKVGDMALHFLNKYGLMAVRLNSKFDLRRLSRSVN 329
Cdd:NF041082 243 KTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 330 ATVLPRITTPSQEELGYCDKVCIEELGDTTIVaFRNEGKDSRIATVVIRGATDNFMDDIERALDDAINNFKCLTRDGRYL 409
Cdd:NF041082 323 ARIVTSIDDLSPEDLGYAGLVEERKVGGDKMI-FVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 410 PGAGATEIELATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHnNEAGKTIGFDIEAEKas 489
Cdd:NF041082 402 AGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAH-EKGNKTAGLDVYTGK-- 478
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 19921848 490 TIDTTKAKLFDLYQSKFWGLKYAVGAAATILKVDQIIMAK 529
Cdd:NF041082 479 VVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
15-529 |
4.45e-117 |
|
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: 355.80 E-value: 4.45e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 15 LKDGARMYSGlEEAVFRNISACKEFAQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHPAAKLIVMASQMQD 94
Cdd:cd03343 4 LKEGTQRTSG-RDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 95 AEVGDGTNFVVVLAGALLESAEELLRLGITTAEISDGYEKALEKALEILPNLVShKIeDYRNVEKVKEVLRTSIMSKQYG 174
Cdd:cd03343 83 EEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAI-KV-DPDDKDTLRKIAKTSLTGKGAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 175 QE-DFLNDLVSKACVSIL---PDEGTFNVDNIRICKILGSGLTKSEVVRGMVF-KRFVEGDVTYA-EKAKIVIFSCPVDI 248
Cdd:cd03343 161 AAkDKLADLVVDAVLQVAekrDGKYVVDLDNIKIEKKTGGSVDDTELIRGIVIdKEVVHPGMPKRvENAKIALLDAPLEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 249 IQTETKGTVLIKSADELLSFSSGEESLLESQIKAIADAGVKVVVAGGKVGDMALHFLNKYGLMAVRLNSKFDLRRLSRSV 328
Cdd:cd03343 241 KKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 329 NATVLPRITTPSQEELGYCDKVCIEELGDTTIVaFRNEGKDSRIATVVIRGATDNFMDDIERALDDAINNFKCLTRDGRY 408
Cdd:cd03343 321 GAKIVTNIDDLTPEDLGEAELVEERKVGDDKMV-FVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 409 LPGAGATEIELATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHNNEaGKTIGFDIEAEKA 488
Cdd:cd03343 400 VAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKG-NKNAGLDVYTGEV 478
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 19921848 489 stIDTTKAKLFDLYQSKFWGLKYAVGAAATILKVDQIIMAK 529
Cdd:cd03343 479 --VDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
15-529 |
1.70e-114 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 349.25 E-value: 1.70e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 15 LKDGARMYSGlEEAVFRNISACKEFAQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHPAAKLIVMASQMQD 94
Cdd:NF041083 6 LKEGTQRTKG-RDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 95 AEVGDGTNFVVVLAGALLESAEELLRLGITTAEISDGYEKALEKALEILpNLVSHKIeDYRNVEKVKEVLRTSIMSKQYG 174
Cdd:NF041083 85 DEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEIL-DEIAEKV-DPDDRETLKKIAETSLTSKGVE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 175 QE-DFLNDLVSKACVSILPDEG---TFNVDNIRICKILGSGLTKSEVVRGMVF-KRFVEGDV-TYAEKAKIVIFSCPVDI 248
Cdd:NF041083 163 EArDYLAEIAVKAVKQVAEKRDgkyYVDLDNIQIEKKHGGSIEDTQLIYGIVIdKEVVHPGMpKRVENAKIALLDAPLEV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 249 IQTETKGTVLIKSADELLSFSSGEESLLESQIKAIADAGVKVVVAGGKVGDMALHFLNKYGLMAVRLNSKFDLRRLSRSV 328
Cdd:NF041083 243 KKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKAT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 329 NATVLPRITTPSQEELGYCDKVCIEELGDTTIVaFRNEGKDSRIATVVIRGATDNFMDDIERALDDAINNFKCLTRDGRY 408
Cdd:NF041083 323 GARIVTNIDDLTPEDLGYAELVEERKVGDDKMV-FVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 409 LPGAGATEIELATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHNNEaGKTIGFDIEAEKA 488
Cdd:NF041083 402 VAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKG-KKWAGINVFTGEV 480
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 19921848 489 stIDTTKAKLFDLYQSKFWGLKYAVGAAATILKVDQIIMAK 529
Cdd:NF041083 481 --VDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
14-528 |
1.92e-108 |
|
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: 333.58 E-value: 1.92e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 14 MLKDGARMYSGlEEAVFRNISACKEFAQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHPAAKLIVMASQMQ 93
Cdd:TIGR02339 4 ILKEGTQRTSG-RDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 94 DAEVGDGTNFVVVLAGALLESAEELLRLGITTAEISDGYEKALEKALEILPNLVSHKIEDYRnvEKVKEVLRTSIMSKQY 173
Cdd:TIGR02339 83 DEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDR--DLLKKIAYTSLTSKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 174 GQE--DFLNDLVSKAC--VSILPDEGTFNVD--NIRICKILGSGLTKSEVVRGMVFKRFV--EGDVTYAEKAKIVIFSCP 245
Cdd:TIGR02339 161 AEVakDKLADLVVEAVkqVAELRGDGKYYVDldNIKIVKKKGGSIEDTELVEGIVVDKEVvhPGMPKRVENAKIALLDAP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 246 VDIIQTETKGTVLIKSADELLSFSSGEESLLESQIKAIADAGVKVVVAGGKVGDMALHFLNKYGLMAVRLNSKFDLRRLS 325
Cdd:TIGR02339 241 LEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 326 RSVNATVLPRITTPSQEELGYCDKVCIEELGDTTIVaFRNEGKDSRIATVVIRGATDNFMDDIERALDDAINNFKCLTRD 405
Cdd:TIGR02339 321 RATGARIVSSIDEITESDLGYAELVEERKVGEDKMV-FVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALED 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 406 GRYLPGAGATEIELATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHNNEAgKTIGFDIEA 485
Cdd:TIGR02339 400 GKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGN-KNAGINVFT 478
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 19921848 486 EKAStiDTTKAKLFDLYQSKFWGLKYAVGAAATILKVDQIIMA 528
Cdd:TIGR02339 479 GEIE--DMLELGVIEPLRVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
27-526 |
2.04e-84 |
|
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: 271.48 E-value: 2.04e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 27 EAVFRNISACKEFAQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHPAAKLIVMASQMQDAEVGDGTNFVVV 106
Cdd:cd03339 23 EAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 107 LAGALLESAEELLRLGITTAEISDGYEKALEKALEILPNlVSHKIE-DYRNVEKVKEVLRTSIMSK-QYGQEDFLNDLVS 184
Cdd:cd03339 103 LAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEE-IADKIEfSPDNKEPLIQTAMTSLGSKiVSRCHRQFAEIAV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 185 KACVSILPDE-GTFNVDNIRICKILGSGLTKSEVVRGMVfkrfVEGDVTYA------EKAKIVIFSCPVDIIQTETKGTV 257
Cdd:cd03339 182 DAVLSVADLErKDVNFELIKVEGKVGGRLEDTKLVKGIV----IDKDFSHPqmpkevKDAKIAILTCPFEPPKPKTKHKL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 258 LIKSADELLSFSSGEESLLESQIKAIADAGVKVVVAGGKVGDMALHFLNKYGLMAVRLNSKFDLRRLSRSVNATVLPRIT 337
Cdd:cd03339 258 DITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 338 TPSQEELGYCDKVciEELGDTTI---VAFRNEGKDSRIATVVIRGATDNFMDDIERALDDAINNFKCLTRDGRYLPGAGA 414
Cdd:cd03339 338 DLSPEKLGKAGLV--REISFGTTkdkMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGGGA 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 415 TEIELATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHNNEAGKTIGfdIEAEKASTIDTT 494
Cdd:cd03339 416 AEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKNPHLG--IDCLGRGTNDMK 493
|
490 500 510
....*....|....*....|....*....|..
gi 19921848 495 KAKLFDLYQSKFWGLKYAVGAAATILKVDQII 526
Cdd:cd03339 494 EQKVFETLISKKQQILLATQVVKMILKIDDVI 525
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
30-528 |
8.07e-84 |
|
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: 269.54 E-value: 8.07e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 30 FRNISACKEFAQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHPAAKLIVMASQMQDAEVGDGTNFVVVLAG 109
Cdd:cd03338 11 LSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 110 ALLESAEELLRLGITTAEISDGYEKALEKALEILPNlVSHKIeDYRNVEKVKEVLRTSIMSK---QYGqeDFLNDLVSKA 186
Cdd:cd03338 91 ALLSACESLLKKGIHPTVISESFQIAAKKAVEILDS-MSIPV-DLNDRESLIKSATTSLNSKvvsQYS--SLLAPIAVDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 187 CVSILPDEGTFNVD--NIRICKILGSGLTKSEVVRGMVF-KRFVE--GDVTYAEKAKIVIFSCPVDIIQTETKGTVLIKS 261
Cdd:cd03338 167 VLKVIDPATATNVDlkDIRIVKKLGGTIEDTELVDGLVFtQKASKkaGGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVND 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 262 ADELLSFSSGEESLLESQIKAIADA-----GVKVVVAGGKVGDMALHFLNKYGLMAVRLNSKFDLRRLSRSVNATVLPRI 336
Cdd:cd03338 247 YAQMDRILREERKYILNMCKKIKKSgcnvlLIQKSILRDAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVASI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 337 TTPSQEELGYCDKVCIEELGDTTIVAFRNEGKDSRIATVVIRGATDNFMDDIERALDDAINNFKCLTRDGRYLPGAGATE 416
Cdd:cd03338 327 DHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPGKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGAPE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 417 IELATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHNNeAGKTIGfdIEAEKASTIDTTKA 496
Cdd:cd03338 407 IEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQ-GEKNAG--INVRKGAITNILEE 483
|
490 500 510
....*....|....*....|....*....|..
gi 19921848 497 KLFDLYQSKFWGLKYAVGAAATILKVDQIIMA 528
Cdd:cd03338 484 NVVQPLLVSTSAITLATETVRMILKIDDIVLA 515
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
27-526 |
2.35e-80 |
|
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: 261.28 E-value: 2.35e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 27 EAVFRNISACKEFAQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHPAAKLIVMASQMQDAEVGDGTNFVVV 106
Cdd:TIGR02343 27 EAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 107 LAGALLESAEELLRLGITTAEISDGYEKALEKALEILPNLVSHKIEDYRNVEKVKEVLRTSIMSK-QYGQEDFLNDLVSK 185
Cdd:TIGR02343 107 LAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEISADNNNREPLIQAAKTSLGSKiVSKCHRRFAEIAVD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 186 ACVSILP-DEGTFNVDNIRICKILGSGLTKSEVVRGMVfkrfVEGDVTY------AEKAKIVIFSCPVDIIQTETKGTVL 258
Cdd:TIGR02343 187 AVLNVADmERRDVDFDLIKVEGKVGGSLEDTKLIKGII----IDKDFSHpqmpkeVEDAKIAILTCPFEPPKPKTKHKLD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 259 IKSADELLSFSSGEESLLESQIKAIADAGVKVVVAGGKVGDMALHFLNKYGLMAVRLNSKFDLRRLSRSVNATVLPRITT 338
Cdd:TIGR02343 263 ISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPRFQE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 339 PSQEELGYCDKVCIEELGDTT--IVAFRNEgKDSRIATVVIRGATDNFMDDIERALDDAINNFKCLTRDGRYLPGAGATE 416
Cdd:TIGR02343 343 LSKDKLGKAGLVREISFGTTKdrMLVIEQC-KNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGGGAAE 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 417 IELATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHNNEAGKTIGFDIEAEkaSTIDTTKA 496
Cdd:TIGR02343 422 ISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNLGVDCLGY--GTNDMKEQ 499
|
490 500 510
....*....|....*....|....*....|
gi 19921848 497 KLFDLYQSKFWGLKYAVGAAATILKVDQII 526
Cdd:TIGR02343 500 FVFETLIGKKQQILLATQLVRMILKIDDVI 529
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
14-526 |
1.69e-79 |
|
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: 257.22 E-value: 1.69e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 14 MLKDGARMYSGlEEAVFRNISACKEFAQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHPAAKLIVMASQMQ 93
Cdd:cd03337 4 VLNQNTKRESG-RKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 94 DAEVGDGTNFVVVLAGALLESAEELLRLGITTAEISDGYEKALEKALEILPNlVSHKIeDYRNVEKVKEVLRTSIMSKQY 173
Cdd:cd03337 83 DEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEE-ISIPV-DVNDRAQMLKIIKSCIGTKFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 174 GQE-DFLNDLVSKA--CVSILPDEGTFNVD---NIRICKILGSGLTKSEVVRGMVFKRfvegDVT------YAEKAKIVI 241
Cdd:cd03337 161 SRWsDLMCNLALDAvkTVAVEENGRKKEIDikrYAKVEKIPGGEIEDSRVLDGVMLNK----DVThpkmrrRIENPRIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 242 FSCPVD-IIQTEtkgtvliksadellsfssgeesllesqiKAIAdagvkvvvaggkvgDMALHFLNKYGLMAVRLNSKFD 320
Cdd:cd03337 237 LDCPLEyLVITE----------------------------KGVS--------------DLAQHYLVKAGITALRRVRKTD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 321 LRRLSRSVNATVLPRITTPSQEELGYCDKVCIEELGDTTIVAFRNEGKDSRIATVVIRGATDNFMDDIERALDDAINNFK 400
Cdd:cd03337 275 NNRIARACGATIVNRPEELTESDVGTGAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVAR 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 401 CLTRDGRYLPGAGATEIELATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHNNEAGKTIG 480
Cdd:cd03337 355 NIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTWG 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 19921848 481 fdIEAEKASTIDTTKAKLFDLYQSKFWGLKYAVGAAATILKVDQII 526
Cdd:cd03337 435 --IDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
26-529 |
1.56e-78 |
|
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: 255.86 E-value: 1.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 26 EEAVFRNISACKEFAQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHPAAKLIVMASQMQDAEVGDGTNFVV 105
Cdd:TIGR02342 8 QDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 106 VLAGALLESAEELLRLGITTAEISDGYEKALEKALEILpNLVSHKIeDYRNVEKVKEVLRTSIMSKQYGQ-EDFLNDLVS 184
Cdd:TIGR02342 88 ILAGALLGACERLLNKGIHPTIISESFQSAADEAIKIL-DEMSIPV-DLSDREQLLKSATTSLSSKVVSQySSLLAPLAV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 185 KACVSILPDEGTFNVD--NIRICKILGSGLTKSEVVRGMVFKRFVE---GDVTYAEKAKIVIFSCPVDIIQTETKGTVLI 259
Cdd:TIGR02342 166 DAVLKVIDPENAKNVDlnDIKVVKKLGGTIDDTELIEGLVFTQKASksaGGPTRIEKAKIGLIQFQISPPKTDMENQIIV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 260 KSADELLSFSSGEESLLESQIKAIADAG-----VKVVVAGGKVGDMALHFLNKYGLMAVRLNSKFDLRRLSRSVNATVLP 334
Cdd:TIGR02342 246 NDYAQMDRVLKEERAYILNIVKKIKKTGcnvllIQKSILRDAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 335 RITTPSQEELGYCDKVCIEELGDTTIVAFRNEGKDSRIATVVIRGATDNFMDDIERALDDAINNFKCLTRDGRYLPGAGA 414
Cdd:TIGR02342 326 SIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 415 TEIELATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHNNeAGKTIGfdIEAEKASTIDTT 494
Cdd:TIGR02342 406 PEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHAN-GEKTAG--ISVRKGGITNML 482
|
490 500 510
....*....|....*....|....*....|....*
gi 19921848 495 KAKLFDLYQSKFWGLKYAVGAAATILKVDQIIMAK 529
Cdd:TIGR02342 483 EEHVLQPLLVTTSAITLASETVRSILKIDDIVFTR 517
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
18-526 |
5.25e-74 |
|
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: 244.63 E-value: 5.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 18 GARMYSGlEEAVFRNISACKEFAQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHPAAKLIVMASQMQDAEV 97
Cdd:TIGR02340 4 GGERTSG-QDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 98 GDGTNFVVVLAGALLESAEELLRLGITTAEISDGYEKALEKALEILPNLVSHKIEDYRNvEKVKEVLRTSIMSKQYGQE- 176
Cdd:TIGR02340 83 GDGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKENLSVSVDELGR-EALINVAKTSMSSKIIGLDs 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 177 DFLNDLVSKACVSI----LPDEGTFNVDNIRICKILGSGLTKSEVVRGMVFK--RFVEGDVTYAEKAKIVIFSCPVDIIQ 250
Cdd:TIGR02340 162 DFFSNIVVDAVLAVkttnENGETKYPIKAINILKAHGKSARESMLVKGYALNctVASQQMPKRIKNAKIACLDFNLQKAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 251 TETKGTVLIKSADELLSFSSGEESLLESQIKAIADAGVKVVVAGGKVGDMALHFLNKYGLMAVRLNSKFDLRRLSRSVNA 330
Cdd:TIGR02340 242 MALGVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 331 TVLPRITTPSQEE------LGYCDKVCIEELGDTTIVAFRNeGKDSRIATVVIRGATDNFMDDIERALDDAINNFKCLTR 404
Cdd:TIGR02340 322 TLVSTLADLEGEEtfeasyLGFADEVVQERIADDECILIKG-TKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 405 DGRYLPGAGATEIELATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHNNEAG-------K 477
Cdd:TIGR02340 401 SNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAQLkpekkhlK 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 19921848 478 TIGFDIEAEKAStiDTTKAKLFDLYQSKFWGLKYAVGAAATILKVDQII 526
Cdd:TIGR02340 481 WYGLDLVNGKIR--DNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLI 527
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
22-526 |
1.39e-73 |
|
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: 243.35 E-value: 1.39e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 22 YSGlEEAVFRNISACKEFAQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHPAAKLIVMASQMQDAEVGDGT 101
Cdd:cd03335 4 TSG-QDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 102 NFVVVLAGALLESAEELLRLGITTAEISDGYEKALEKALEILPNLVSHKIEDYRNvEKVKEVLRTSIMSKQYGQE-DFLN 180
Cdd:cd03335 83 TSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEHLSISVDNLGK-ESLINVAKTSMSSKIIGADsDFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 181 DLVSKA--CVSILPDEG--TFNVDNIRICKILGSGLTKSEVVRGMVFK--RFVEGDVTYAEKAKIVIFScpVDIIQTETK 254
Cdd:cd03335 162 NMVVDAilAVKTTNEKGktKYPIKAVNILKAHGKSAKESYLVNGYALNctRASQGMPTRVKNAKIACLD--FNLQKTKMK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 255 -GT-VLIKSADELLSFSSGEESLLESQIKAIADAGVKVVVAGGKVGDMALHFLNKYGLMAVRLNSKFDLRRLSRSVNATV 332
Cdd:cd03335 240 lGVqVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 333 LPRITTPSQEE------LGYCDKVCIEELGDTTIVAFRNeGKDSRIATVVIRGATDNFMDDIERALDDAINNFKCLTRDG 406
Cdd:cd03335 320 VSTLANLEGEEtfdpsyLGEAEEVVQERIGDDELILIKG-TKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 407 RYLPGAGATEIELATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHN-------NEAGKTI 479
Cdd:cd03335 399 SVVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAaaqvkpdKKHLKWY 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 19921848 480 GFDIEAEKAStiDTTKAKLFDLYQSKFWGLKYAVGAAATILKVDQII 526
Cdd:cd03335 479 GLDLINGKVR--DNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLI 523
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
32-526 |
4.55e-73 |
|
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: 241.95 E-value: 4.55e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 32 NISACKEFAQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHPAAKLIVMASQMQDAEVGDGTNFVVVLAGAL 111
Cdd:TIGR02344 21 NIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILAGEM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 112 LESAEELLRLGITTAEISDGYEKALEKALEILPNLVshKIEDYRNVEKVKEVLRTSIMSKQYGQ-EDFLNDLVSKACVSI 190
Cdd:TIGR02344 101 LSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEIS--IPVDVNDDAAMLKLIQSCIGTKFVSRwSDLMCDLALDAVRTV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 191 LPDE-GTFNVD---NIRICKILGSGLTKSEVVRGMVFKRfvegDVT------YAEKAKIVIFSCPVDIIQTETKGTVLIK 260
Cdd:TIGR02344 179 QRDEnGRKEIDikrYAKVEKIPGGDIEDSCVLKGVMINK----DVThpkmrrYIENPRIVLLDCPLEYKKGESQTNIEIT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 261 SADELLSFSSGEESLLESQIKAIADAGVKVVVAGGKVGDMALHFLNKYGLMAVRLNSKFDLRRLSRSVNATVLPRITTPS 340
Cdd:TIGR02344 255 KEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACGATIVNRPEELR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 341 QEELGY-CDKVCIEELGDTTIvAFRNEGKDSRIATVVIRGATDNFMDDIERALDDAINNFKCLTRDGRYLPGAGATEIEL 419
Cdd:TIGR02344 335 ESDVGTgCGLFEVKKIGDEYF-TFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKLVPGGGATEMAV 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 420 ATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHNNEAGKTIGfdIEAEKASTIDTTKAKLF 499
Cdd:TIGR02344 414 SVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTWG--IDGETGKIVDMKEKGIW 491
|
490 500
....*....|....*....|....*..
gi 19921848 500 DLYQSKFWGLKYAVGAAATILKVDQII 526
Cdd:TIGR02344 492 EPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
14-531 |
1.75e-70 |
|
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: 234.87 E-value: 1.75e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 14 MLKDGARMYSGLEEAVfRNISACKEFAQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHPAAKLIVMASQMQ 93
Cdd:cd03340 4 LLKEGTDTSQGKGQLI-SNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 94 DAEVGDGTNFVVVLAGALLESAEELLRLGITTAEISDGYEKALEKALEILpNLVSHKIEDYRNVEKvKEVL----RTSIM 169
Cdd:cd03340 83 DAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKI-KEIAVNIDKEDKEEQ-RELLekcaATALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 170 SKQYGQE-DFLNDLVSKAcVSILPDEgtFNVDNIRICKILGSGLTKSEVVRGMVFKR-FvegdvTYA---------EKAK 238
Cdd:cd03340 161 SKLIASEkEFFAKMVVDA-VLSLDDD--LDLDMIGIKKVPGGSLEDSQLVNGVAFKKtF-----SYAgfeqqpkkfKNPK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 239 IVIFSCPVDIIQTETKGTVLIKSADELLSFSSGEESLLESQIKAIADAGVKVVVAGGKVGDMALHFLNKYGLM-AVRLnS 317
Cdd:cd03340 233 ILLLNVELELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFcAGRV-P 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 318 KFDLRRLSRSVNATVLPRITTPSQEELGYCDKVCIEELGDTTIVAFRNEGKdSRIATVVIRGATDNFMDDIERALDDAIN 397
Cdd:cd03340 312 EEDLKRVAQATGGSIQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPK-AKTCTIILRGGAEQFIEEAERSLHDAIM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 398 NFKCLTRDGRYLPGAGATEIELATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHNNEAGK 477
Cdd:cd03340 391 IVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGK 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 19921848 478 TIGFDIEAEKasTIDTTKAKLFDLYQSKFWGLKYAVGAAATILKVDQIIMAKRA 531
Cdd:cd03340 471 WYGVDINNEG--IADNFEAFVWEPSLVKINALTAATEAACLILSVDETIKNPKS 522
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
26-535 |
2.05e-69 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 231.51 E-value: 2.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 26 EEAVFRNISACKEFAQTMRSAYGPNGMNKMIinhiEKQF----VTSDAGTIMRELDVEHP----AAKLIVMASQMQDAEV 97
Cdd:COG0459 9 EDARRANIRGVKALADAVKVTLGPKGRNVML----VKSFgdptITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 98 GDGTNFVVVLAGALLESAEELLRLGITTAEISDGYEKALEKALEILPNLvSHKIEDyrnVEKVKEVLRTSIMSKqygqeD 177
Cdd:COG0459 85 GDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKI-AKPVDD---KEELAQVATISANGD-----E 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 178 FLNDLVSKAcVSILPDEGTFNVDnirickiLGSGL-TKSEVVRGMVF-KRFV-EGDVTYAEK-------AKIVIFSCPVD 247
Cdd:COG0459 156 EIGELIAEA-MEKVGKDGVITVE-------EGKGLeTELEVVEGMQFdKGYLsPYFVTDPEKmpaelenAYILLTDKKIS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 248 IIQtetkgtvliksadELLSfssgeesLLESQIKA------IADAGVkvvvaggkvgDMALHFLNKYGLMAVR------- 314
Cdd:COG0459 228 SIQ-------------DLLP-------LLEKVAQSgkplliIAEDID----------GEALATLVVNGIRGVLrvvavka 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 315 ----LNSKFDLRRLSRSVNATVL-----PRITTPSQEELGYCDKVCIEElGDTTIVafrNEGKDSRIATVVIRGATDNFM 385
Cdd:COG0459 278 pgfgDRRKAMLEDIAILTGGRVIsedlgLKLEDVTLDDLGRAKRVEVDK-DNTTIV---EGAGNPKAIVILVGAATEVEV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 386 DDIERALDDAINNFKCLTRDGrYLPGAGATEIELATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVN 465
Cdd:COG0459 354 KERKRRVEDALHATRAAVEEG-IVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVE 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19921848 466 QLYlahnNEAGKTIGFDIEAEK------ASTIDTTKAKlfdlYQSkfwgLKYAVGAAATILKVDQIIMAKRAGGPK 535
Cdd:COG0459 433 KVR----AAKDKGFGFDAATGEyvdmleAGVIDPAKVK----RSA----LQNAASVAGLILTTEAVIADKPEKEEA 496
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
14-531 |
1.12e-68 |
|
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: 230.03 E-value: 1.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 14 MLKDGARMYSGLEEAVfRNISACKEFAQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHPAAKLIVMASQMQ 93
Cdd:TIGR02345 6 LLKEGTDTSQGKGQLI-SNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 94 DAEVGDGTNFVVVLAGALLESAEELLRLGITTAEISDGYEKALEKALEILPNL-VSHKIEDYRNVEKVKEVLRTSIMSKQ 172
Cdd:TIGR02345 85 DAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIaVTIDEEKGEQRELLEKCAATALSSKL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 173 YGQE-DFLNDLVSKACVSIlpDEGTFNVDNIRICKILGSGLTKSEVVRGMVFKRfvegDVTYA---------EKAKIVIF 242
Cdd:TIGR02345 165 ISHNkEFFSKMIVDAVLSL--DRDDLDLKLIGIKKVQGGALEDSQLVNGVAFKK----TFSYAgfeqqpkkfANPKILLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 243 SCPVDIIQTETKGTVLIKSADELLSFSSGEESLLESQIKAIADAGVKVVVAGGKVGDMALHFLNKYGLMAVRLNSKFDLR 322
Cdd:TIGR02345 239 NVELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 323 RLSRSVNATVLPRITTPSQEELGYCDKVCIEELGDTTIVAFRNeGKDSRIATVVIRGATDNFMDDIERALDDAINNFKCL 402
Cdd:TIGR02345 319 RVIKACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYFTG-CPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 403 TRDGRYLPGAGATEIELATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHNNEaGKTIGFD 482
Cdd:TIGR02345 398 LKNKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKG-GKWYGVD 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 19921848 483 IEAEKasTIDTTKAKLFDLYQSKFWGLKYAVGAAATILKVDQIIMAKRA 531
Cdd:TIGR02345 477 INTED--IGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITNPKS 523
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
11-533 |
4.15e-62 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 212.97 E-value: 4.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 11 VSQMLKDGARMYSGlEEAVFRNISACKEFAQTMRSAYGPNGMNKMIINHIEKQ-----FVTSDAGTIMRELDVEHPAAKL 85
Cdd:PTZ00212 7 PPQVLKQGAQEEKG-ETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMSEGPrsgnvTVTNDGATILKSVWLDNPAAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 86 IVMASQMQDAEVGDGTNFVVVLAGALLESAEELLRLGITTAEISDGYEKALEKALEILPNL-VSHKIEDYRNVEKVKEVL 164
Cdd:PTZ00212 86 LVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIaFDHGSDEEKFKEDLLNIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 165 RTSIMSKQYGQEdflNDLVSKACV-SILPDEGTFNVDNIRICKILGSGLTKSEVVRGMVF-KRFVEGDVTYAEKAKIVIF 242
Cdd:PTZ00212 166 RTTLSSKLLTVE---KDHFAKLAVdAVLRLKGSGNLDYIQIIKKPGGTLRDSYLEDGFILeKKIGVGQPKRLENCKILVA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 243 SCPVDIIQTETKGT-VLIKSADELLSFSSGEESLLESQIKAIADAGVKVVVAGGKVGDMALHFLNKYGLMAVRlNSKFD- 320
Cdd:PTZ00212 243 NTPMDTDKIKIYGAkVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIE-HADFDg 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 321 LRRLSRSVNATVLPRITTPSQEELGYCDKvcIEE--LGDTTIVAF----RNEGkdsriATVVIRGATDNFMDDIERALDD 394
Cdd:PTZ00212 322 MERLAAALGAEIVSTFDTPEKVKLGHCDL--IEEimIGEDKLIRFsgcaKGEA-----CTIVLRGASTHILDEAERSLHD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 395 AINNFKCLTRDGRYLPGAGATEIELATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHnNE 474
Cdd:PTZ00212 395 ALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEH-YK 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921848 475 AGKTIGFDIeaEKASTIDTTKAKLFDLYQSKFWGLKYAVGAAATILKVDQIIMA---KRAGG 533
Cdd:PTZ00212 474 GNKTAGIDM--EKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRCaprQREQV 533
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
44-529 |
5.23e-61 |
|
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: 209.49 E-value: 5.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 44 RSAYGPNGMNKMII-----NHIEkqfVTSDAGTIMRELDVEHPAAKLIVMASQMQDAEVGDGTNFVVVLAGALLESAEEL 118
Cdd:cd03336 30 KTTLGPKGMDKILQsvgrsGGVT---VTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDGTTSVTVLAAELLREAEKL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 119 LRLGITTAEISDGYEKALEKALEIlpnLVSHKIEDYRNVEKVKEVL----RTSIMSKQYGQE-DFLNDLVSKAcvsILPD 193
Cdd:cd03336 107 VAQKIHPQTIIEGYRMATAAAREA---LLSSAVDHSSDEEAFREDLlniaRTTLSSKILTQDkEHFAELAVDA---VLRL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 194 EGTFNVDNIRICKILGSGLTKSEVVRGMVF-KRFVEGDVTYAEKAKIVIFSCPVDIIQTETKGT-VLIKSADELLSFSSG 271
Cdd:cd03336 181 KGSGNLDAIQIIKKLGGSLKDSYLDEGFLLdKKIGVNQPKRIENAKILIANTPMDTDKIKIFGAkVRVDSTAKVAEIEEA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 272 EESLLESQIKAIADAGVKVVVAGGKVGDMALHFLNKYGLMAVRlNSKFD-LRRLSRSVNATVLPRITTPSQEELGYCDKv 350
Cdd:cd03336 261 EKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIE-HADFDgVERLALVTGGEIASTFDHPELVKLGTCKL- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 351 cIEE--LGDTTIVAFrnEGKDSRIA-TVVIRGATDNFMDDIERALDDAINNFKCLTRDGRYLPGAGATEIELATQLSAYA 427
Cdd:cd03336 339 -IEEimIGEDKLIRF--SGVAAGEAcTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRVVLGGGCSEMLMAKAVEELA 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 428 DTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHNNEaGKTIGFDIeaEKASTIDTTKAKLFDLYQSKFW 507
Cdd:cd03336 416 KKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNG-NTTAGLDM--RKGTVGDMKELGITESFKVKRQ 492
|
490 500
....*....|....*....|..
gi 19921848 508 GLKYAVGAAATILKVDQIIMAK 529
Cdd:cd03336 493 VLLSASEAAEMILRVDDIIKCA 514
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
158-405 |
1.17e-54 |
|
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: 183.44 E-value: 1.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 158 EKVKEVLRTSIMSKQYGQEDFLNDLVSKACVSILPDEGTFNVDNIRICKILGSGLTKSEVVRGMVFKRFVEGDV--TYAE 235
Cdd:cd03333 2 ELLLQVATTSLNSKLSSWDDFLGKLVVDAVLKVGPDNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYmpKRLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 236 KAKIVIFSCPVDIIqtetkgtVLIKsadellsfssgeesllesqiKAIADagvkvvvaggkvgdMALHFLNKYGLMAVRL 315
Cdd:cd03333 82 NAKILLLDCPLEYV-------VIAE--------------------KGIDD--------------LALHYLAKAGIMAVRR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 316 NSKFDLRRLSRSVNATVLPRITTPSQEELGYCDKVCIEELGDTTIVAFRnEGKDSRIATVVIRGATDNFMDDIERALDDA 395
Cdd:cd03333 121 VKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIE-GCKGGKAATILLRGATEVELDEVKRSLHDA 199
|
250
....*....|
gi 19921848 396 INNFKCLTRD 405
Cdd:cd03333 200 LCAVRAAVEE 209
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
13-528 |
1.40e-51 |
|
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: 184.29 E-value: 1.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 13 QMLKDGARMYSGlEEAVFRNISACKEFAQTMRSAYGPNGMNKMII--NHIEKQFVTSDAGTIMRELDVEHPAAKLIVMAS 90
Cdd:TIGR02341 1 QIFKDGADEERA-ENARLSSFVGAIAIGDLVKSTLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 91 QMQDAEVGDGTNFVVVLAGALLESAEELLRLGITTAEISDGYEKALEKALEILPN-LVSHKIEDYRNVEKVKEVLRTSIM 169
Cdd:TIGR02341 80 KVQDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKsAVDNGSDEVKFRQDLMNIARTTLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 170 SKQYGQEDflNDLVSKACVSILPDEGTFNVDNIRICKILGSGLTKSEVVRGMVF-KRFVEGDVTYAEKAKIVIFSCPVDI 248
Cdd:TIGR02341 160 SKILSQHK--DHFAQLAVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFLLdKKIGVNQPKRIENAKILIANTGMDT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 249 IQTETKGT-VLIKSADELLSFSSGEESLLESQIKAIADAGVKVVVAGGKVGDMALHFLNKYGLMAVRLNSKFDLRRLSRS 327
Cdd:TIGR02341 238 DKVKIFGSrVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 328 VNATVLPRITTPSQEELGYCDKvcIEE--LGDTTIVAFRNEgKDSRIATVVIRGATDNFMDDIERALDDAINNFKCLTRD 405
Cdd:TIGR02341 318 TGGEIVSTFDHPELVKLGSCDL--IEEimIGEDKLLKFSGV-KLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 406 GRYLPGAGATEIELATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHNNeAGKTIGFDIea 485
Cdd:TIGR02341 395 SRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYN-GNTTMGLDM-- 471
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 19921848 486 EKASTIDTTKAKLFDLYQSKFWGLKYAVGAAATILKVDQIIMA 528
Cdd:TIGR02341 472 NEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKA 514
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
32-531 |
9.27e-49 |
|
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: 176.85 E-value: 9.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 32 NISACKEFAQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHPAAKLIVMASQMQDAEVGDGTNFVVVLAGAL 111
Cdd:TIGR02347 21 NINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 112 LESAEELLRLGITTAEISDGYEKALEKALEILPNLVShKIEDYRNVEKVKEVLRTSIMSKQY-GQEDFLNDLVSKACVSI 190
Cdd:TIGR02347 101 LKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKV-KKEDEVDREFLLNVARTSLRTKLPaDLADQLTEIVVDAVLAI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 191 LPDEGTFNVDNIRICKILGSGLTKSEVVRGMVFKR-FVEGDV-TYAEKAKIVIFSCPVDIIQTETKGTVLIKSADELLSF 268
Cdd:TIGR02347 180 KKDGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHgARHPDMpRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQREKL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 269 SSGEESLLESQIKAIADAGVKVVVAGGKVG----------DMALHFLNKYGLMAVRLNSKFDLRRLSRSVNATVLPRITT 338
Cdd:TIGR02347 260 VKAERKFVDDRVKKIIELKKKVCGKSPDKGfvvinqkgidPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEALNSVED 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 339 PSQEELGYCDKVCIEELGDTTIVaFRNEGKDSRIATVVIRGATDNFMDDIERALDDAINNFKCLTRDGRYLPGAGATEIE 418
Cdd:TIGR02347 340 LTPECLGWAGLVYETTIGEEKYT-FIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAGAFEIA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 419 LATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHnNEAGKTIGFDIEAEKAstIDTTKAKL 498
Cdd:TIGR02347 419 AYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEH-DEGGEVVGVDLNTGEP--IDPEIKGI 495
|
490 500 510
....*....|....*....|....*....|...
gi 19921848 499 FDLYQSKFWGLKYAVGAAATILKVDQIIMAKRA 531
Cdd:TIGR02347 496 WDNYRVKKQLIQSATVIASQLLLVDEVMRAGRS 528
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
32-530 |
1.19e-48 |
|
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: 175.52 E-value: 1.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 32 NISACKEFAQTMRSAYGPNGMNKMIIN---HIEkqfVTSDAGTIMRELDVEHPAAKLIVMASQMQDAEVGDGTNFVVVLA 108
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSgagDIK---LTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 109 GALLESAEELLRLGITTAEISDGYEKALEKALEILPNLVShKIEDYRNVEKVKEVLRTSIMSKQYGQ-EDFLNDLVSKAC 187
Cdd:cd03342 94 GELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKV-PVEIDTDRELLLSVARTSLRTKLHADlADQLTEIVVDAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 188 VSILPDEGTFNVDNIRICKILGSGLTKSEVVRGMVF---------KRFVEgdvtyaeKAKIVIFSCPVDIIQTETkgtvl 258
Cdd:cd03342 173 LAIYKPDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLdhgarhpdmPKRVE-------NAYILTCNVSLEYEKTEV----- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 259 iksadellsFSSGEESLLESQiKAIadagvkvvvaggkvgD-MALHFLNKYGLMAVRLNSKFDLRRLSRSVNATVLPRIT 337
Cdd:cd03342 241 ---------NSGFFYSVVINQ-KGI---------------DpPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVD 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 338 TPSQEELGYCDKVCIEELGDTTIvAFRNEGKDSRIATVVIRGATDNFMDDIERALDDAINNFKCLTRDGRYLPGAGATEI 417
Cdd:cd03342 296 DLSPECLGYAGLVYERTLGEEKY-TFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 418 ELATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLyLAHNNEAGKTIGFDIEAEKasTIDTTKAK 497
Cdd:cd03342 375 ALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKL-QDEYAEGGQVGGVDLDTGE--PMDPESEG 451
|
490 500 510
....*....|....*....|....*....|...
gi 19921848 498 LFDLYQSKFWGLKYAVGAAATILKVDQIIMAKR 530
Cdd:cd03342 452 IWDNYSVKRQILHSATVIASQLLLVDEIIRAGR 484
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
48-520 |
4.80e-10 |
|
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: 62.09 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 48 GPNGMNKMIinhiEKQF----VTSDAGTIMRELDVEHP----AAKLI-VMASQMQDaEVGDGTNFVVVLAGALLESAEEL 118
Cdd:cd03344 29 GPKGRNVVI----EKSFgspkITKDGVTVAKEIELEDPfenmGAQLVkEVASKTND-VAGDGTTTATVLARAIIKEGLKA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 119 LRLGITTAEISDGYEKALEKALEILPNLvSHKIEDYRNVEKVkevlrTSIMSkqyGQEDFLNDLVSKAcVSILPDEGTFN 198
Cdd:cd03344 104 VAAGANPMDLKRGIEKAVEAVVEELKKL-SKPVKTKEEIAQV-----ATISA---NGDEEIGELIAEA-MEKVGKDGVIT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 199 VDnirickiLGSGL-TKSEVVRGMVFKR------FvegdVTYAEKaKIVIFSCPvDIIQTETKgtvlIKSADELLsfssg 271
Cdd:cd03344 174 VE-------EGKTLeTELEVVEGMQFDRgylspyF----VTDPEK-MEVELENP-YILLTDKK----ISSIQELL----- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 272 eeSLLESQIKA------IADAGVKVvvaggkvgdmALHFL--NK-YGLM---AVRLNSKFDLRR-----LSRSVNATVLp 334
Cdd:cd03344 232 --PILELVAKAgrplliIAEDVEGE----------ALATLvvNKlRGGLkvcAVKAPGFGDRRKamledIAILTGGTVI- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 335 rittpsQEELGYC-DKVCIEELG----------DTTIVAFRNEGKD--SRIA---------------------------- 373
Cdd:cd03344 299 ------SEELGLKlEDVTLEDLGrakkvvvtkdDTTIIGGAGDKAAikARIAqirkqieettsdydkeklqerlaklsgg 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 374 TVVIR--GATDNFMDDIERALDDAINNFKCLTRDGrYLPGAGATEIELATQLsayaDTLPGLD---QYAVRKFANALEVF 448
Cdd:cd03344 373 VAVIKvgGATEVELKEKKDRVEDALNATRAAVEEG-IVPGGGVALLRASPAL----DKLKALNgdeKLGIEIVRRALEAP 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19921848 449 PKALAENSGINGTEIVNQLyLAHNNEagktIGFDIEAE------KASTIDTTKAKLfdlyqskfWGLKYAVGAAATIL 520
Cdd:cd03344 448 LRQIAENAGVDGSVVVEKV-LESPDG----FGYDAATGeyvdmiEAGIIDPTKVVR--------SALQNAASVASLLL 512
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
40-482 |
4.86e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 52.50 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 40 AQTMRSAYGPNGMNKMIinhiEKQF----VTSDAGTIMRELDVEHP----AAKLI-VMASQMQDaEVGDGTNFVVVLAGA 110
Cdd:PRK12849 23 ADAVKVTLGPKGRNVVI----DKSFgaptITKDGVSIAKEIELEDPfenlGAQLVkEVASKTND-VAGDGTTTATVLAQA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 111 LLESAEELLRLGITTAEISDGYEKALEKALEILPNLvSHKIEDYRNVEKVkevlrTSIMSkqyGQEDFLNDLVSKAcVSI 190
Cdd:PRK12849 98 LVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKAL-ARPVSGSEEIAQV-----ATISA---NGDEEIGELIAEA-MEK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 191 LPDEGTFNVDNirickilGSGL-TKSEVVRGMVFKR------FvegdVTYAEKaKIVIFSCPVdIIQTETKgtvlIKSAD 263
Cdd:PRK12849 168 VGKDGVITVEE-------SKTLeTELEVTEGMQFDRgylspyF----VTDPER-MEAVLEDPL-ILLTDKK----ISSLQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 264 ELLsfssgeeSLLESQIKA------IADAGVKVvvaggkvgdmALHFL----NKYGLMAVRLNSKF--DLRR-----LSR 326
Cdd:PRK12849 231 DLL-------PLLEKVAQSgkplliIAEDVEGE----------ALATLvvnkLRGGLKVAAVKAPGfgDRRKamledIAI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 327 SVNATVLprittpsQEELGYC-DKVCIEELG----------DTTIVAFRN----------------EGKDS--------- 370
Cdd:PRK12849 294 LTGGTVI-------SEDLGLKlEEVTLDDLGrakrvtitkdNTTIVDGAGdkeaiearvaqirrqiEETTSdydreklqe 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 371 RIA-----TVVIR--GATDNFMDDIERALDDAINNFKCLTRDGrYLPGAGATEIELATQLSAYADtLPGLDQYAVRKFAN 443
Cdd:PRK12849 367 RLAklaggVAVIKvgAATEVELKERKDRVEDALNATRAAVEEG-IVPGGGVALLRAAKALDELAG-LNGDQAAGVEIVRR 444
|
490 500 510
....*....|....*....|....*....|....*....
gi 19921848 444 ALEVFPKALAENSGINGTEIVNQLylahnNEAGKTIGFD 482
Cdd:PRK12849 445 ALEAPLRQIAENAGLDGSVVVAKV-----LELEDGFGFN 478
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
48-529 |
9.61e-07 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 51.64 E-value: 9.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 48 GPNGMNKMIinhiEKQF----VTSDAGTIMRELD----VEHPAAKLIVMASQMQDAEVGDGTNFVVVLAGALLESAEELL 119
Cdd:CHL00093 31 GPKGRNVVL----EKKYgspqIVNDGVTIAKEIEledhIENTGVALIRQAASKTNDVAGDGTTTATVLAYAIVKQGMKNV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 120 RLGITTAEISDGYEKALEKALEILPNLvSHKIEDYRNVEKVkevlrTSIMSkqyGQEDFLNDLVSKAcVSILPDEGTFNV 199
Cdd:CHL00093 107 AAGANPISLKRGIEKATQYVVSQIAEY-ARPVEDIQAITQV-----ASISA---GNDEEVGSMIADA-IEKVGREGVISL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 200 DNIRickilgSGLTKSEVVRGMVF-KRFVEGD-VTYAEKAKiVIFSCPVdIIQTETKGTvLIKSadELLSfssgeesLLE 277
Cdd:CHL00093 177 EEGK------STVTELEITEGMRFeKGFISPYfVTDTERME-VVQENPY-ILLTDKKIT-LVQQ--DLLP-------ILE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 278 SQIKA------IADAGVKVVvaggkvgdMALHFLNKY----GLMAVRLNSKFDLRR-----LSRSVNATVlprITtpsqE 342
Cdd:CHL00093 239 QVTKTkrplliIAEDVEKEA--------LATLVLNKLrgivNVVAVRAPGFGDRRKamledIAILTGGQV---IT----E 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 343 ELGYC-DKVCIEELGD----------TTIVAFRNEGK---------------DS---------RIATV-----VIR--GA 380
Cdd:CHL00093 304 DAGLSlETIQLDLLGQarriivtkdsTTIIADGNEEQvkarceqlrkqieiaDSsyekeklqeRLAKLsggvaVIKvgAA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 381 TDNFMDDIERALDDAINNFKCLTRDGrYLPGAGATEIELATQLSAYA-DTLPGLDQYAVRKFANALEVFPKALAENSGIN 459
Cdd:CHL00093 384 TETEMKDKKLRLEDAINATKAAVEEG-IVPGGGATLVHLSENLKTWAkNNLKEDELIGALIVARAILAPLKRIAENAGKN 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 460 GTEIVNQLylahnNEAGKTIGFDieAEKASTIDTTKAKLFDLYQSKFWGLKYAVGAAATILKVDQIIMAK 529
Cdd:CHL00093 463 GSVIIEKV-----QEQDFEIGYN--AANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDK 525
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
160-383 |
3.09e-06 |
|
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: 48.76 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 160 VKEVLR-TSIMSKQYgQEDFLNDLVSKACVSILPDEGTFNVDNIR----ICKILGSGLTKSEVVRGMVFKRFV--EGDVT 232
Cdd:cd03334 4 LAQLLKdEGISNDES-WLDILLPLVWKAASNVKPDVRAGDDMDIRqyvkIKKIPGGSPSDSEVVDGVVFTKNVahKRMPS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 233 YAEKAKIVIFSCPVDIIQTETKgtvlIKSADELLsfsSGEESLLESQIKAIADAGVKVVVAGGKVGDMALHFLNKYGLmA 312
Cdd:cd03334 83 KIKNPRILLLQGPLEYQRVENK----LLSLDPVI---LQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGI-T 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 313 VRLNSKFD-LRRLSRSVNATVLPRI----TTPSqeeLGYCD----KVCIEELGDT-TIVAFrnEGKDSRI-ATVVIRGAT 381
Cdd:cd03334 155 LVLNVKPSvLERISRCTGADIISSMddllTSPK---LGTCEsfrvRTYVEEHGRSkTLMFF--EGCPKELgCTILLRGGD 229
|
..
gi 19921848 382 DN 383
Cdd:cd03334 230 LE 231
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
40-545 |
1.16e-05 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 48.20 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 40 AQTMRSAYGPNGMNKMIinhiEKQF----VTSDAGTIMRELDVEHP-----AAKLIVMASQMQDAeVGDGTNFVVVLAGA 110
Cdd:PRK12851 24 ADAVKVTLGPKGRNVVI----DKSFgaptITNDGVTIAKEIELEDKfenmgAQMVREVASKTNDV-AGDGTTTATVLAQA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 111 LLESAEELLRLGITTAEISDGYEKALEKALEILPNLVshkiedyRNVEKVKEVLRTSIMSKQYGQEdfLNDLVSKAcVSI 190
Cdd:PRK12851 99 IVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANA-------RPVTTNAEIAQVATISANGDAE--IGRLVAEA-MEK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 191 LPDEGTFNVDNiriCKILGsglTKSEVVRGMVFKR------FvegdVTYAEKAKiVIFSCPVdIIQTETKgtvlIKSADE 264
Cdd:PRK12851 169 VGNEGVITVEE---SKTAE---TELEVVEGMQFDRgylspyF----VTDADKME-AELEDPY-ILIHEKK----ISNLQD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 265 LLsfssgeeSLLESQIKA------IADAGVKVVvaggkvgdMALHFLNKY--GLMAVRLNSK-FDLRRLSRSVNATVLPR 335
Cdd:PRK12851 233 LL-------PVLEAVVQSgkplliIAEDVEGEA--------LATLVVNKLrgGLKVAAVKAPgFGDRRKAMLEDIAILTG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 336 ITTPSQ-----------EELGYCDKVCIEElGDTTIV--------------AFRNEGKDS-----------RIATV---- 375
Cdd:PRK12851 298 GTVISEdlgiklenvtlEQLGRAKKVVVEK-ENTTIIdgagskteiegrvaQIRAQIEETtsdydreklqeRLAKLaggv 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 376 -VIR--GATDNFMDDIERALDDAINNFKCLTRDGrYLPGAGATEIELATQLSAyADTLPGLDQYAVRKFANALEVFPKAL 452
Cdd:PRK12851 377 aVIRvgASTEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRAVKALDK-LETANGDQRTGVEIVRRALEAPVRQI 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 453 AENSGINGTEIVNQLYlahnnEAGKTIGFDieAEKASTIDTTKAKLFDLYQSKFWGLKYAVGAAATILKVDQIIMAKRAG 532
Cdd:PRK12851 455 AENAGAEGSVVVGKLR-----EKPGGYGFN--AATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKK 527
|
570
....*....|...
gi 19921848 533 GPKVRQAAGSDDE 545
Cdd:PRK12851 528 EPAPPAPPGGGMD 540
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
48-544 |
1.40e-05 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 47.79 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 48 GPNGMNKMIinhiEKQF----VTSDAGTIMRELDVEHPAAKlivMASQM-------QDAEVGDGTNFVVVLAGALLESAE 116
Cdd:PRK12850 32 GPKGRNVVL----EKSFgaprITKDGVTVAKEIELEDKFEN---MGAQMvkevaskTNDLAGDGTTTATVLAQAIVREGA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 117 ELLRLGITTAEISDGYEKALEKALEILPNLVshkiedyRNVEKVKEVLRTSIMSKqyGQEDFLNDLVSKAcVSILPDEGT 196
Cdd:PRK12850 105 KLVAAGMNPMDLKRGIDLAVAAVVDELKKIA-------KKVTSSKEIAQVATISA--NGDESIGEMIAEA-MDKVGKEGV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 197 FNVDNiriCKILGSGLtksEVVRGMVFKR-FVEGD-VTYAEKAKIViFSCPVdIIQTETKgtvlIKSADELLsfssgeeS 274
Cdd:PRK12850 175 ITVEE---AKTLGTEL---DVVEGMQFDRgYLSPYfVTNPEKMRAE-LEDPY-ILLHEKK----ISNLQDLL-------P 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 275 LLESQIKA------IADAGVKVVvaggkvgdMALHFLNKY--GLMAVRLNSK-FDLRRLSRSVNATVLP----------- 334
Cdd:PRK12850 236 ILEAVVQSgrplliIAEDVEGEA--------LATLVVNKLrgGLKSVAVKAPgFGDRRKAMLEDIAVLTggqvisedlgi 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 335 RITTPSQEELGYCDKVCIEElGDTTIVAFRNEGK--DSRIATV----------------------------VIR--GATD 382
Cdd:PRK12850 308 KLENVTLDMLGRAKRVLITK-ENTTIIDGAGDKKniEARVKQIraqieettsdydreklqerlaklaggvaVIRvgGATE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 383 NFMDDIERALDDAINNFKCLTRDGrYLPGAGA----TEIELATQLSAYADTLPGLDqyAVRKfanALEVFPKALAENSGI 458
Cdd:PRK12850 387 VEVKEKKDRVDDALHATRAAVEEG-IVPGGGVallrARSALRGLKGANADETAGID--IVRR---ALEEPLRQIATNAGF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 459 NGTEIVNQLylahnneAGKTIGFDIEAEKASTIDTTKAKLFDLYQSKFWGLKYAVGAAATILKVDQIIMAKRAGGPKVRQ 538
Cdd:PRK12850 461 EGSVVVGKV-------AELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAAAAAA 533
|
....*.
gi 19921848 539 AAGSDD 544
Cdd:PRK12850 534 GPGPGM 539
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
39-225 |
1.91e-04 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 44.25 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 39 FAQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDV----EHPAAKLI-VMASQMQDAeVGDGTNFVVVLAGALLE 113
Cdd:PRK14104 23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVrEVASKSADA-AGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 114 SAEELLRLGITTAEISDGYEKALEKaleilpnLVSHKIEDYRNVEKVKEVLRTSIMSKQYGQE--DFLNDLVSKacvsiL 191
Cdd:PRK14104 102 EGAKSVAAGMNPMDLKRGIDLAVEA-------VVADLVKNSKKVTSNDEIAQVGTISANGDAEigKFLADAMKK-----V 169
|
170 180 190
....*....|....*....|....*....|....
gi 19921848 192 PDEGTFNVDNIRickilgSGLTKSEVVRGMVFKR 225
Cdd:PRK14104 170 GNEGVITVEEAK------SLETELDVVEGMQFDR 197
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
48-153 |
5.55e-04 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 42.60 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921848 48 GPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHP----AAKLIVMASQMQDAEVGDGTNFVVVLAGALLESAEELLRLGI 123
Cdd:PLN03167 87 GPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGA 166
|
90 100 110
....*....|....*....|....*....|
gi 19921848 124 TTAEISDGYEKALeKALEILPNLVSHKIED 153
Cdd:PLN03167 167 NPVQITRGIEKTA-KALVKELKKMSKEVED 195
|
|
| |
