|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
2-486 |
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: 969.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 2 DVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVR 81
Cdd:cd03335 43 DVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 82 YINENLIINTDELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVKYTDARGQPRYPVNSVNILKAHGRSQIESML 161
Cdd:cd03335 123 YIKEHLSISVDNLGKESLINVAKTSMSSKIIGADSDFFANMVVDAILAVKTTNEKGKTKYPIKAVNILKAHGKSAKESYL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 162 INGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTG 241
Cdd:cd03335 203 VNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKLGVQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 242 GIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEETFEVTMLGQAEEVVQERICDDELILIKNTKAR 321
Cdd:cd03335 283 GIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVSTLANLEGEETFDPSYLGEAEEVVQERIGDDELILIKGTKKR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 322 TSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPN 401
Cdd:cd03335 363 SSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPK 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 402 TLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDL 481
Cdd:cd03335 443 TLAVNAAKDATELVAKLRAYHAAAQVKPDKKHLKWYGLDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDL 522
|
....*
gi 595582154 482 IKLHP 486
Cdd:cd03335 523 IKLNP 527
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
2-491 |
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: 913.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 2 DVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVR 81
Cdd:TIGR02340 47 DVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 82 YINENLIINTDELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVKYTDARGQPRYPVNSVNILKAHGRSQIESML 161
Cdd:TIGR02340 127 YIKENLSVSVDELGREALINVAKTSMSSKIIGLDSDFFSNIVVDAVLAVKTTNENGETKYPIKAINILKAHGKSARESML 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 162 INGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTG 241
Cdd:TIGR02340 207 VKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAKMALGVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 242 GIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEETFEVTMLGQAEEVVQERICDDELILIKNTKAR 321
Cdd:TIGR02340 287 GIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVSTLADLEGEETFEASYLGFADEVVQERIADDECILIKGTKKR 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 322 TSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPN 401
Cdd:TIGR02340 367 KSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPK 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 402 TLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDL 481
Cdd:TIGR02340 447 TLAVNAAKDSTELVAKLRAYHAAAQLKPEKKHLKWYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDL 526
|
490
....*....|
gi 595582154 482 IKLHPESKDD 491
Cdd:TIGR02340 527 IKLNPEQSKG 536
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
2-483 |
4.69e-177 |
|
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: 506.74 E-value: 4.69e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 2 DVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVR 81
Cdd:pfam00118 24 DVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKLLAAGVHPTTIIEGYEKALEKALE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 82 YINENLIINTDELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVKYTDArgqpRYPVNSVNILKAHGRSQIESML 161
Cdd:pfam00118 104 ILDSIISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDG----SFDLGNIGVVKILGGSLEDSEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 162 INGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTG 241
Cdd:pfam00118 180 VDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQILEIVEKIIDSGVNVVVCQK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 242 GIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEEtfevtmLGQAEEVVQERICDDELILIKNTKAR 321
Cdd:pfam00118 260 GIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDD------LGTAGKVEEEKIGDEKYTFIEGCKSP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 322 TSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPN 401
Cdd:pfam00118 334 KAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGKEQLAIEAFAEALEVIPK 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 402 TLAVNAAQDSTDLVAKLRAFHNeaqvnperKNLKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDL 481
Cdd:pfam00118 414 TLAENAGLDPIEVLAELRAAHA--------SGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDI 485
|
..
gi 595582154 482 IK 483
Cdd:pfam00118 486 IK 487
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
2-483 |
3.19e-175 |
|
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: 501.19 E-value: 3.19e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 2 DVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVR 81
Cdd:cd00309 43 DPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 82 YINENLIiNTDELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVKytdaRGQPRYPVNSVNILKAHGRSQIESML 161
Cdd:cd00309 123 ILKEIAV-PIDVEDREELLKVATTSLNSKLVSGGDDFLGELVVDAVLKVG----KENGDVDLGVIRVEKKKGGSLEDSEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 162 INGYALNCVVGSQGMPKRIVNAKIACLDFSLQktkmklgvqvvitdpekldqirqresditkeriqkilatgaNVILTTG 241
Cdd:cd00309 198 VVGMVFDKGYLSPYMPKRLENAKILLLDCKLE-----------------------------------------YVVIAEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 242 GIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEetfevtMLGQAEEVVQERICDDELILIKNTKAR 321
Cdd:cd00309 237 GIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLEDLTPE------DLGTAGLVEETKIGDEKYTFIEGCKGG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 322 TSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPN 401
Cdd:cd00309 311 KVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 402 TLAVNAAQDSTDLVAKLRAFHNEAQvnperknlKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDL 481
Cdd:cd00309 391 TLAENAGLDPIEVVTKLRAKHAEGG--------GNAGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDI 462
|
..
gi 595582154 482 IK 483
Cdd:cd00309 463 IV 464
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
2-482 |
2.00e-153 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 447.41 E-value: 2.00e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 2 DVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVR 81
Cdd:NF041082 52 DVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 82 YINEnLIINTDELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVkyTDARGQPRYPVNSVNILKAHGRSQIESML 161
Cdd:NF041082 132 ILDE-IAIKVDPDDKETLKKIAATAMTGKGAEAAKDKLADLVVDAVKAV--AEKDGGYNVDLDNIKVEKKVGGSIEDSEL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 162 INGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTG 241
Cdd:NF041082 209 VEGVVIDKERVHPGMPKRVENAKIALLDAPLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 242 GIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEEtfevtmLGQAEEVVQERICDDELILIKNTKAR 321
Cdd:NF041082 289 GIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSIDDLSPED------LGYAGLVEERKVGGDKMIFVEGCKNP 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 322 TSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPN 401
Cdd:NF041082 363 KAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPR 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 402 TLAVNAAQDSTDLVAKLRAFHNeaqvnperKNLKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDL 481
Cdd:NF041082 443 TLAENAGLDPIDALVELRSAHE--------KGNKTAGLDVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDV 514
|
.
gi 595582154 482 I 482
Cdd:NF041082 515 I 515
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
2-482 |
2.56e-152 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 444.78 E-value: 2.56e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 2 DVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVR 81
Cdd:NF041083 52 DIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 82 YINEnLIINTDELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVkyTDARGQpRYPV--NSVNILKAHGRSQIES 159
Cdd:NF041083 132 ILDE-IAEKVDPDDRETLKKIAETSLTSKGVEEARDYLAEIAVKAVKQV--AEKRDG-KYYVdlDNIQIEKKHGGSIEDT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 160 MLINGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILT 239
Cdd:NF041083 208 QLIYGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFC 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 240 TGGIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEEtfevtmLGQAEEVVQERICDDELILIKNTK 319
Cdd:NF041083 288 QKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVTNIDDLTPED------LGYAELVEERKVGDDKMVFVEGCK 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 320 ARTSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVI 399
Cdd:NF041083 362 NPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEII 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 400 PNTLAVNAAQDSTDLVAKLRAFHNEAQvnperknlKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRID 479
Cdd:NF041083 442 PRTLAENAGLDPIDILVKLRSAHEKGK--------KWAGINVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRID 513
|
...
gi 595582154 480 DLI 482
Cdd:NF041083 514 DVI 516
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
2-483 |
6.93e-150 |
|
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: 438.62 E-value: 6.93e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 2 DVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVR 81
Cdd:cd03343 50 DVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 82 YInENLIINTDELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVKYTDaRGQPRYPVNSVNILKAHGRSQIESML 161
Cdd:cd03343 130 LL-DEIAIKVDPDDKDTLRKIAKTSLTGKGAEAAKDKLADLVVDAVLQVAEKR-DGKYVVDLDNIKIEKKTGGSVDDTEL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 162 INGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTG 241
Cdd:cd03343 208 IRGIVIDKEVVHPGMPKRVENAKIALLDAPLEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQK 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 242 GIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEEtfevtmLGQAEEVVQERICDDELILIKNTKAR 321
Cdd:cd03343 288 GIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTNIDDLTPED------LGEAELVEERKVGDDKMVFVEGCKNP 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 322 TSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPN 401
Cdd:cd03343 362 KAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPR 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 402 TLAVNAAQDSTDLVAKLRAFHNeaqvnperKNLKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDL 481
Cdd:cd03343 442 TLAENAGLDPIDTLVELRAAHE--------KGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDV 513
|
..
gi 595582154 482 IK 483
Cdd:cd03343 514 IA 515
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
2-482 |
4.38e-143 |
|
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: 421.40 E-value: 4.38e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 2 DVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVR 81
Cdd:TIGR02339 51 DVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 82 YInENLIINTDELGRDCLINAAKTSMSSK-IIGINGDYFANMVVDAVLAVKYTDARGQPRYPVNSVNILKAHGRSQIESM 160
Cdd:TIGR02339 131 II-DEIATKISPEDRDLLKKIAYTSLTSKaSAEVAKDKLADLVVEAVKQVAELRGDGKYYVDLDNIKIVKKKGGSIEDTE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 161 LINGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTT 240
Cdd:TIGR02339 210 LVEGIVVDKEVVHPGMPKRVENAKIALLDAPLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 241 GGIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEEtfevtmLGQAEEVVQERICDDELILIKNTKA 320
Cdd:TIGR02339 290 KGIDDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVSSIDEITESD------LGYAELVEERKVGEDKMVFVEGCKN 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 321 RTSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIP 400
Cdd:TIGR02339 364 PKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIP 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 401 NTLAVNAAQDSTDLVAKLRAFHNeaqvnperKNLKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDD 480
Cdd:TIGR02339 444 RILAENAGLDPIDALVDLRAKHE--------KGNKNAGINVFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDD 515
|
..
gi 595582154 481 LI 482
Cdd:TIGR02339 516 VI 517
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
2-488 |
1.57e-129 |
|
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: 386.64 E-value: 1.57e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 2 DVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVR 81
Cdd:cd03340 51 KVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 82 YINE---NLIINTDELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVKYTDargqpryPVNSVNILKAHGRSQIE 158
Cdd:cd03340 131 KIKEiavNIDKEDKEEQRELLEKCAATALNSKLIASEKEFFAKMVVDAVLSLDDDL-------DLDMIGIKKVPGGSLED 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 159 SMLING--------YAlncvvGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKIL 230
Cdd:cd03340 204 SQLVNGvafkktfsYA-----GFEQQPKKFKNPKILLLNVELELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 231 ATGANVILTTGGIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEetfevtMLGQAEEVVQERICDD 310
Cdd:cd03340 279 KSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGSIQTTVSNITDD------VLGTCGLFEERQVGGE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 311 ELILIKN-TKARTsASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAI 389
Cdd:cd03340 353 RYNIFTGcPKAKT-CTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVI 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 390 AEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVnperknlKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFAT 469
Cdd:cd03340 432 NAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGG-------KWYGVDINNEGIADNFEAFVWEPSLVKINALTAAT 504
|
490
....*....|....*....
gi 595582154 470 EAAITILRIDDLIKLhPES 488
Cdd:cd03340 505 EAACLILSVDETIKN-PKS 522
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
4-484 |
3.92e-112 |
|
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: 342.12 E-value: 3.92e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 4 TITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYI 83
Cdd:TIGR02345 55 TISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 84 NENLIINTDELG--RDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVKYTDARgqprypVNSVNILKAHGRSQIESML 161
Cdd:TIGR02345 135 KEIAVTIDEEKGeqRELLEKCAATALSSKLISHNKEFFSKMIVDAVLSLDRDDLD------LKLIGIKKVQGGALEDSQL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 162 INGYALN---CVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVIL 238
Cdd:TIGR02345 209 VNGVAFKktfSYAGFEQQPKKFANPKILLLNVELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 239 TTGGIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEetfevtMLGQAEEVVQERICDDELILIKNT 318
Cdd:TIGR02345 289 SKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTTSDLEAD------VLGTCALFEERQIGSERYNYFTGC 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 319 KARTSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLV 398
Cdd:TIGR02345 363 PHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEI 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 399 IPNTLAVNAAQDSTDLVAKLRAFHNeaqvnperKNLKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRI 478
Cdd:TIGR02345 443 IPRQLCENAGFDSIEILNKLRSRHA--------KGGKWYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSV 514
|
....*.
gi 595582154 479 DDLIKL 484
Cdd:TIGR02345 515 DETITN 520
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
3-486 |
1.03e-108 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 333.53 E-value: 1.03e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 3 VTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRY 82
Cdd:PTZ00212 63 VTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 83 INENLIINT--DELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVKytdargqPRYPVNSVNILKAHGRSQIESM 160
Cdd:PTZ00212 143 LEEIAFDHGsdEEKFKEDLLNIARTTLSSKLLTVEKDHFAKLAVDAVLRLK-------GSGNLDYIQIIKKPGGTLRDSY 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 161 LINGYALNCVVGSqGMPKRIVNAKIACLDFSLQKTKMKL-GVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILT 239
Cdd:PTZ00212 216 LEDGFILEKKIGV-GQPKRLENCKILVANTPMDTDKIKIyGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFIN 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 240 TGGIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLanlegeETFEVTMLGQAEEVVQERICDDELILIKNTK 319
Cdd:PTZ00212 295 RQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEIVSTF------DTPEKVKLGHCDLIEEIMIGEDKLIRFSGCA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 320 ARTSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVI 399
Cdd:PTZ00212 369 KGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 400 PNTLAVNAAQDSTDLVAKLRAFHNEAQVNperknlkwIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRID 479
Cdd:PTZ00212 449 PTIIADNGGYDSAELVSKLRAEHYKGNKT--------AGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVD 520
|
....*..
gi 595582154 480 DLIKLHP 486
Cdd:PTZ00212 521 DIIRCAP 527
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
2-486 |
5.76e-108 |
|
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: 331.22 E-value: 5.76e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 2 DVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVR 81
Cdd:cd03336 50 GVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAARE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 82 YINENLIINTD--ELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVKytdargqPRYPVNSVNILKAHGRSQIES 159
Cdd:cd03336 130 ALLSSAVDHSSdeEAFREDLLNIARTTLSSKILTQDKEHFAELAVDAVLRLK-------GSGNLDAIQIIKKLGGSLKDS 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 160 MLINGYALNCVVGSqGMPKRIVNAKIACLDFSLQKTKMKL-GVQVVITDPEKLDQIRQRESDITKERIQKILATGANVIL 238
Cdd:cd03336 203 YLDEGFLLDKKIGV-NQPKRIENAKILIANTPMDTDKIKIfGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 239 TTGGIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLegeetfEVTMLGQAEEVVQERICDDELILIKNT 318
Cdd:cd03336 282 NRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTGGEIASTFDHP------ELVKLGTCKLIEEIMIGEDKLIRFSGV 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 319 KARTSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLV 398
Cdd:cd03336 356 AAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQ 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 399 IPNTLAVNAAQDSTDLVAKLRAFHNeaqvnperKNLKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRI 478
Cdd:cd03336 436 LPTIIADNAGYDSAELVAQLRAAHY--------NGNTTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRV 507
|
....*...
gi 595582154 479 DDLIKLHP 486
Cdd:cd03336 508 DDIIKCAP 515
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
2-482 |
1.55e-105 |
|
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: 324.62 E-value: 1.55e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 2 DVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVR 81
Cdd:cd03338 43 EVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 82 YINEnLIINTDELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVkyTDARGQPRYPVNSVNILKAHGRSQIESML 161
Cdd:cd03338 123 ILDS-MSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKV--IDPATATNVDLKDIRIVKKLGGTIEDTEL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 162 INGYALNC-VVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTT 240
Cdd:cd03338 200 VDGLVFTQkASKKAGGPTRIEKAKIGLIQFCLSPPKTDMDNNIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQ 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 241 GGI-----DDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGAsilSTLANLEGeetFEVTMLGQAEEVVQERICDDELILI 315
Cdd:cd03338 280 KSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTIGC---KPVASIDH---FTEDKLGSADLVEEVSLGDGKIVKI 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 316 KNTK-ARTSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFAR 394
Cdd:cd03338 354 TGVKnPGKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGAPEIEIALQLSEWARTLTGVEQYCVRAFAD 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 395 SLLVIPNTLAVNAAQDSTDLVAKLRAFHneAQVNperknlKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAIT 474
Cdd:cd03338 434 ALEVIPYTLAENAGLNPISIVTELRNRH--AQGE------KNAGINVRKGAITNILEENVVQPLLVSTSAITLATETVRM 505
|
....*...
gi 595582154 475 ILRIDDLI 482
Cdd:cd03338 506 ILKIDDIV 513
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
2-483 |
1.05e-100 |
|
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: 312.70 E-value: 1.05e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 2 DVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVR 81
Cdd:cd03339 58 EVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 82 YINE-NLIINTDELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVKYTDargqpRYPVN--SVNILKAHGRSQIE 158
Cdd:cd03339 138 HLEEiADKIEFSPDNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAVLSVADLE-----RKDVNfeLIKVEGKVGGRLED 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 159 SMLINGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVIL 238
Cdd:cd03339 213 TKLVKGIVIDKDFSHPQMPKEVKDAKIAILTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVI 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 239 TTGGIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEEtfevtmLGQAeEVVQER---ICDDELILI 315
Cdd:cd03339 293 CQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFEDLSPEK------LGKA-GLVREIsfgTTKDKMLVI 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 316 ---KNTKARTsasIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEF 392
Cdd:cd03339 366 egcPNSKAVT---IFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAF 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 393 ARSLLVIPNTLAVNAAQDSTDLVAKLRAfhneAQVNPERKNLkwiGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAA 472
Cdd:cd03339 443 ADALESIPLALAENSGLNPIETLSEVKA----RQVKEKNPHL---GIDCLGRGTNDMKEQKVFETLISKKQQILLATQVV 515
|
490
....*....|.
gi 595582154 473 ITILRIDDLIK 483
Cdd:cd03339 516 KMILKIDDVIV 526
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
2-483 |
6.24e-98 |
|
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: 305.57 E-value: 6.24e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 2 DVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVR 81
Cdd:TIGR02343 62 DITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 82 YINE-NLIINTDELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVKYTDargqpRYPVNS--VNILKAHGRSQIE 158
Cdd:TIGR02343 142 HLEEiSDEISADNNNREPLIQAAKTSLGSKIVSKCHRRFAEIAVDAVLNVADME-----RRDVDFdlIKVEGKVGGSLED 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 159 SMLINGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVIL 238
Cdd:TIGR02343 217 TKLIKGIIIDKDFSHPQMPKEVEDAKIAILTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 239 TTGGIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEEtfevtmLGQAEEVVQERI--CDDELILIK 316
Cdd:TIGR02343 297 CQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPRFQELSKDK------LGKAGLVREISFgtTKDRMLVIE 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 317 NTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSL 396
Cdd:TIGR02343 371 QCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADAL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 397 LVIPNTLAVNAAQDSTDLVAKLRAFHNEaQVNPErknlkwIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITIL 476
Cdd:TIGR02343 451 ETIPMALAENSGLDPIGTLSTLKSLQLK-EKNPN------LGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMIL 523
|
....*..
gi 595582154 477 RIDDLIK 483
Cdd:TIGR02343 524 KIDDVIS 530
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
2-482 |
7.86e-93 |
|
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: 292.07 E-value: 7.86e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 2 DVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVR 81
Cdd:TIGR02342 44 EVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 82 YINEnLIINTDELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVkyTDARGQPRYPVNSVNILKAHGRSQIESML 161
Cdd:TIGR02342 124 ILDE-MSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPLAVDAVLKV--IDPENAKNVDLNDIKVVKKLGGTIDDTEL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 162 INGYAL-NCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTT 240
Cdd:TIGR02342 201 IEGLVFtQKASKSAGGPTRIEKAKIGLIQFQISPPKTDMENQIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 241 GGI-----DDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLanlegeETFEVTMLGQAEEVvqERICDDELILI 315
Cdd:TIGR02342 281 KSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASI------DHFTADKLGSAELV--EEVDSDGGKII 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 316 KNT---KARTSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEF 392
Cdd:TIGR02342 353 KITgiqNAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPEIEIARRLSKYARTMKGVESYCVRAF 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 393 ARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQvnperknlKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAA 472
Cdd:TIGR02342 433 ADALEVIPYTLAENAGLNPIKVVTELRNRHANGE--------KTAGISVRKGGITNMLEEHVLQPLLVTTSAITLASETV 504
|
490
....*....|
gi 595582154 473 ITILRIDDLI 482
Cdd:TIGR02342 505 RSILKIDDIV 514
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
2-492 |
1.03e-88 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 280.43 E-value: 1.03e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 2 DVTITNDGATILKLLEVEHP----AAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACK 77
Cdd:COG0459 45 DPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 78 EAVRYINENLI-INTDELgrdcLINAAKTSMSSKiigingDYFANMVVDAVLAVkytdarGQprypvNSVNILKAHGRSQ 156
Cdd:COG0459 125 KAVEELKKIAKpVDDKEE----LAQVATISANGD------EEIGELIAEAMEKV------GK-----DGVITVEEGKGLE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 157 IESMLINGYALN-------CVVGSQGMPKRIVNAKIAcldfslqktkmklgvqvvITDpEKLDQIRQResditKERIQKI 229
Cdd:COG0459 184 TELEVVEGMQFDkgylspyFVTDPEKMPAELENAYIL------------------LTD-KKISSIQDL-----LPLLEKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 230 LATGANVILTTGGIDDMYLKYFVEAGAMAVRRVL-----------KRDLKHVAKASGASILSTLANLEGEETfEVTMLGQ 298
Cdd:COG0459 240 AQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVavkapgfgdrrKAMLEDIAILTGGRVISEDLGLKLEDV-TLDDLGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 299 AEEVVQEricDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLElKSVVPGGGAVEAALSIYLENYA 378
Cdd:COG0459 319 AKRVEVD---KDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALHATRAAVE-EGIVPGGGAALLRAARALRELA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 379 TSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAfhneaqvnperKNLKWIGLDLVHGKPRDNKQAGVFEPT 458
Cdd:COG0459 395 AKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRA-----------AKDKGFGFDAATGEYVDMLEAGVIDPA 463
|
490 500 510
....*....|....*....|....*....|....
gi 595582154 459 IVKVKSLKFATEAAITILRIDDLIKLHPESKDDK 492
Cdd:COG0459 464 KVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
2-489 |
1.46e-87 |
|
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: 278.28 E-value: 1.46e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 2 DVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVR 81
Cdd:TIGR02341 51 SIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 82 YINENLIINTDELG--RDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVKYTDArgqprypVNSVNILKAHGRSQIES 159
Cdd:TIGR02341 131 ALLKSAVDNGSDEVkfRQDLMNIARTTLSSKILSQHKDHFAQLAVDAVLRLKGSGN-------LEAIQIIKKLGGSLADS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 160 MLINGYALNCVVGSQgMPKRIVNAKIACLDFSLQKTKMKL-GVQVVITDPEKLDQIRQRESDITKERIQKILATGANVIL 238
Cdd:TIGR02341 204 YLDEGFLLDKKIGVN-QPKRIENAKILIANTGMDTDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 239 TTGGIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLanlegeETFEVTMLGQAEEVVQERICDDELILIKNT 318
Cdd:TIGR02341 283 NRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIVSTF------DHPELVKLGSCDLIEEIMIGEDKLLKFSGV 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 319 KARTSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLV 398
Cdd:TIGR02341 357 KLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQ 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 399 IPNTLAVNAAQDSTDLVAKLRAFHNEAQVNperknlkwIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRI 478
Cdd:TIGR02341 437 LPTIIADNAGFDSAELVAQLRAAHYNGNTT--------MGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRV 508
|
490
....*....|.
gi 595582154 479 DDLIKLHPESK 489
Cdd:TIGR02341 509 DNIIKAAPRKR 519
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
3-482 |
3.36e-87 |
|
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: 276.10 E-value: 3.36e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 3 VTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRY 82
Cdd:cd03337 52 IVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 83 InENLIINTDELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVKYTDARGQP-----RYpvnsVNILKAHGRSQI 157
Cdd:cd03337 132 L-EEISIPVDVNDRAQMLKIIKSCIGTKFVSRWSDLMCNLALDAVKTVAVEENGRKKeidikRY----AKVEKIPGGEIE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 158 ESMLINGYALNCVVGSQGMPKRIVNAKIACLDFSLQktkmklgvQVVITdpEKldqirqresditkeriqkilatganvi 237
Cdd:cd03337 207 DSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPLE--------YLVIT--EK--------------------------- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 238 lttgGIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEEtfeVTMLGQAEEVvqeRICDDE----LI 313
Cdd:cd03337 250 ----GVSDLAQHYLVKAGITALRRVRKTDNNRIARACGATIVNRPEELTESD---VGTGAGLFEV---KKIGDEyftfIT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 314 LIKNTKArtsASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFA 393
Cdd:cd03337 320 ECKDPKA---CTILLRGASKDVLNEVERNLQDAMAVARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 394 RSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQvnperkNLKWiGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAI 473
Cdd:cd03337 397 SALEVIPRTLAQNCGANVIRTLTELRAKHAQGE------NSTW-GIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAAC 469
|
....*....
gi 595582154 474 TILRIDDLI 482
Cdd:cd03337 470 MLLRIDDIV 478
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
3-482 |
5.25e-87 |
|
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: 277.00 E-value: 5.25e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 3 VTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRY 82
Cdd:TIGR02344 52 IVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 83 INEnLIINTDELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVKYTdarGQPRYPVN---SVNILKAHGRSQIES 159
Cdd:TIGR02344 132 LEE-ISIPVDVNDDAAMLKLIQSCIGTKFVSRWSDLMCDLALDAVRTVQRD---ENGRKEIDikrYAKVEKIPGGDIEDS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 160 MLINGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILT 239
Cdd:TIGR02344 208 CVLKGVMINKDVTHPKMRRYIENPRIVLLDCPLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVIT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 240 TGGIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEET------FEVTMLGqaeevvqericDDELI 313
Cdd:TIGR02344 288 EKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACGATIVNRPEELRESDVgtgcglFEVKKIG-----------DEYFT 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 314 LIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFA 393
Cdd:TIGR02344 357 FITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVA 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 394 RSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAqvnperkNLKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAI 473
Cdd:TIGR02344 437 DALEIIPRTLAQNCGANVIRTLTELRAKHAQE-------NNCTWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESAC 509
|
....*....
gi 595582154 474 TILRIDDLI 482
Cdd:TIGR02344 510 LLLRIDDIV 518
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
4-482 |
2.96e-82 |
|
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: 262.93 E-value: 2.96e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 4 TITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRyI 83
Cdd:cd03341 45 FVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGELLEKAEELLRMGLHPSEIIEGYEKALKKALE-I 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 84 NENLIINTDELGRDC--LINAAKTSMSSKIIGiNGDYFANMVVDAVLAVKYTDARgqpRYPVNSVNILKAHGRSQIESML 161
Cdd:cd03341 124 LEELVVYKIEDLRNKeeVSKALKTAIASKQYG-NEDFLSPLVAEACISVLPENIG---NFNVDNIRVVKILGGSLEDSKV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 162 INGYALNcvVGSQGMPKRIVNAKIAcldfslqktkmklgvqvVITDPekldqirqresditkeriqkiLATGANVILTTG 241
Cdd:cd03341 200 VRGMVFK--REPEGSVKRVKKAKVA-----------------VFSCP---------------------FDIGVNVIVAGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 242 GIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEEtfevtmLGQAEEVVQERICDDELILIKNTKAR 321
Cdd:cd03341 240 SVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEE------IGYCDSVYVEEIGDTKVVVFRQNKED 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 322 TS-ASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIP 400
Cdd:cd03341 314 SKiATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 401 NTLAVNAAQDSTDLVAKLRAFHNEAQVNperknlkwIGLDLVHGKP--RDNKQAGVFEPTIVKVKSLKFATEAAITILRI 478
Cdd:cd03341 394 RTLAENAGLDATEVLSELYAAHQKGNKS--------AGVDIESGDEgtKDAKEAGIFDHLATKKWAIKLATEAAVTVLRV 465
|
....
gi 595582154 479 DDLI 482
Cdd:cd03341 466 DQII 469
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
5-486 |
8.74e-82 |
|
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: 263.50 E-value: 8.74e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 5 ITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYIN 84
Cdd:TIGR02346 56 VTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 85 ENLIINTDEL-GRDCLINAAKTSMSSKIIGiNGDYFANMVVDAVLAVKYTDargQPRYPVNSVNILKAHGRSQIESMLIN 163
Cdd:TIGR02346 136 ELVVWEVKDLrDKDELIKALKASISSKQYG-NEDFLAQLVAQACSTVLPKN---PQNFNVDNIRVCKILGGSLSNSEVLK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 164 GYALNcvVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGI 243
Cdd:TIGR02346 212 GMVFN--REAEGSVKSVKNAKVAVFSCPLDTATTETKGTVLIHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSV 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 244 DDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEEtfevtmLGQAEEVVQERICDDELILIKNTKARTS 323
Cdd:TIGR02346 290 GDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPEE------IGYVDSVYVSEIGGDKVTVFKQENGDSK 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 324 -ASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNT 402
Cdd:TIGR02346 364 iSTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRT 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 403 LAVNAAQDSTDLVAKLRAFHNeaqvnperKNLKWIGLDLVHGKPR--DNKQAGVFEPTIVKVKSLKFATEAAITILRIDD 480
Cdd:TIGR02346 444 LAENAGLNANEVIPKLYAAHK--------KGNKSKGIDIEAESDGvkDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQ 515
|
....*.
gi 595582154 481 LIKLHP 486
Cdd:TIGR02346 516 IIMAKP 521
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
2-483 |
9.53e-73 |
|
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: 240.02 E-value: 9.53e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 2 DVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVR 81
Cdd:TIGR02347 51 DIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 82 YINENLIINTDELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVKytdaRGQPRYPVNSVNILKAHGRSQIESML 161
Cdd:TIGR02347 131 FLDKFKVKKEDEVDREFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIK----KDGEDIDLFMVEIMEMKHKSATDTTL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 162 INGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKIL-------ATGA 234
Cdd:TIGR02347 207 IRGLVLDHGARHPDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIelkkkvcGKSP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 235 N---VILTTGGIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEEtfevtmLGQAEEVVQERICDDE 311
Cdd:TIGR02347 287 DkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEALNSVEDLTPEC------LGWAGLVYETTIGEEK 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 312 LILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAE 391
Cdd:TIGR02347 361 YTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEA 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 392 FARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQvnperknlKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEA 471
Cdd:TIGR02347 441 FANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGG--------EVVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVI 512
|
490
....*....|..
gi 595582154 472 AITILRIDDLIK 483
Cdd:TIGR02347 513 ASQLLLVDEVMR 524
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
2-483 |
1.61e-69 |
|
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: 230.22 E-value: 1.61e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 2 DVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVR 81
Cdd:cd03342 47 DIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 82 YINENLIINTDELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVKytdargQPRYPV--NSVNILKAHGRSQIES 159
Cdd:cd03342 127 FLESFKVPVEIDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIY------KPDEPIdlHMVEIMQMQHKSDSDT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 160 MLINGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKmklgvqvvitdpekldqirqreSDITKERIQKilatganVILT 239
Cdd:cd03342 201 KLIRGLVLDHGARHPDMPKRVENAYILTCNVSLEYEK----------------------TEVNSGFFYS-------VVIN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 240 TGGIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEEtfevtmLGQAEEVVQERICDDELILIKNTK 319
Cdd:cd03342 252 QKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPEC------LGYAGLVYERTLGEEKYTFIEGVK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 320 ARTSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVI 399
Cdd:cd03342 326 NPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 400 PNTLAVNAAQDSTDLVAKLRAFHNEAQVNPerknlkwiGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRID 479
Cdd:cd03342 406 PKTLAENSGLDVQETLVKLQDEYAEGGQVG--------GVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASQLLLVD 477
|
....
gi 595582154 480 DLIK 483
Cdd:cd03342 478 EIIR 481
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
96-355 |
2.14e-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: 205.39 E-value: 2.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 96 RDCLINAAKTSMSSKIIGiNGDYFANMVVDAVLAVKYTDargqPRYPVNSVNILKAHGRSQIESMLINGYALNCVVGSQG 175
Cdd:cd03333 1 RELLLQVATTSLNSKLSS-WDDFLGKLVVDAVLKVGPDN----RMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 176 MPKRIVNAKIACLDFSLQktkmklgvqvvitdpekldqirqresditkeriqkilatgaNVILTTGGIDDMYLKYFVEAG 255
Cdd:cd03333 76 MPKRLENAKILLLDCPLE-----------------------------------------YVVIAEKGIDDLALHYLAKAG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 256 AMAVRRVLKRDLKHVAKASGASILSTLANLEGEetfevtMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFM 335
Cdd:cd03333 115 IMAVRRVKKEDLERIARATGATIVSSLEDLTPE------DLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVE 188
|
250 260
....*....|....*....|
gi 595582154 336 CDEMERSLHDALCVVKRVLE 355
Cdd:cd03333 189 LDEVKRSLHDALCAVRAAVE 208
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
146-375 |
2.38e-12 |
|
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: 67.25 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 146 VNILKAHGRSQIESMLINGYALNCVVGSQGMPKRIVNAKIACLDFSLqktkmklGVQVVITDPEKLDQIRQRESDITKER 225
Cdd:cd03334 50 VKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPL-------EYQRVENKLLSLDPVILQEKEYLKNL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 226 IQKILATGANVILTTGGIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEetfevTMLGQAEEVVQE 305
Cdd:cd03334 123 VSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDLLTS-----PKLGTCESFRVR 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 595582154 306 RICDDE-----LILIKNTKARTSASIILRGANdfmcdemerslHDALCVVKRVLELksvvpgggAVEAALSIYLE 375
Cdd:cd03334 198 TYVEEHgrsktLMFFEGCPKELGCTILLRGGD-----------LEELKKVKRVVEF--------MVFAAYHLKLE 253
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
4-86 |
4.27e-05 |
|
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: 45.91 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 4 TITNDGATILKLLEVEHP----AAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEA 79
Cdd:cd03344 45 KITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAV 124
|
....*..
gi 595582154 80 VRYINEN 86
Cdd:cd03344 125 VEELKKL 131
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
5-85 |
1.64e-04 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 44.13 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 5 ITNDGATILKLLEVEHPA----AKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAV 80
Cdd:PTZ00114 60 ITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVL 139
|
....*
gi 595582154 81 RYINE 85
Cdd:PTZ00114 140 ESLKE 144
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
4-86 |
1.74e-04 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 43.94 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 4 TITNDGATILKLLEVEHP----AAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEA 79
Cdd:PRK12850 48 RITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAV 127
|
....*..
gi 595582154 80 VRYINEN 86
Cdd:PRK12850 128 VDELKKI 134
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
4-81 |
4.58e-03 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 39.72 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582154 4 TITNDGATILKLLEVEHP----AAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEA 79
Cdd:PRK12851 48 TITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAV 127
|
..
gi 595582154 80 VR 81
Cdd:PRK12851 128 VE 129
|
|
| |
