|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
13-538 |
0e+00 |
|
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: 983.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 13 GKRTTGQGIRSQNVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQLQDEEVGD 92
Cdd:cd03335 1 GERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 93 GTTSVVIVAAELLKRADELVKQKVHPTTIINGYRLACKEAVKYISENISFTSDSIGRQSVVNAAKTSMSSKIIGPDADFF 172
Cdd:cd03335 81 GTTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEHLSISVDNLGKESLINVAKTSMSSKIIGADSDFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 173 GELVVDAAEAVRVEN-NGKVTYPINAVNVLKAHGKSARESVLVKGYALNCTVASQAMPLRVQNAKIACLDFSLMKAKMHL 251
Cdd:cd03335 161 ANMVVDAILAVKTTNeKGKTKYPIKAVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 252 GISVVVEDPAKLEAIRREEFDITKRRIDKILKAGANVVLTTGGIDDLCLKQFVESGAMAVRRCKKSDLKRIAKATGATLT 331
Cdd:cd03335 241 GVQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 332 VSLATLEGDEAFDASLLGHADEIVQERISDDELILIKGPKSRTASSIILRGANDVMLDEMERSVHDSLCVVRRVLESKKL 411
Cdd:cd03335 321 STLANLEGEETFDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 412 VAGGGAVETSLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKAQLIPQLQHLKWAGL 491
Cdd:cd03335 401 VPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKPDKKHLKWYGL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 3879449 492 DLEEGTIRDNKEAGILEPALSKVKSLKFATEAAITILRIDDLIKLDK 538
Cdd:cd03335 481 DLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIKLNP 527
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
9-543 |
0e+00 |
|
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: 965.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 9 LALTGKRTTGQGIRSQNVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQLQDE 88
Cdd:TIGR02340 1 LFLGGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 89 EVGDGTTSVVIVAAELLKRADELVKQKVHPTTIINGYRLACKEAVKYISENISFTSDSIGRQSVVNAAKTSMSSKIIGPD 168
Cdd:TIGR02340 81 EVGDGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKENLSVSVDELGREALINVAKTSMSSKIIGLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 169 ADFFGELVVDAAEAVRVEN-NGKVTYPINAVNVLKAHGKSARESVLVKGYALNCTVASQAMPLRVQNAKIACLDFSLMKA 247
Cdd:TIGR02340 161 SDFFSNIVVDAVLAVKTTNeNGETKYPIKAINILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 248 KMHLGISVVVEDPAKLEAIRREEFDITKRRIDKILKAGANVVLTTGGIDDLCLKQFVESGAMAVRRCKKSDLKRIAKATG 327
Cdd:TIGR02340 241 KMALGVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 328 ATLTVSLATLEGDEAFDASLLGHADEIVQERISDDELILIKGPKSRTASSIILRGANDVMLDEMERSVHDSLCVVRRVLE 407
Cdd:TIGR02340 321 ATLVSTLADLEGEETFEASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 408 SKKLVAGGGAVETSLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKAQLIPQLQHLK 487
Cdd:TIGR02340 401 SNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAQLKPEKKHLK 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 3879449 488 WAGLDLEEGTIRDNKEAGILEPALSKVKSLKFATEAAITILRIDDLIKLDKQEPLG 543
Cdd:TIGR02340 481 WYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIKLNPEQSKG 536
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
32-535 |
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: 575.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 32 IANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQLQDEEVGDGTTSVVIVAAELLKRADEL 111
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 112 VKQKVHPTTIINGYRLACKEAVKYISENISFTSDSIGRQSVVNAAKTSMSSKIIGPDADFFGELVVDAAEAVRVENNgkv 191
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDG--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 192 TYPINAVNVLKAHGKSARESVLVKGYALNCTVASQAMPLRVQNAKIACLDFSLMKAKMHLGISVVVEDPAKLEAIRREEF 271
Cdd:pfam00118 158 SFDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 272 DITKRRIDKILKAGANVVLTTGGIDDLCLKQFVESGAMAVRRCKKSDLKRIAKATGATLTVSLATLEGDEafdaslLGHA 351
Cdd:pfam00118 238 EQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDD------LGTA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 352 DEIVQERISDDELILIKGPKSRTASSIILRGANDVMLDEMERSVHDSLCVVRRVLESKKLVAGGGAVETSLSLFLETYAQ 431
Cdd:pfam00118 312 GKVEEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 432 TLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKAQlipqlqhlKWAGLDLEEGTIRDNKEAGILEPAL 511
Cdd:pfam00118 392 SVSGKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGE--------KHAGIDVETGEIIDMKEAGVVDPLK 463
|
490 500
....*....|....*....|....
gi 3879449 512 SKVKSLKFATEAAITILRIDDLIK 535
Cdd:pfam00118 464 VKRQALKSATEAASTILRIDDIIK 487
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
13-535 |
0e+00 |
|
chaperonin families, type I and type II. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.
Pssm-ID: 238189 Cd Length: 464 Bit Score: 550.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 13 GKRTTGQGIRSQNVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQLQDEEVGD 92
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 93 GTTSVVIVAAELLKRADELVKQKVHPTTIINGYRLACKEAVKYIsENISFTSDSIGRQSVVNAAKTSMSSKIIGPDADFF 172
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEIL-KEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 173 GELVVDAAEAVRVENNgkvTYPINAVNVLKAHGKSARESVLVKGYALNCTVASQAMPLRVQNAKIACLDFSLMkakmhlg 252
Cdd:cd00309 160 GELVVDAVLKVGKENG---DVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLE------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 253 isvvvedpakleairreefditkrridkilkagaNVVLTTGGIDDLCLKQFVESGAMAVRRCKKSDLKRIAKATGATLTV 332
Cdd:cd00309 230 ----------------------------------YVVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 333 SLatlegdEAFDASLLGHADEIVQERISDDELILIKGPKSRTASSIILRGANDVMLDEMERSVHDSLCVVRRVLESKKLV 412
Cdd:cd00309 276 RL------EDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIV 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 413 AGGGAVETSLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKAQlipqlqhlKWAGLD 492
Cdd:cd00309 350 PGGGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGG--------GNAGGD 421
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 3879449 493 LEEGTIRDNKEAGILEPALSKVKSLKFATEAAITILRIDDLIK 535
Cdd:cd00309 422 VETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
14-534 |
4.29e-174 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 501.72 E-value: 4.29e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 14 KRTTGQGIRSQNVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQLQDEEVGDG 93
Cdd:NF041082 11 QRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 94 TTSVVIVAAELLKRADELVKQKVHPTTIINGYRLACKEAVKyISENISFTSDSIGRQSVVNAAKTSMSSKIIGPDADFFG 173
Cdd:NF041082 91 TTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALE-ILDEIAIKVDPDDKETLKKIAATAMTGKGAEAAKDKLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 174 ELVVDAAEAVrVENNGKVTYPINAVNVLKAHGKSARESVLVKGYALNCTVASQAMPLRVQNAKIACLDFSLMKAKMHLGI 253
Cdd:NF041082 170 DLVVDAVKAV-AEKDGGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 254 SVVVEDPAKLEAIRREEFDITKRRIDKILKAGANVVLTTGGIDDLCLKQFVESGAMAVRRCKKSDLKRIAKATGATLTVS 333
Cdd:NF041082 249 KISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 334 LatlegdEAFDASLLGHAdEIVQER-ISDDELILIKGPKSRTASSIILRGANDVMLDEMERSVHDSLCVVRRVLESKKLV 412
Cdd:NF041082 329 I------DDLSPEDLGYA-GLVEERkVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 413 AGGGAVETSLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKAqlipqlqhLKWAGLD 492
Cdd:NF041082 402 AGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKG--------NKTAGLD 473
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 3879449 493 LEEGTIRDNKEAGILEPALSKVKSLKFATEAAITILRIDDLI 534
Cdd:NF041082 474 VYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVI 515
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
14-534 |
1.93e-169 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 490.23 E-value: 1.93e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 14 KRTTGQGIRSQNVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQLQDEEVGDG 93
Cdd:NF041083 11 QRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 94 TTSVVIVAAELLKRADELVKQKVHPTTIINGYRLACKEAVKyISENISFTSDSIGRQSVVNAAKTSMSSKIIGPDADFFG 173
Cdd:NF041083 91 TTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIE-ILDEIAEKVDPDDRETLKKIAETSLTSKGVEEARDYLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 174 ELVVDAAEAVRVENNGKVTYPINAVNVLKAHGKSARESVLVKGYALNCTVASQAMPLRVQNAKIACLDFSLMKAKMHLGI 253
Cdd:NF041083 170 EIAVKAVKQVAEKRDGKYYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 254 SVVVEDPAKLEAIRREEFDITKRRIDKILKAGANVVLTTGGIDDLCLKQFVESGAMAVRRCKKSDLKRIAKATGATLTVS 333
Cdd:NF041083 250 EIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVTN 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 334 LATLEgdeafdASLLGHADEIVQERISDDELILIKGPKSRTASSIILRGANDVMLDEMERSVHDSLCVVRRVLESKKLVA 413
Cdd:NF041083 330 IDDLT------PEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 414 GGGAVETSLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKAQlipqlqhlKWAGLDL 493
Cdd:NF041083 404 GGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGK--------KWAGINV 475
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 3879449 494 EEGTIRDNKEAGILEPALSKVKSLKFATEAAITILRIDDLI 534
Cdd:NF041083 476 FTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVI 516
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
8-535 |
1.41e-166 |
|
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: 482.53 E-value: 1.41e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 8 ILALTGKRTTGQGIRSQNVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQLQD 87
Cdd:cd03343 3 ILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 88 EEVGDGTTSVVIVAAELLKRADELVKQKVHPTTIINGYRLACKEAVKyISENISFTSDSIGRQSVVNAAKTSMSSKIIGP 167
Cdd:cd03343 83 EEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALE-LLDEIAIKVDPDDKDTLRKIAKTSLTGKGAEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 168 DADFFGELVVDAAEAVRVENNGKVTYPINAVNVLKAHGKSARESVLVKGYALNCTVASQAMPLRVQNAKIACLDFSLMKA 247
Cdd:cd03343 162 AKDKLADLVVDAVLQVAEKRDGKYVVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 248 KMHLGISVVVEDPAKLEAIRREEFDITKRRIDKILKAGANVVLTTGGIDDLCLKQFVESGAMAVRRCKKSDLKRIAKATG 327
Cdd:cd03343 242 KTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 328 ATLTVSLATLEGDEafdaslLGHADEIVQERISDDELILIKGPKSRTASSIILRGANDVMLDEMERSVHDSLCVVRRVLE 407
Cdd:cd03343 322 AKIVTNIDDLTPED------LGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 408 SKKLVAGGGAVETSLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKAqlipqlqhLK 487
Cdd:cd03343 396 DGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKG--------NK 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 3879449 488 WAGLDLEEGTIRDNKEAGILEPALSKVKSLKFATEAAITILRIDDLIK 535
Cdd:cd03343 468 NAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIA 515
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
8-534 |
1.95e-155 |
|
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: 454.53 E-value: 1.95e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 8 ILALTGKRTTGQGIRSQNVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQLQD 87
Cdd:TIGR02339 4 ILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 88 EEVGDGTTSVVIVAAELLKRADELVKQKVHPTTIINGYRLACKEAVKYIsENISFTSDSIGRQSVVNAAKTSMSSKIIGP 167
Cdd:TIGR02339 84 EEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEII-DEIATKISPEDRDLLKKIAYTSLTSKASAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 168 DA-DFFGELVVDAAEAVRVE-NNGKVTYPINAVNVLKAHGKSARESVLVKGYALNCTVASQAMPLRVQNAKIACLDFSLM 245
Cdd:TIGR02339 163 VAkDKLADLVVEAVKQVAELrGDGKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDAPLE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 246 KAKMHLGISVVVEDPAKLEAIRREEFDITKRRIDKILKAGANVVLTTGGIDDLCLKQFVESGAMAVRRCKKSDLKRIAKA 325
Cdd:TIGR02339 243 VEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 326 TGATLTVSLatlegDEAfDASLLGHADEIVQERISDDELILIKGPKSRTASSIILRGANDVMLDEMERSVHDSLCVVRRV 405
Cdd:TIGR02339 323 TGARIVSSI-----DEI-TESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 406 LESKKLVAGGGAVETSLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKAqlipqlqh 485
Cdd:TIGR02339 397 LEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKG-------- 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 3879449 486 LKWAGLDLEEGTIRDNKEAGILEPALSKVKSLKFATEAAITILRIDDLI 534
Cdd:TIGR02339 469 NKNAGINVFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVI 517
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
17-538 |
7.91e-135 |
|
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: 401.67 E-value: 7.91e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 17 TGQGiRSQ---NVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQLQDEEVGDG 93
Cdd:cd03340 11 TSQG-KGQlisNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 94 TTSVVIVAAELLKRADELVKQKVHPTTIINGYRLACKEAVKYISE---NISFTSDSIGRQSVVNAAKTSMSSKIIGPDAD 170
Cdd:cd03340 90 TTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEiavNIDKEDKEEQRELLEKCAATALNSKLIASEKE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 171 FFGELVVDAAEAVRVENngkvtyPINAVNVLKAHGKSARESVLVKGYALNCTVaSQA----MPLRVQNAKIACLDFSL-M 245
Cdd:cd03340 170 FFAKMVVDAVLSLDDDL------DLDMIGIKKVPGGSLEDSQLVNGVAFKKTF-SYAgfeqQPKKFKNPKILLLNVELeL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 246 KAKMHlGISVVVEDPAKLEAIRREEFDITKRRIDKILKAGANVVLTTGGIDDLCLKQFVESGAMAVRRCKKSDLKRIAKA 325
Cdd:cd03340 243 KAEKD-NAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 326 TGATLTVSLATLegdeafDASLLGHADEIVQERISDDELILIKG-PKSRTAsSIILRGANDVMLDEMERSVHDSLCVVRR 404
Cdd:cd03340 322 TGGSIQTTVSNI------TDDVLGTCGLFEERQVGGERYNIFTGcPKAKTC-TIILRGGAEQFIEEAERSLHDAIMIVRR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 405 VLESKKLVAGGGAVETSLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKAQlipqlq 484
Cdd:cd03340 395 AIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGG------ 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 3879449 485 hLKWAGLDLEEGTIRDNKEAGILEPALSKVKSLKFATEAAITILRIDDLIKLDK 538
Cdd:cd03340 469 -GKWYGVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLILSVDETIKNPK 521
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
21-534 |
1.03e-126 |
|
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: 380.86 E-value: 1.03e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 21 IRSQNVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQLQDEEVGDGTTSVVIV 100
Cdd:cd03338 9 VRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 101 AAELLKRADELVKQKVHPTTIINGYRLACKEAVKYIsENISFTSDSIGRQSVVNAAKTSMSSKIIGPDADFFGELVVDAA 180
Cdd:cd03338 89 AGALLSACESLLKKGIHPTVISESFQIAAKKAVEIL-DSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 181 EAVrVENNGKVTYPINAVNVLKAHGKSARESVLVKGYALNCTVASQA-MPLRVQNAKIACLDFSLMKAKMHLGISVVVED 259
Cdd:cd03338 168 LKV-IDPATATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKAgGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVND 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 260 PAKLEAIRREEFDITKRRIDKILKAGANVVLTTGGI-----DDLCLKQFVESGAMAVRRCKKSDLKRIAKATGATLTVSL 334
Cdd:cd03338 247 YAQMDRILREERKYILNMCKKIKKSGCNVLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVASI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 335 atlegdEAFDASLLGHADEIVQERISDDELILIKG-PKSRTASSIILRGANDVMLDEMERSVHDSLCVVRRVLESKKLVA 413
Cdd:cd03338 327 ------DHFTEDKLGSADLVEEVSLGDGKIVKITGvKNPGKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 414 GGGAVETSLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKAQlipqlqhlKWAGLDL 493
Cdd:cd03338 401 GGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGE--------KNAGINV 472
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 3879449 494 EEGTIRDNKEAGILEPALSKVKSLKFATEAAITILRIDDLI 534
Cdd:cd03338 473 RKGAITNILEENVVQPLLVSTSAITLATETVRMILKIDDIV 513
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-535 |
1.83e-121 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 367.82 E-value: 1.83e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 1 MASAGDSILALTGKRTTGQGIRSQNVTAAVAIANIVKSSLGPVGLDKMLV-----DDVGDVIVTNDGATILKQLEVEHPA 75
Cdd:PTZ00212 3 MANVPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQpmsegPRSGNVTVTNDGATILKSVWLDNPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 76 GKVLVELAQLQDEEVGDGTTSVVIVAAELLKRADELVKQKVHPTTIINGYRLACKEAVKYIsENISFTSDS---IGRQSV 152
Cdd:PTZ00212 83 AKILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKAL-EEIAFDHGSdeeKFKEDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 153 VNAAKTSMSSKIIGPDADFFGELVVDAAEavRVENNGKVTYpinaVNVLKAHGKSARESVLVKGYALNCTVASqAMPLRV 232
Cdd:PTZ00212 162 LNIARTTLSSKLLTVEKDHFAKLAVDAVL--RLKGSGNLDY----IQIIKKPGGTLRDSYLEDGFILEKKIGV-GQPKRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 233 QNAKIACLDFSLMKAKMHL-GISVVVEDPAKLEAIRREEFDITKRRIDKILKAGANVVLTTGGIDDLCLKQFVESGAMAV 311
Cdd:PTZ00212 235 ENCKILVANTPMDTDKIKIyGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 312 RRCKKSDLKRIAKATGATLtvsLATLEGDEAFDaslLGHADEIVQERISDDELILIKGPKSRTASSIILRGANDVMLDEM 391
Cdd:PTZ00212 315 EHADFDGMERLAAALGAEI---VSTFDTPEKVK---LGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 392 ERSVHDSLCVVRRVLESKKLVAGGGAVETSLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLR 471
Cdd:PTZ00212 389 ERSLHDALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLR 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3879449 472 AYHSKAQlipqlqhlKWAGLDLEEGTIRDNKEAGILEPALSKVKSLKFATEAAITILRIDDLIK 535
Cdd:PTZ00212 469 AEHYKGN--------KTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIR 524
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
8-535 |
3.49e-120 |
|
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: 363.96 E-value: 3.49e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 8 ILALTGKRTTGQGIRSQNVTAAVAIANIVKSSLGPVGLDKML--VDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQL 85
Cdd:cd03336 1 ILKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 86 QDEEVGDGTTSVVIVAAELLKRADELVKQKVHPTTIINGYRLACKEAVKYISENISFTSDSIG--RQSVVNAAKTSMSSK 163
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEafREDLLNIARTTLSSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 164 IIGPDADFFGELVVDAAEavRVENNGKvtypINAVNVLKAHGKSARESVLVKGYALNCTVaSQAMPLRVQNAKIACLDFS 243
Cdd:cd03336 161 ILTQDKEHFAELAVDAVL--RLKGSGN----LDAIQIIKKLGGSLKDSYLDEGFLLDKKI-GVNQPKRIENAKILIANTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 244 LMKAKMHL-GISVVVEDPAKLEAIRREEFDITKRRIDKILKAGANVVLTTGGIDDLCLKQFVESGAMAVRRCKKSDLKRI 322
Cdd:cd03336 234 MDTDKIKIfGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 323 AKATGATLtvsLATLEGDEAfdaSLLGHADEIVQERISDDELILIKGPKSRTASSIILRGANDVMLDEMERSVHDSLCVV 402
Cdd:cd03336 314 ALVTGGEI---ASTFDHPEL---VKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 403 RRVLESKKLVAGGGAVETSLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKAQlipq 482
Cdd:cd03336 388 AQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGN---- 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 3879449 483 lqhlKWAGLDLEEGTIRDNKEAGILEPALSKVKSLKFATEAAITILRIDDLIK 535
Cdd:cd03336 464 ----TTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIK 512
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
25-538 |
1.39e-119 |
|
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: 362.54 E-value: 1.39e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 25 NVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQLQDEEVGDGTTSVVIVAAEL 104
Cdd:TIGR02345 23 NINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 105 LKRADELVKQKVHPTTIINGYRLACKEAVKYISEnISFTSDSI---GRQSVVNAAKTSMSSKIIGPDADFFGELVVDAAE 181
Cdd:TIGR02345 103 LKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKE-IAVTIDEEkgeQRELLEKCAATALSSKLISHNKEFFSKMIVDAVL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 182 AVRVENNGKvtypiNAVNVLKAHGKSARESVLVKGYALNCTVAS---QAMPLRVQNAKIACLDFSL-MKAKMHlGISVVV 257
Cdd:TIGR02345 182 SLDRDDLDL-----KLIGIKKVQGGALEDSQLVNGVAFKKTFSYagfEQQPKKFANPKILLLNVELeLKAEKD-NAEIRV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 258 EDPAKLEAIRREEFDITKRRIDKILKAGANVVLTTGGIDDLCLKQFVESGAMAVRRCKKSDLKRIAKATGATLTVSLATL 337
Cdd:TIGR02345 256 EDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTTSDL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 338 EGDeAFDASLLGHADEIVQERISddelILIKGPKSRTAsSIILRGANDVMLDEMERSVHDSLCVVRRVLESKKLVAGGGA 417
Cdd:TIGR02345 336 EAD-VLGTCALFEERQIGSERYN----YFTGCPHAKTC-TIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 418 VETSLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKAQlipqlqhlKWAGLDLEEGT 497
Cdd:TIGR02345 410 IEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGG--------KWYGVDINTED 481
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 3879449 498 IRDNKEAGILEPALSKVKSLKFATEAAITILRIDDLIKLDK 538
Cdd:TIGR02345 482 IGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITNPK 522
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
13-534 |
3.90e-110 |
|
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: 336.96 E-value: 3.90e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 13 GKRTTGQGIRSQNVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQLQDEEVGD 92
Cdd:cd03337 9 TKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 93 GTTSVVIVAAELLKRADELVKQKVHPTTIINGYRLACKEAVKyISENISFTSDSIGRQSVVNAAKTSMSSKIIGPDADFF 172
Cdd:cd03337 89 GTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALK-ILEEISIPVDVNDRAQMLKIIKSCIGTKFVSRWSDLM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 173 GELVVDAAEAVRVENNGKVTyPI---NAVNVLKAHGKSARESVLVKGYALNCTVASQAMPLRVQNAKIACLDFSLmkakm 249
Cdd:cd03337 168 CNLALDAVKTVAVEENGRKK-EIdikRYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPL----- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 250 hlgisvvvedpakleairreEFditkrridkilkaganVVLTTGGIDDLCLKQFVESGAMAVRRCKKSDLKRIAKATGAT 329
Cdd:cd03337 242 --------------------EY----------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIARACGAT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 330 LTVSLATLEGDEafdaslLGHADEIVQERISDDE----LILIKGPKsrtASSIILRGANDVMLDEMERSVHDSLCVVRRV 405
Cdd:cd03337 286 IVNRPEELTESD------VGTGAGLFEVKKIGDEyftfITECKDPK---ACTILLRGASKDVLNEVERNLQDAMAVARNI 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 406 LESKKLVAGGGAVETSLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSkaqlipQLQH 485
Cdd:cd03337 357 ILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHA------QGEN 430
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 3879449 486 LKWaGLDLEEGTIRDNKEAGILEPALSKVKSLKFATEAAITILRIDDLI 534
Cdd:cd03337 431 STW-GIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
13-535 |
6.30e-110 |
|
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: 337.73 E-value: 6.30e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 13 GKRTTGQGIRSQNVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQLQDEEVGD 92
Cdd:cd03339 16 KKRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 93 GTTSVVIVAAELLKRADELVKQKVHPTTIINGYRLACKEAVKY---ISENISFTSDSigRQSVVNAAKTSMSSKIIGPDA 169
Cdd:cd03339 96 GTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHleeIADKIEFSPDN--KEPLIQTAMTSLGSKIVSRCH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 170 DFFGELVVDAAEAVRVENNGKVTYPInaVNVLKAHGKSARESVLVKGYALNCTVASQAMPLRVQNAKIACLD--FSLMKA 247
Cdd:cd03339 174 RQFAEIAVDAVLSVADLERKDVNFEL--IKVEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAKIAILTcpFEPPKP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 248 KMHLGISVV-VEDPAKLEAIRREEFDitkRRIDKILKAGANVVLTTGGIDDLCLKQFVESGAMAVRRCKKSDLKRIAKAT 326
Cdd:cd03339 252 KTKHKLDITsVEDYKKLQEYEQKYFR---EMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIAT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 327 GATLTVSLATLEGDEafdaslLGHADeIVQER---ISDDELILIKGPKSRTASSIILRGANDVMLDEMERSVHDSLCVVR 403
Cdd:cd03339 329 GGRIVPRFEDLSPEK------LGKAG-LVREIsfgTTKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 404 RVLESKKLVAGGGAVETSLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKaQLIPQL 483
Cdd:cd03339 402 NLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVK-EKNPHL 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 3879449 484 qhlkwaGLD-LEEGTIrDNKEAGILEPALSKVKSLKFATEAAITILRIDDLIK 535
Cdd:cd03339 481 ------GIDcLGRGTN-DMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
19-534 |
1.91e-107 |
|
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: 331.36 E-value: 1.91e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 19 QGIRSQNVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQLQDEEVGDGTTSVV 98
Cdd:TIGR02342 8 QDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 99 IVAAELLKRADELVKQKVHPTTIINGYRLACKEAVKYISEnISFTSDSIGRQSVVNAAKTSMSSKIIGPDADFFGELVVD 178
Cdd:TIGR02342 88 ILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDE-MSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 179 AAEAVRVENNGKvTYPINAVNVLKAHGKSARESVLVKGYALNCTVASQA-MPLRVQNAKIACLDFSLMKAKMHLGISVVV 257
Cdd:TIGR02342 167 AVLKVIDPENAK-NVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDMENQIIV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 258 EDPAKLEAIRREEFDITKRRIDKILKAGANVVLTTGGI-----DDLCLKQFVESGAMAVRRCKKSDLKRIAKATGatlTV 332
Cdd:TIGR02342 246 NDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIG---CK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 333 SLATLEGdeaFDASLLGHADEIVQERISDDELILIKG-PKSRTASSIILRGANDVMLDEMERSVHDSLCVVRRVLESKKL 411
Cdd:TIGR02342 323 PIASIDH---FTADKLGSAELVEEVDSDGGKIIKITGiQNAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 412 VAGGGAVETSLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKAQlipqlqhlKWAGL 491
Cdd:TIGR02342 400 IAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGE--------KTAGI 471
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 3879449 492 DLEEGTIRDNKEAGILEPALSKVKSLKFATEAAITILRIDDLI 534
Cdd:TIGR02342 472 SVRKGGITNMLEEHVLQPLLVTTSAITLASETVRSILKIDDIV 514
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
22-541 |
5.01e-107 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 329.35 E-value: 5.01e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 22 RSQNVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHP----AGKVLVELAQLQDEEVGDGTTSV 97
Cdd:COG0459 12 RRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTTTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 98 VIVAAELLKRADELVKQKVHPTTIINGYRLACKEAVKYIsENISFTSDsiGRQSVVNAAKTSMSSKiigpdaDFFGELVV 177
Cdd:COG0459 92 TVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEEL-KKIAKPVD--DKEELAQVATISANGD------EEIGELIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 178 DAAEAvrVENNGKVTypinavnvLKAHGKSARESVLVKGYALNCTVAS-------QAMPLRVQNAKIACLDfslmkakmh 250
Cdd:COG0459 163 EAMEK--VGKDGVIT--------VEEGKGLETELEVVEGMQFDKGYLSpyfvtdpEKMPAELENAYILLTD--------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 251 lgisvvvedpAKLEAIRreefdITKRRIDKILKAGANVVLTTGGIDDLCLKQFVESGAMAVRRC-----------KKSDL 319
Cdd:COG0459 224 ----------KKISSIQ-----DLLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgdrRKAML 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 320 KRIAKATGATLtVSLATLEGDEAFDASLLGHADEIVqerISDDELILIKGPKSRTASSIILRGANDVMLDEMERSVHDSL 399
Cdd:COG0459 289 EDIAILTGGRV-ISEDLGLKLEDVTLDDLGRAKRVE---VDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDAL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 400 CVVRRVLESkKLVAGGGAVETSLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAyhskaql 479
Cdd:COG0459 365 HATRAAVEE-GIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRA------- 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3879449 480 ipqlQHLKWAGLDLEEGTIRDNKEAGILEPALSKVKSLKFATEAAITILRIDDLIKlDKQEP 541
Cdd:COG0459 437 ----AKDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIA-DKPEK 493
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
8-534 |
1.63e-106 |
|
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: 329.01 E-value: 1.63e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 8 ILALTGKRTTGQGIRSQNVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQLQD 87
Cdd:TIGR02344 4 VLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 88 EEVGDGTTSVVIVAAELLKRADELVKQKVHPTTIINGYRLACKEAVKYISEnISFTSDSIGRQSVVNAAKTSMSSKIIGP 167
Cdd:TIGR02344 84 EEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEE-ISIPVDVNDDAAMLKLIQSCIGTKFVSR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 168 DADFFGELVVDAAEAVRVENNGKVTYPINA-VNVLKAHGKSARESVLVKGYALNCTVASQAMPLRVQNAKIACLDFSLMK 246
Cdd:TIGR02344 163 WSDLMCDLALDAVRTVQRDENGRKEIDIKRyAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 247 AKMHLGISVVVEDPAKLEAIRREEFDITKRRIDKILKAGANVVLTTGGIDDLCLKQFVESGAMAVRRCKKSDLKRIAKAT 326
Cdd:TIGR02344 243 KKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARAC 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 327 GATLTVSLATL-EGDEAFDASLLghadEIvqERISDDELILIKGPKSRTASSIILRGANDVMLDEMERSVHDSLCVVRRV 405
Cdd:TIGR02344 323 GATIVNRPEELrESDVGTGCGLF----EV--KKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 406 LESKKLVAGGGAVETSLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKAQlipqlqh 485
Cdd:TIGR02344 397 LLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQEN------- 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 3879449 486 LKWAGLDLEEGTIRDNKEAGILEPALSKVKSLKFATEAAITILRIDDLI 534
Cdd:TIGR02344 470 NCTWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
13-535 |
1.81e-105 |
|
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: 326.76 E-value: 1.81e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 13 GKRTTGQGIRSQNVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQLQDEEVGD 92
Cdd:TIGR02343 20 KKRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 93 GTTSVVIVAAELLKRADELVKQKVHPTTIINGYRLACKEAVKY---ISENISFTSDSigRQSVVNAAKTSMSSKIIGPDA 169
Cdd:TIGR02343 100 GTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHleeISDEISADNNN--REPLIQAAKTSLGSKIVSKCH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 170 DFFGELVVDAAEAVRVENNGKVTYPInaVNVLKAHGKSARESVLVKGYALNCTVASQAMPLRVQNAKIACLDFSLMKAKM 249
Cdd:TIGR02343 178 RRFAEIAVDAVLNVADMERRDVDFDL--IKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAILTCPFEPPKP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 250 HLGISVVVEDPAKLEAIRREEFDITKRRIDKILKAGANVVLTTGGIDDLCLKQFVESGAMAVRRCKKSDLKRIAKATGAT 329
Cdd:TIGR02343 256 KTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 330 LTVSLATLEGDEafdaslLGHADEIVQERI--SDDELILIKGPKSRTASSIILRGANDVMLDEMERSVHDSLCVVRRVLE 407
Cdd:TIGR02343 336 IVPRFQELSKDK------LGKAGLVREISFgtTKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 408 SKKLVAGGGAVETSLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKaQLIPQLqhlk 487
Cdd:TIGR02343 410 DSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLK-EKNPNL---- 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 3879449 488 waGLD-LEEGTiRDNKEAGILEPALSKVKSLKFATEAAITILRIDDLIK 535
Cdd:TIGR02343 485 --GVDcLGYGT-NDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVIS 530
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
25-534 |
5.23e-103 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239457 [Multi-domain] Cd Length: 472 Bit Score: 318.40 E-value: 5.23e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 25 NVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQLQDEEVGDGTTSVVIVAAEL 104
Cdd:cd03341 13 NIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 105 LKRADELVKQKVHPTTIINGYRLACKEAVKYISENISFT-SDSIGRQSVVNAAKTSMSSKIIGPDaDFFGELVVDAAEAV 183
Cdd:cd03341 93 LEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKiEDLRNKEEVSKALKTAIASKQYGNE-DFLSPLVAEACISV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 184 RVENNGkvTYPINAVNVLKAHGKSARESVLVKGYALNCTVASQAmpLRVQNAKIAcldfslmkakmhlgisvVVEDPakl 263
Cdd:cd03341 172 LPENIG--NFNVDNIRVVKILGGSLEDSKVVRGMVFKREPEGSV--KRVKKAKVA-----------------VFSCP--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 264 eairreeFDItkrridkilkaGANVVLTTGGIDDLCLkQFVES-GAMAVRRCKKSDLKRIAKATGATLTVSLATLEGDEa 342
Cdd:cd03341 228 -------FDI-----------GVNVIVAGGSVGDLAL-HYCNKyGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEE- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 343 fdaslLGHADEIVQERISDDELILIKGPKSRTA-SSIILRGANDVMLDEMERSVHDSLCVVRRVLESKKLVAGGGAVETS 421
Cdd:cd03341 288 -----IGYCDSVYVEEIGDTKVVVFRQNKEDSKiATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 422 LSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKAQlipqlqhlKWAGLDLEEG--TIR 499
Cdd:cd03341 363 LAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGN--------KSAGVDIESGdeGTK 434
|
490 500 510
....*....|....*....|....*....|....*
gi 3879449 500 DNKEAGILEPALSKVKSLKFATEAAITILRIDDLI 534
Cdd:cd03341 435 DAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
24-534 |
3.23e-99 |
|
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274087 [Multi-domain] Cd Length: 531 Bit Score: 310.49 E-value: 3.23e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 24 QNVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQLQDEEVGDGTTSVVIVAAE 103
Cdd:TIGR02346 22 KNIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 104 LLKRADELVKQKVHPTTIINGYRLACKEAVKYISENISFT-SDSIGRQSVVNAAKTSMSSKIIGpDADFFGELVVDAAEA 182
Cdd:TIGR02346 102 LLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEvKDLRDKDELIKALKASISSKQYG-NEDFLAQLVAQACST 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 183 VRVENNGkvTYPINAVNVLKAHGKSARESVLVKGYALNctVASQAMPLRVQNAKIACLDFSLMKAKMHLGISVVVEDPAK 262
Cdd:TIGR02346 181 VLPKNPQ--NFNVDNIRVCKILGGSLSNSEVLKGMVFN--REAEGSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNAEE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 263 LEAIRREEFDITKRRIDKILKAGANVVLTTGGIDDLCLkQFVES-GAMAVRRCKKSDLKRIAKATGATLTVSLATLEGDE 341
Cdd:TIGR02346 257 LLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMAL-HYLNKyNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 342 afdaslLGHADEIVQERISDDELILIKGPKSRTA-SSIILRGANDVMLDEMERSVHDSLCVVRRVLESKKLVAGGGAVET 420
Cdd:TIGR02346 336 ------IGYVDSVYVSEIGGDKVTVFKQENGDSKiSTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEI 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 421 SLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKAQlipqlqhlKWAGLDLEEGTIR- 499
Cdd:TIGR02346 410 ELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGN--------KSKGIDIEAESDGv 481
|
490 500 510
....*....|....*....|....*....|....*.
gi 3879449 500 -DNKEAGILEPALSKVKSLKFATEAAITILRIDDLI 534
Cdd:TIGR02346 482 kDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQII 517
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
8-535 |
6.39e-98 |
|
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: 306.79 E-value: 6.39e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 8 ILALTGKRTTGQGIRSQNVTAAVAIANIVKSSLGPVGLDKMLVDD--VGDVIVTNDGATILKQLEVEHPAGKVLVELAQL 85
Cdd:TIGR02341 2 IFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSssDASIMVTNDGATILKSIGVDNPAAKVLVDMSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 86 QDEEVGDGTTSVVIVAAELLKRADELVKQKVHPTTIINGYRLACKEAVKYISEN-ISFTSDSIG-RQSVVNAAKTSMSSK 163
Cdd:TIGR02341 82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSaVDNGSDEVKfRQDLMNIARTTLSSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 164 IIGPDADFFGELVVDAaeAVRVENNGKvtypINAVNVLKAHGKSARESVLVKGYALNCTVASQaMPLRVQNAKIACLDFS 243
Cdd:TIGR02341 162 ILSQHKDHFAQLAVDA--VLRLKGSGN----LEAIQIIKKLGGSLADSYLDEGFLLDKKIGVN-QPKRIENAKILIANTG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 244 LMKAKMHL-GISVVVEDPAKLEAIRREEFDITKRRIDKILKAGANVVLTTGGIDDLCLKQFVESGAMAVRRCKKSDLKRI 322
Cdd:TIGR02341 235 MDTDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 323 AKATGATLTvslATLEGDEAFDaslLGHADEIVQERISDDELILIKGPKSRTASSIILRGANDVMLDEMERSVHDSLCVV 402
Cdd:TIGR02341 315 ALVTGGEIV---STFDHPELVK---LGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 403 RRVLESKKLVAGGGAVETSLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKAQlipq 482
Cdd:TIGR02341 389 SQTVKESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGN---- 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 3879449 483 lqhlKWAGLDLEEGTIRDNKEAGILEPALSKVKSLKFATEAAITILRIDDLIK 535
Cdd:TIGR02341 465 ----TTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIK 513
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
25-535 |
8.88e-78 |
|
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: 252.95 E-value: 8.88e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 25 NVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQLQDEEVGDGTTSVVIVAAEL 104
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 105 LKRADELVKQKVHPTTIINGYRLACKEAVKYISENISFTSDSIGRQSVVNAAKTSMSSKIIGPDADFFGELVVDAAEAVR 184
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 185 VENNgkvtyPI--NAVNVLKAHGKSARESVLVKGYALNCTVASQAMPLRVQNAKIACLDFSLmkakmhlgisvvvedpak 262
Cdd:cd03342 177 KPDE-----PIdlHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSL------------------ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 263 leairreEFDITKrridkiLKAG--ANVVLTTGGIDDLCLKQFVESGAMAVRRCKKSDLKRIAKATGATLTVSLATLEGD 340
Cdd:cd03342 234 -------EYEKTE------VNSGffYSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 341 EafdaslLGHADEIVQERISDDELILIKGPKSRTASSIILRGANDVMLDEMERSVHDSLCVVRRVLESKKLVAGGGAVET 420
Cdd:cd03342 301 C------LGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 421 SLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKAQLIPqlqhlkwaGLDLEEGTIRD 500
Cdd:cd03342 375 ALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVG--------GVDLDTGEPMD 446
|
490 500 510
....*....|....*....|....*....|....*
gi 3879449 501 NKEAGILEPALSKVKSLKFATEAAITILRIDDLIK 535
Cdd:cd03342 447 PESEGIWDNYSVKRQILHSATVIASQLLLVDEIIR 481
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
25-535 |
3.91e-77 |
|
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: 252.73 E-value: 3.91e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 25 NVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPAGKVLVELAQLQDEEVGDGTTSVVIVAAEL 104
Cdd:TIGR02347 21 NINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 105 LKRADELVKQKVHPTTIINGYRLACKEAVKYISENISFTSDSIGRQSVVNAAKTSMSSKIIGPDADFFGELVVDAAEAVR 184
Cdd:TIGR02347 101 LKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEVDREFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 185 venngKVTYPIN--AVNVLKAHGKSARESVLVKGYALNCTVASQAMPLRVQNAKIACLDFSLMKAKMHLGISVVVEDPAK 262
Cdd:TIGR02347 181 -----KDGEDIDlfMVEIMEMKHKSATDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 263 LEAIRREEFDITKRRIDKI--LKA-----GAN---VVLTTGGIDDLCLKQFVESGAMAVRRCKKSDLKRIAKATGATLTV 332
Cdd:TIGR02347 256 REKLVKAERKFVDDRVKKIieLKKkvcgkSPDkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEALN 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 333 SLATLEGDEafdaslLGHADEIVQERISDDELILI---KGPKSRTassIILRGANDVMLDEMERSVHDSLCVVRRVLESK 409
Cdd:TIGR02347 336 SVEDLTPEC------LGWAGLVYETTIGEEKYTFIeecKNPKSCT---ILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 410 KLVAGGGAVETSLSLFLETYAQTLSSREQLAVAEFASALLIIPKVLASNAARDSTDLVTKLRAYHSKAQlipqlqhlKWA 489
Cdd:TIGR02347 407 CVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGG--------EVV 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 3879449 490 GLDLEEGTIRDNKEAGILEPALSKVKSLKFATEAAITILRIDDLIK 535
Cdd:TIGR02347 479 GVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMR 524
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
149-408 |
3.01e-63 |
|
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: 205.78 E-value: 3.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 149 RQSVVNAAKTSMSSKIIGpDADFFGELVVDAAEAVRVENNgkvTYPINAVNVLKAHGKSARESVLVKGYALNCTVASQAM 228
Cdd:cd03333 1 RELLLQVATTSLNSKLSS-WDDFLGKLVVDAVLKVGPDNR---MDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 229 PLRVQNAKIACLDFSLMkakmhlgisvvvedpakleairreefditkrridkilkagaNVVLTTGGIDDLCLKQFVESGA 308
Cdd:cd03333 77 PKRLENAKILLLDCPLE-----------------------------------------YVVIAEKGIDDLALHYLAKAGI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 309 MAVRRCKKSDLKRIAKATGATLTVSLatlegdEAFDASLLGHADEIVQERISDDELILIKGPKSRTASSIILRGANDVML 388
Cdd:cd03333 116 MAVRRVKKEDLERIARATGATIVSSL------EDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVEL 189
|
250 260
....*....|....*....|
gi 3879449 389 DEMERSVHDSLCVVRRVLES 408
Cdd:cd03333 190 DEVKRSLHDALCAVRAAVEE 209
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
175-402 |
6.22e-15 |
|
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: 74.95 E-value: 6.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 175 LVVDAAEAVRVE-NNGKVTYPINAVNVLKAHGKSARESVLVKGYALNCTVASQAMPLRVQNAKIACLDFSLMKAKmhlgi 253
Cdd:cd03334 26 LVWKAASNVKPDvRAGDDMDIRQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLEYQR----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 254 svvVEDP-AKLEAIRREEFDITKRRIDKILKAGANVVLTTGGIDDLCLKQFVESGAMAVRRCKKSDLKRIAKATGATLTV 332
Cdd:cd03334 101 ---VENKlLSLDPVILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIIS 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3879449 333 SlatleGDEAFDASLLGHADEIVQERISDDE-----LILIKGPKSRTASSIILRGANDVMLDEMERSVHDSLCVV 402
Cdd:cd03334 178 S-----MDDLLTSPKLGTCESFRVRTYVEEHgrsktLMFFEGCPKELGCTILLRGGDLEELKKVKRVVEFMVFAA 247
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
31-136 |
9.92e-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: 60.93 E-value: 9.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 31 AIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHP---AG-KVLVELAQLQDEEVGDGTTSVVIVAAELLK 106
Cdd:cd03344 19 KLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenMGaQLVKEVASKTNDVAGDGTTTATVLARAIIK 98
|
90 100 110
....*....|....*....|....*....|
gi 3879449 107 RADELVKQKVHPTTIINGYRLACKEAVKYI 136
Cdd:cd03344 99 EGLKAVAAGANPMDLKRGIEKAVEAVVEEL 128
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
32-532 |
3.57e-08 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 56.07 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 32 IANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHP---AGKVLV-ELAQLQDEEVGDGTTSVVIVAAELLKR 107
Cdd:PTZ00114 34 LADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRfenVGAQLIrQVASKTNDKAGDGTTTATILARAIFRE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 108 ADELVKQKVHPTTIINGYRLACKEAVKYISENisfTSDSIGRQSVVNAAK--TSMSSKIigpdadffGELVVDAAEAVrv 185
Cdd:PTZ00114 114 GCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQ---SRPVKTKEDILNVATisANGDVEI--------GSLIADAMDKV-- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 186 ennGKvtypiNAVNVLKAHGKSARESVLVKGYALNCTVASQAMPLRVQNAKIACLD-FSLMKAKMHLGISVVVedPAkLE 264
Cdd:PTZ00114 181 ---GK-----DGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENpLILVTDKKISSIQSIL--PI-LE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 265 AIRReefdiTKRRIDKILKAGANVVLTT-------GGIDDLCLK--QFVESgamavrrcKKSDLKRIAKATGATLTVSLA 335
Cdd:PTZ00114 250 HAVK-----NKRPLLIIAEDVEGEALQTliinklrGGLKVCAVKapGFGDN--------RKDILQDIAVLTGATVVSEDN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 336 TLEGDEAFDASLLGHADEIVqerISDDELILIKGP----------------KSRTASS-------------------IIL 380
Cdd:PTZ00114 317 VGLKLDDFDPSMLGSAKKVT---VTKDETVILTGGgdkaeikervellrsqIERTTSEydkeklkerlaklsggvavIKV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 381 RGANDVMLDEMERSVHDSLCVVRRVLESkKLVAGGGAVETSLSLFLETYAQT--LSSREQLAVAEFASALLIIPKVLASN 458
Cdd:PTZ00114 394 GGASEVEVNEKKDRIEDALNATRAAVEE-GIVPGGGVALLRASKLLDKLEEDneLTPDQRTGVKIVRNALRLPTKQIAEN 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 459 AARDSTDLVTKLRAYHSKAQlipqlqhlkwaGLDLEEGTIRDNKEAGILEP----------ALSkVKSLKFATEAAITIL 528
Cdd:PTZ00114 473 AGVEGAVVVEKILEKKDPSF-----------GYDAQTGEYVNMFEAGIIDPtkvvrsalvdAAS-VASLMLTTEAAIVDL 540
|
....
gi 3879449 529 RIDD 532
Cdd:PTZ00114 541 PKEK 544
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
31-192 |
9.63e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 54.72 E-value: 9.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 31 AIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHP---AGKVLV-ELAQLQDEEVGDGTTSVVIVAAELLK 106
Cdd:PRK12850 22 ILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenMGAQMVkEVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 107 RADELVKQKVHPTTIINGYRLACKEAVKYISENIS--FTSDSIGRQSVVNAAktsmsskiigpDADFFGELVVDAAEavR 184
Cdd:PRK12850 102 EGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKkvTSSKEIAQVATISAN-----------GDESIGEMIAEAMD--K 168
|
....*...
gi 3879449 185 VENNGKVT 192
Cdd:PRK12850 169 VGKEGVIT 176
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
22-192 |
1.94e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 53.59 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 22 RSQNVTAAVAIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHP----AGKVLVELAQLQDEEVGDGTTSV 97
Cdd:PRK12851 13 REKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 98 VIVAAELLKRADELVKQKVHPTTIINGYRLACKEAVKYISENisftsdsigRQSVVNAAKTSMSSKIIGPDADFFGELVV 177
Cdd:PRK12851 93 TVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKAN---------ARPVTTNAEIAQVATISANGDAEIGRLVA 163
|
170
....*....|....*
gi 3879449 178 DAAEavRVENNGKVT 192
Cdd:PRK12851 164 EAME--KVGNEGVIT 176
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
31-192 |
4.87e-07 |
|
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES cytosolic chaperonin. It is found in bacteria, organelles derived from bacteria, and occasionally in the Archaea. The bacterial GroEL/GroES group I chaperonin is replaced a group II chaperonin, usually called the thermosome in the Archaeota and CCT (chaperone-containing TCP) in the Eukaryota. GroEL, thermosome subunits, and CCT subunits all fall under the scope of pfam00118. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274089 Cd Length: 524 Bit Score: 52.30 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 31 AIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHP----AGKVLVELAQLQDEEVGDGTTSVVIVAAELLK 106
Cdd:TIGR02348 20 KLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKfenmGAQLVKEVASKTNDVAGDGTTTATVLAQAIVK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 107 RADELVKQKVHPTTIINGYRLACKEAVKYISENISFTSDSigrQSVVNAAKTSMsskiiGPDADfFGELVVDAAEavRVE 186
Cdd:TIGR02348 100 EGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGK---KEIAQVATISA-----NNDEE-IGSLIAEAME--KVG 168
|
....*.
gi 3879449 187 NNGKVT 192
Cdd:TIGR02348 169 KDGVIT 174
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
32-541 |
5.44e-07 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 52.23 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 32 IANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHP----AGKVLVELAQLQDEEVGDGTTSVVIVAAELLKR 107
Cdd:PLN03167 78 LADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 108 ADELVKQKVHPTTIINGYRLACKEAVKYISENISFTSDS-IGRQSVVNAAKTSMSSKIIgpdadffgelvvdaAEAV-RV 185
Cdd:PLN03167 158 GVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDSeLADVAAVSAGNNYEVGNMI--------------AEAMsKV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 186 ENNGKVTYpinavnvlkAHGKSARESVLV-------KGYALNCTVA-SQAMPLRVQNAKIACLDFSLMKAKMHLGIsvvV 257
Cdd:PLN03167 224 GRKGVVTL---------EEGKSAENNLYVvegmqfdRGYISPYFVTdSEKMSVEYDNCKLLLVDKKITNARDLIGI---L 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 258 ED------PAKLEAIRREEFDITKRRIDKILKAGANVVLTTGG--------IDDLClkqfVESGAMAVR-----RCKKSD 318
Cdd:PLN03167 292 EDairggyPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGfgerksqyLDDIA----ILTGGTVIReevglSLDKVG 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 319 LKRIAKATGATLTVSLATLEGDEAFDASLLGHADEI-----VQERISDDELILIKGPKSRTASSIILRGAN-DVMLDEME 392
Cdd:PLN03167 368 KEVLGTAAKVVLTKDTTTIVGDGSTQEAVNKRVAQIknlieAAEQDYEKEKLNERIAKLSGGVAVIQVGAQtETELKEKK 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 393 RSVHDSLCVVRRVLEsKKLVAGGGAVETSLSLFLETYAQTLSSREQLAVAEFASALLIIP-KVLASNAARDSTDLVTKLR 471
Cdd:PLN03167 448 LRVEDALNATKAAVE-EGIVVGGGCTLLRLASKVDAIKDTLENDEQKVGADIVKRALSYPlKLIAKNAGVNGSVVSEKVL 526
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 472 AYHSKAQlipqlqhlkwaGLDLEEGTIRDNKEAGILEPALSKVKSLKFATEAAITILrIDDLIKLDKQEP 541
Cdd:PLN03167 527 SNDNPKF-----------GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFL-TSDCVVVEIKEP 584
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
31-134 |
1.17e-05 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 47.88 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 31 AIANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHP----AGKVLVELAQLQDEEVGDGTTSVVIVAAELLK 106
Cdd:PRK12849 21 KLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQALVQ 100
|
90 100
....*....|....*....|....*...
gi 3879449 107 RADELVKQKVHPTTIINGYRLACKEAVK 134
Cdd:PRK12849 101 EGLKNVAAGANPMDLKRGIDKAVEAVVE 128
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
31-139 |
6.75e-05 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 45.50 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 31 AIANIVKSSLGP----VGLDKmlvdDVGDVIVTNDGATILKQLEVEHP---AGKVLV-ELAQLQDEEVGDGTTSVVIVAA 102
Cdd:PRK00013 21 KLADAVKVTLGPkgrnVVLEK----SFGAPTITKDGVTVAKEIELEDPfenMGAQLVkEVASKTNDVAGDGTTTATVLAQ 96
|
90 100 110
....*....|....*....|....*....|....*..
gi 3879449 103 ELLKRADELVKQKVHPTTIINGYRLACKEAVKYISEN 139
Cdd:PRK00013 97 AIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKI 133
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
32-183 |
1.46e-04 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 44.32 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3879449 32 IANIVKSSLGPVGLDKMLVDDVGDVIVTNDGATILKQLEVEHPA---GKVLVELAQLQDEEV-GDGTTSVVIVAAELLKR 107
Cdd:CHL00093 22 LAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIentGVALIRQAASKTNDVaGDGTTTATVLAYAIVKQ 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3879449 108 ADELVKQKVHPTTIINGYRLACKEAVKYISENISFTSDSigrQSVVNAAktSMSSkiiGPDADfFGELVVDAAEAV 183
Cdd:CHL00093 102 GMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDI---QAITQVA--SISA---GNDEE-VGSMIADAIEKV 168
|
|
| |
