|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
11-527 |
0e+00 |
|
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: 1005.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 11 IFKAGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDAALMVTNDGATILKNIGVDNPAAKVLVDMSRV 90
Cdd:cd03336 1 ILKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILQSVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 91 QDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAVDHGSDEARFWQDLMNIAGTTLSSK 170
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEAFREDLLNIARTTLSSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 171 LLTHHKDHFTKLAVEAVLRLKGSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIK 250
Cdd:cd03336 161 ILTQDKEHFAELAVDAVLRLKGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQPKRIENAKILIANTPMDTDKIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 251 IFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGE 330
Cdd:cd03336 241 IFGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTGGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 331 IASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDPRTVYGG 410
Cdd:cd03336 321 IASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRVVLGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 411 GCSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHITAGLDMKEGTIGDMAV 490
Cdd:cd03336 401 GCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTVGDMKE 480
|
490 500 510
....*....|....*....|....*....|....*..
gi 1302188017 491 LGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRK 527
Cdd:cd03336 481 LGITESFKVKRQVLLSASEAAEMILRVDDIIKCAPRK 517
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
5-530 |
0e+00 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 926.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 5 SLAPVNIFKAGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSG---RDAALMVTNDGATILKNIGVDNPAA 81
Cdd:PTZ00212 4 ANVPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMSegpRSGNVTVTNDGATILKSVWLDNPAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 82 KVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAVDHGSDEARFWQDLMN 161
Cdd:PTZ00212 84 KILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEKFKEDLLN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 162 IAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIAN 241
Cdd:PTZ00212 164 IARTTLSSKLLTVEKDHFAKLAVDAVLRLKGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVGQPKRLENCKILVAN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 242 TGMDTDKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVE 321
Cdd:PTZ00212 244 TPMDTDKIKIYGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGME 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 322 RLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTV 401
Cdd:PTZ00212 324 RLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 402 KDPRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHITAGLDMK 481
Cdd:PTZ00212 404 KDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGIDME 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1302188017 482 EGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKRVP 530
Cdd:PTZ00212 484 KGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRCAPRQREQ 532
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
10-528 |
0e+00 |
|
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: 906.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 10 NIFKAGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDAALMVTNDGATILKNIGVDNPAAKVLVDMSR 89
Cdd:TIGR02341 1 QIFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 90 VQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAVDHGSDEARFWQDLMNIAGTTLSS 169
Cdd:TIGR02341 81 VQDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVKFRQDLMNIARTTLSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 170 KLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKI 249
Cdd:TIGR02341 161 KILSQHKDHFAQLAVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 250 KIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGG 329
Cdd:TIGR02341 241 KIFGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 330 EIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDPRTVYG 409
Cdd:TIGR02341 321 EIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 410 GGCSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHITAGLDMKEGTIGDMA 489
Cdd:TIGR02341 401 GGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGTIADMR 480
|
490 500 510
....*....|....*....|....*....|....*....
gi 1302188017 490 VLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKR 528
Cdd:TIGR02341 481 QLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPRKR 519
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
16-522 |
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: 541.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 16 ADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDaaLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEV 95
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGD--PTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 96 GDGTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAVDHgsdEARFWQDLMNIAGTTLSSKLLTHH 175
Cdd:cd00309 79 GDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPI---DVEDREELLKVATTSLNSKLVSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 176 KDHFTKLAVEAVLRLKGSG---NLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTdkiki 251
Cdd:cd00309 156 DDFLGELVVDAVLKVGKENgdvDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYmPKRLENAKILLLDCKLEY----- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 252 fgsrvrvdstakvaeiehaekekmkekverilkhginCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEI 331
Cdd:cd00309 231 -------------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 332 ASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDPRTVYGGG 411
Cdd:cd00309 274 VSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 412 CSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHITAGLDMKEGTIGDMAVL 491
Cdd:cd00309 354 AAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKEA 433
|
490 500 510
....*....|....*....|....*....|.
gi 1302188017 492 GITESFQVKRQVLLSAAEAAEVILRVDNIIK 522
Cdd:cd00309 434 GIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
35-523 |
4.66e-175 |
|
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: 502.50 E-value: 4.66e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 35 IGDLVKSTLGPKGMDKILLSSGRDaaLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAE 114
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGD--VTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 115 SLIAKKIHPQTIISGWREATKAAREALLSsaVDHGSDEARFWQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLK--- 191
Cdd:pfam00118 79 KLLAAGVHPTTIIEGYEKALEKALEILDS--IISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 192 GSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKI-GVNQPKRIENAKILIANTGMDTDKIKIFGSrVRVDSTAKVAEIEHA 270
Cdd:pfam00118 157 GSFDLGNIGVVKILGGSLEDSELVDGVVLDKGPlHPDMPKRLENAKVLLLNCSLEYEKTETKAT-VVLSDAEQLERFLKA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 271 EKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIE 350
Cdd:pfam00118 236 EEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 351 EVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDPRTVYGGGCSEMLMAHAVTQLANRTPG 430
Cdd:pfam00118 316 EEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 431 KEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHITAGLDMKEGTIGDMAVLGITESFQVKRQVLLSAAEA 510
Cdd:pfam00118 396 KEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEA 475
|
490
....*....|...
gi 1302188017 511 AEVILRVDNIIKA 523
Cdd:pfam00118 476 ASTILRIDDIIKA 488
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
9-524 |
4.81e-130 |
|
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: 388.93 E-value: 4.81e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 9 VNIFKAGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDaaLMVTNDGATILKNIGVDNPAAKVLVDMS 88
Cdd:cd03343 1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGD--VTITNDGATILKEMDIEHPAAKMLVEVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 89 RVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAVDHGSDEARFwqdLMNIAGTTLS 168
Cdd:cd03343 79 KTQDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDT---LRKIAKTSLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 169 SKLLTHHKDHFTKLAVEAVLRL--KGSG----NLEAIHVIKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIAN 241
Cdd:cd03343 156 GKGAEAAKDKLADLVVDAVLQVaeKRDGkyvvDLDNIKIEKKTGGSVDDTELIRGIVIDKeVVHPGMPKRVENAKIALLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 242 TGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVE 321
Cdd:cd03343 236 APLEVKKTEI-DAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDME 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 322 RLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTV 401
Cdd:cd03343 315 KLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADAL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 402 KDPRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHITAGLDMK 481
Cdd:cd03343 395 EDGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVY 474
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1302188017 482 EGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAA 524
Cdd:cd03343 475 TGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
8-524 |
5.45e-130 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 388.86 E-value: 5.45e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 8 PVNIFKAGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDaaLMVTNDGATILKNIGVDNPAAKVLVDM 87
Cdd:NF041082 2 PILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGD--VVITNDGVTILKEMDIEHPAAKMIVEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 88 SRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAVDHGSDEARFwqdLMNIAGTTL 167
Cdd:NF041082 80 AKTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKET---LKKIAATAM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 168 SSKLLTHHKDHFTKLAVEAVLRL---KGSGN--LEAIHVIKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIAN 241
Cdd:NF041082 157 TGKGAEAAKDKLADLVVDAVKAVaekDGGYNvdLDNIKVEKKVGGSIEDSELVEGVVIDKeRVHPGMPKRVENAKIALLD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 242 TGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVE 321
Cdd:NF041082 237 APLEVKKTEI-DAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDME 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 322 RLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTV 401
Cdd:NF041082 316 KLAKATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 402 KDPRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHITAGLDMK 481
Cdd:NF041082 396 EDGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVY 475
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1302188017 482 EGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAA 524
Cdd:NF041082 476 TGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
7-524 |
1.08e-126 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 380.45 E-value: 1.08e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 7 APVNIFKAGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDaaLMVTNDGATILKNIGVDNPAAKVLVD 86
Cdd:NF041083 1 QPVLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGD--IVITNDGATILKEMDVQHPAAKMLVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 87 MSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAVDHGSDEARFwqdLMNIAGTT 166
Cdd:NF041083 79 VAKTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRET---LKKIAETS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 167 LSSKLLTHHKDHFTKLAVEAVLRL------KGSGNLEAIHVIKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILI 239
Cdd:NF041083 156 LTSKGVEEARDYLAEIAVKAVKQVaekrdgKYYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKeVVHPGMPKRVENAKIAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 240 ANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAG 319
Cdd:NF041083 236 LDAPLEVKKTEI-DAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 320 VERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQ 399
Cdd:NF041083 315 MEKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVAD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 400 TVKDPRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHITAGLD 479
Cdd:NF041083 395 AVEDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGIN 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1302188017 480 MKEGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAA 524
Cdd:NF041083 475 VFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
8-523 |
4.84e-123 |
|
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: 370.94 E-value: 4.84e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 8 PVNIFKAGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDaaLMVTNDGATILKNIGVDNPAAKVLVDM 87
Cdd:TIGR02339 1 PVFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGD--VTITNDGATILKEMDIEHPAAKMLVEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 88 SRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAVDHGSDEARFwqdLMNIAGTTL 167
Cdd:TIGR02339 79 AKTQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDL---LKKIAYTSL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 168 SSKLLT-HHKDHFTKLAVEAVLRL-------KGSGNLEAIHVIKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKIL 238
Cdd:TIGR02339 156 TSKASAeVAKDKLADLVVEAVKQVaelrgdgKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKeVVHPGMPKRVENAKIA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 239 IANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFA 318
Cdd:TIGR02339 236 LLDAPLEVEKTEI-DAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 319 GVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLA 398
Cdd:TIGR02339 315 DIEKLARATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 399 QTVKDPRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHITAGL 478
Cdd:TIGR02339 395 NALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGI 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1302188017 479 DMKEGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKA 523
Cdd:TIGR02339 475 NVFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
8-523 |
1.30e-120 |
|
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: 364.69 E-value: 1.30e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 8 PVNIFKAGADEERAeTARLSSFIGA-IAIGDLVKSTLGPKGMDKILLSSGRDAalMVTNDGATILKNIGVDNPAAKVLVD 86
Cdd:cd03340 1 PIILLKEGTDTSQG-KGQLISNINAcQAIADAVRTTLGPRGMDKLIVDGRGKV--TISNDGATILKLLDIVHPAAKTLVD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 87 MSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAVD-HGSDEARFWQDLMNIAGT 165
Cdd:cd03340 78 IAKSQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNiDKEDKEEQRELLEKCAAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 166 TLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKIGV----NQPKRIENAKILIAN 241
Cdd:cd03340 158 ALNSKLIASEKEFFAKMVVDAVLSLDDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYagfeQQPKKFKNPKILLLN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 242 TGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMA---IEHADFa 318
Cdd:cd03340 238 VELELKAEKD-NAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCagrVPEEDL- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 319 gvERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLA 398
Cdd:cd03340 316 --KRVAQATGGSIQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 399 QTVKDPRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHIT-AG 477
Cdd:cd03340 394 RAIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKwYG 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1302188017 478 LDMKEGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKA 523
Cdd:cd03340 474 VDINNEGIADNFEAFVWEPSLVKINALTAATEAACLILSVDETIKN 519
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
22-525 |
1.58e-114 |
|
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: 349.28 E-value: 1.58e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 22 ETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDaaLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTS 101
Cdd:cd03335 7 QDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGD--VTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 102 VTVLAAELLREAESLIAKKIHPQTIISGWR----EATKAAREALLSSAVDHGSDEarfwqdLMNIAGTTLSSKLLTHHKD 177
Cdd:cd03335 85 VVIIAAELLKRANELVKQKIHPTTIISGYRlackEAVKYIKEHLSISVDNLGKES------LINVAKTSMSSKIIGADSD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 178 HFTKLAVEAVLRLKGSGNL-------EAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTDKI 249
Cdd:cd03335 159 FFANMVVDAILAVKTTNEKgktkypiKAVNILKAHGKSAKESYLVNGYALNCTRASQGmPTRVKNAKIACLDFNLQKTKM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 250 KIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGG 329
Cdd:cd03335 239 KL-GVQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 330 EIASTFDHPE------LVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKD 403
Cdd:cd03335 318 TLVSTLANLEgeetfdPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLES 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 404 PRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHITA------- 476
Cdd:cd03335 398 NSVVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKPdkkhlkw 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1302188017 477 -GLDMKEGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAP 525
Cdd:cd03335 478 yGLDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIKLNP 527
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
8-523 |
3.52e-113 |
|
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: 345.59 E-value: 3.52e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 8 PVNIFKAGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDAalMVTNDGATILKNIGVDNPAAKVLVDM 87
Cdd:TIGR02345 3 TIVLLKEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKA--TISNDGATILKLLDIVHPAAKTLVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 88 SRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAVDHGSDEARFWQDLMNIAGTTL 167
Cdd:TIGR02345 81 AKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKGEQRELLEKCAATAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 168 SSKLLTHHKDHFTKLAVEAVLRLKGSG-NLEAIHVIKKLGGSLADSYLDEGFLLDKKIGV----NQPKRIENAKILIANT 242
Cdd:TIGR02345 161 SSKLISHNKEFFSKMIVDAVLSLDRDDlDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYagfeQQPKKFANPKILLLNV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 243 GMDTdKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVER 322
Cdd:TIGR02345 241 ELEL-KAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 323 LALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVK 402
Cdd:TIGR02345 320 VIKACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 403 DPRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHITAGLDMKE 482
Cdd:TIGR02345 400 NKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINT 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1302188017 483 GTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKA 523
Cdd:TIGR02345 480 EDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITN 520
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
15-527 |
8.53e-113 |
|
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: 345.17 E-value: 8.53e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 15 GADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDaaLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDE 94
Cdd:TIGR02340 4 GGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGD--VTITNDGATILKLLEVEHPAAKILVELAQLQDRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 95 VGDGTTSVTVLAAELLREAESLIAKKIHPQTIISGWR----EATKAAREALLSSAVDHGSDearfwqDLMNIAGTTLSSK 170
Cdd:TIGR02340 82 VGDGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRlackEAVKYIKENLSVSVDELGRE------ALINVAKTSMSSK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 171 LLTHHKDHFTKLAVEAVLRLKGSGN-------LEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANT 242
Cdd:TIGR02340 156 IIGLDSDFFSNIVVDAVLAVKTTNEngetkypIKAINILKAHGKSARESMLVKGYALNCTVASQQmPKRIKNAKIACLDF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 243 GMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVER 322
Cdd:TIGR02340 236 NLQKAKMAL-GVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 323 LALVTGGEIASTFDHPE------LVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCV 396
Cdd:TIGR02340 315 IAKATGATLVSTLADLEgeetfeASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 397 LAQTVKDPRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHITA 476
Cdd:TIGR02340 395 VKRTLESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAQLKP 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1302188017 477 --------GLDMKEGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRK 527
Cdd:TIGR02340 475 ekkhlkwyGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIKLNPEQ 533
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
8-522 |
2.97e-105 |
|
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: 325.41 E-value: 2.97e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 8 PVNIFKAGADEERAE--TARLSSFIGAIAIGDLVKSTLGPKGMDKILLSsgRDAALMVTNDGATILKNIGVDNPAAKVLV 85
Cdd:cd03339 6 PFIIVREQEKKKRLKglEAHKSHILAAKSVANILRTSLGPRGMDKILVS--PDGEVTVTNDGATILEKMDVDHQIAKLLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 86 DMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAvDHGSDEARFWQDLMNIAGT 165
Cdd:cd03339 84 ELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIA-DKIEFSPDNKEPLIQTAMT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 166 TLSSKLLTHHKDHFTKLAVEAVLRL----KGSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIA 240
Cdd:cd03339 163 SLGSKIVSRCHRQFAEIAVDAVLSVadleRKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQmPKEVKDAKIAIL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 241 NTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFI---------NRQLIYNypeqlfgaaGVMA 311
Cdd:cd03339 243 TCPFEPPKPKT-KHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVIcqwgfddeaNHLLLQN---------GLPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 312 IEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIG--EDKLIHFSGVALGEACTIVLRGATQQILDEAERS 389
Cdd:cd03339 313 VRWVGGVEIELIAIATGGRIVPRFEDLSPEKLGKAGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 390 LHDALCVLAQTVKDPRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAH 469
Cdd:cd03339 393 LHDALCVVRNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQ 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1302188017 470 -SEGHITAGLD-MKEGTiGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIK 522
Cdd:cd03339 473 vKEKNPHLGIDcLGRGT-NDMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
17-521 |
1.99e-104 |
|
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: 322.70 E-value: 1.99e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 17 DEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDaaLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVG 96
Cdd:cd03338 2 DKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGE--VIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 97 DGTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREAL--LSSAVDHGSDEarfwqDLMNIAGTTLSSKLLTH 174
Cdd:cd03338 80 DGTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILdsMSIPVDLNDRE-----SLIKSATTSLNSKVVSQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 175 HKDHFTKLAVEAVLRL-----KGSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKI--GVNQPKRIENAKILIAN------ 241
Cdd:cd03338 155 YSSLLAPIAVDAVLKVidpatATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKAskKAGGPTRIEKAKIGLIQfclspp 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 242 -TGMDtdkikifgSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCF-----INRQLIYNYPEQLFGAAGVMAIEHA 315
Cdd:cd03338 235 kTDMD--------NNIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLliqksILRDAVSDLALHFLAKLKIMVVKDI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 316 DFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVA-LGEACTIVLRGATQQILDEAERSLHDAL 394
Cdd:cd03338 307 EREEIEFICKTIGCKPVASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKnPGKTVTILVRGSNKLVLDEAERSLHDAL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 395 CVLAQTVKDPRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHI 474
Cdd:cd03338 387 CVIRCLVKKRALIPGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEK 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1302188017 475 TAGLDMKEGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNII 521
Cdd:cd03338 467 NAGINVRKGAITNILEENVVQPLLVSTSAITLATETVRMILKIDDIV 513
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
24-522 |
1.13e-97 |
|
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: 305.96 E-value: 1.13e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 24 ARLSSFIGAIAIGDLVKSTLGPKGMDKILLSsgRDAALMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVT 103
Cdd:TIGR02343 28 AKKSNIAAAKSVASILRTSLGPKGMDKMLIS--PDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 104 VLAAELLREAESLIAKKIHPQTIISGWREATKAAREALlSSAVDHGSDEARFWQDLMNIAGTTLSSKLLTHHKDHFTKLA 183
Cdd:TIGR02343 106 VLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHL-EEISDEISADNNNREPLIQAAKTSLGSKIVSKCHRRFAEIA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 184 VEAVLRL----KGSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTDKIKIfGSRVRV 258
Cdd:TIGR02343 185 VDAVLNVadmeRRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQmPKEVEDAKIAILTCPFEPPKPKT-KHKLDI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 259 DSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHP 338
Cdd:TIGR02343 264 SSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPRFQEL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 339 ELVKLGSCKLIEEVMIG--EDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDPRTVYGGGCSEML 416
Cdd:TIGR02343 344 SKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGGGAAEIS 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 417 MAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHITA-GLD-MKEGTiGDMAVLGIT 494
Cdd:TIGR02343 424 CSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNlGVDcLGYGT-NDMKEQFVF 502
|
490 500
....*....|....*....|....*...
gi 1302188017 495 ESFQVKRQVLLSAAEAAEVILRVDNIIK 522
Cdd:TIGR02343 503 ETLIGKKQQILLATQLVRMILKIDDVIS 530
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
8-521 |
6.90e-95 |
|
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: 296.90 E-value: 6.90e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 8 PVNIFKAGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGrdAALMVTNDGATILKNIGVDNPAAKVLVDM 87
Cdd:cd03337 1 PVLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPM--GGIVLTNDGNAILREIDVAHPAAKSMIEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 88 SRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREAL--LSSAVDHGSDEarfwqDLMNIAGT 165
Cdd:cd03337 79 SRTQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILeeISIPVDVNDRA-----QMLKIIKS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 166 TLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHV-IKK-------LGGSLADSYLDEGFLLDKKigVNQPK---RIEN 234
Cdd:cd03337 154 CIGTKFVSRWSDLMCNLALDAVKTVAVEENGRKKEIdIKRyakvekiPGGEIEDSRVLDGVMLNKD--VTHPKmrrRIEN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 235 AKILIantgmdtdkikifgsrvrVDSTakvaeIEHAEkekmkekverILKHGINcfinrQLIYNYpeqlFGAAGVMAIEH 314
Cdd:cd03337 232 PRIVL------------------LDCP-----LEYLV----------ITEKGVS-----DLAQHY----LVKAGITALRR 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 315 ADFAGVERLALVTGGEIASTFDHPELVKLG-SCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDA 393
Cdd:cd03337 270 VRKTDNNRIARACGATIVNRPEELTESDVGtGAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 394 LCVLAQTVKDPRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAH-SEG 472
Cdd:cd03337 350 MAVARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHaQGE 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1302188017 473 HITAGLDMKEGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNII 521
Cdd:cd03337 430 NSTWGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
17-524 |
4.58e-94 |
|
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: 296.31 E-value: 4.58e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 17 DEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDaaLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVG 96
Cdd:TIGR02342 3 DKDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGE--VIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 97 DGTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREAL--LSSAVDHGSDEArfwqdLMNIAGTTLSSKLLTH 174
Cdd:TIGR02342 81 DGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILdeMSIPVDLSDREQ-----LLKSATTSLSSKVVSQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 175 HKDHFTKLAVEAVLRLKGSG-----NLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQ--PKRIENAKILIANTGMDTD 247
Cdd:TIGR02342 156 YSSLLAPLAVDAVLKVIDPEnaknvDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAggPTRIEKAKIGLIQFQISPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 248 KIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCF-----INRQLIYNYPEQLFGAAGVMAIEHADFAGVER 322
Cdd:TIGR02342 236 KTDM-ENQIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLliqksILRDAVNDLALHFLAKMKIMVVKDIEREEIEF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 323 LALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVA-LGEACTIVLRGATQQILDEAERSLHDALCVLAQTV 401
Cdd:TIGR02342 315 ICKTIGCKPIASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQnAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 402 KDPRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHITAGLDMK 481
Cdd:TIGR02342 395 KKRGLIAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVR 474
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1302188017 482 EGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAA 524
Cdd:TIGR02342 475 KGGITNMLEEHVLQPLLVTTSAITLASETVRSILKIDDIVFTR 517
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
35-523 |
2.15e-88 |
|
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: 279.88 E-value: 2.15e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 35 IGDLVKSTLGPKGMDKILLSSGRDaaLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAE 114
Cdd:cd03341 20 LSQITRTSYGPNGMNKMVINHLEK--LFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGELLEKAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 115 SLIAKKIHPQTIISGWREATKAAREALLSSAVdHGSDEARFWQDLMNIAGTTLSSKLLtHHKDHFTKLAVEAVLRLK--- 191
Cdd:cd03341 98 ELLRMGLHPSEIIEGYEKALKKALEILEELVV-YKIEDLRNKEEVSKALKTAIASKQY-GNEDFLSPLVAEACISVLpen 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 192 -GSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKIgVNQPKRIENAKILIANTGMDtdkikiFGSRVRVdSTAKVAEIeha 270
Cdd:cd03341 176 iGNFNVDNIRVVKILGGSLEDSKVVRGMVFKREP-EGSVKRVKKAKVAVFSCPFD------IGVNVIV-AGGSVGDL--- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 271 ekekmkekveriLKHgincFINRqliynypeqlfgaAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIE 350
Cdd:cd03341 245 ------------ALH----YCNK-------------YGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEEIGYCDSVY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 351 EVMIGEDKLIHFSGV-ALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDPRTVYGGGCSEMLMAHAVTQLANRTP 429
Cdd:cd03341 296 VEEIGDTKVVVFRQNkEDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAKKLKEYGEKTP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 430 GKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHITAGLDMKEGTIG--DMAVLGITESFQVKRQVLLSA 507
Cdd:cd03341 376 GLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDEGtkDAKEAGIFDHLATKKWAIKLA 455
|
490
....*....|....*.
gi 1302188017 508 AEAAEVILRVDNIIKA 523
Cdd:cd03341 456 TEAAVTVLRVDQIIMA 471
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
8-527 |
3.98e-84 |
|
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: 270.46 E-value: 3.98e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 8 PVNIFKAGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLssgrDAA--LMVTNDGATILKNIGVDNPAAKVLV 85
Cdd:TIGR02344 1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLL----DPMggIVMTNDGNAILREIDVAHPAAKSMI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 86 DMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREAL--LSSAVDHGSDEarfwqDLMNIA 163
Cdd:TIGR02344 77 ELSRTQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLeeISIPVDVNDDA-----AMLKLI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 164 GTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHVIKKL-------GGSLADSYLDEGFLLDKKigVNQPK---RIE 233
Cdd:TIGR02344 152 QSCIGTKFVSRWSDLMCDLALDAVRTVQRDENGRKEIDIKRYakvekipGGDIEDSCVLKGVMINKD--VTHPKmrrYIE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 234 NAKILIANTGMDTDKIKifgSRVRVDST-----AKVAEIEHaekEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAG 308
Cdd:TIGR02344 230 NPRIVLLDCPLEYKKGE---SQTNIEITkeedwNRILQMEE---EYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKAN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 309 VMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGS-CKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAE 387
Cdd:TIGR02344 304 ITAIRRVRKTDNNRIARACGATIVNRPEELRESDVGTgCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 388 RSLHDALCVLAQTVKDPRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRA 467
Cdd:TIGR02344 384 RNLQDAMAVARNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRA 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1302188017 468 AHS-EGHITAGLDMKEGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRK 527
Cdd:TIGR02344 464 KHAqENNCTWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVSGVKKK 524
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
22-527 |
1.08e-83 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 268.48 E-value: 1.08e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 22 ETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSgrDAALMVTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGD 97
Cdd:COG0459 9 EDARRANIRGVKALADAVKVTLGPKGRNVMLVKS--FGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 98 GTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAVDHGSDEarfwqDLMNIAGTTLSSkllthhKD 177
Cdd:COG0459 87 GTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKE-----ELAQVATISANG------DE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 178 HFTKLAVEAVLRLKGSGNLeaihVIKKLGGSLADSYLDEGFLLDKKI--------GVNQPKRIENAKILIANtgmdtDKI 249
Cdd:COG0459 156 EIGELIAEAMEKVGKDGVI----TVEEGKGLETELEVVEGMQFDKGYlspyfvtdPEKMPAELENAYILLTD-----KKI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 250 KIFGSRVrvdstaKVAEiehaekekmkekveRILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHAdfAGV--------- 320
Cdd:COG0459 227 SSIQDLL------PLLE--------------KVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRV--VAVkapgfgdrr 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 321 ----ERLALVTGGEIAS-----TFDHPELVKLGSCKLIEevmIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLH 391
Cdd:COG0459 285 kamlEDIAILTGGRVISedlglKLEDVTLDDLGRAKRVE---VDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 392 DALCVLAQTVKDpRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSE 471
Cdd:COG0459 362 DALHATRAAVEE-GIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKDK 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1302188017 472 GHitaGLDMKEGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRK 527
Cdd:COG0459 441 GF---GFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEK 493
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
35-525 |
9.94e-77 |
|
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: 251.17 E-value: 9.94e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 35 IGDLVKSTLGPKGMDKILLSsgRDAALMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAE 114
Cdd:TIGR02346 30 LSQITRTSLGPNGMNKMVIN--HLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGELLNKAE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 115 SLIAKKIHPQTIISGWREATKAAREALLSSAVDHGSDEARFwQDLMNIAGTTLSSKLLtHHKDHFTKLAVEAVLRLK--- 191
Cdd:TIGR02346 108 ELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDLRDK-DELIKALKASISSKQY-GNEDFLAQLVAQACSTVLpkn 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 192 -GSGNLEAIHVIKKLGGSLADSYLDEGFLLdKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSrVRVDSTAKVAEIEHA 270
Cdd:TIGR02346 186 pQNFNVDNIRVCKILGGSLSNSEVLKGMVF-NREAEGSVKSVKNAKVAVFSCPLDTATTETKGT-VLIHNAEELLNYSKG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 271 EKEKMKEKVERILKHGINCFINRqliynypeqlfGAAGVMAIEHADFAGV-----------ERLALVTGGEIASTFDHPE 339
Cdd:TIGR02346 264 EENQIEAMIKAIADSGVNVIVTG-----------GSVGDMALHYLNKYNImvlkipskfelRRLCKTVGATPLPRLGAPT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 340 LVKLGSCKLIEEVMIGEDKLIHFSGV-ALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDPRTVYGGGCSEMLMA 418
Cdd:TIGR02346 333 PEEIGYVDSVYVSEIGGDKVTVFKQEnGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 419 HAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHITAGLDMKEGTIG--DMAVLGITES 496
Cdd:TIGR02346 413 SRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAESDGvkDASEAGIYDM 492
|
490 500
....*....|....*....|....*....
gi 1302188017 497 FQVKRQVLLSAAEAAEVILRVDNIIKAAP 525
Cdd:TIGR02346 493 LATKKWAIKLATEAAVTVLRVDQIIMAKP 521
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
31-523 |
1.25e-64 |
|
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: 217.90 E-value: 1.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 31 GAIAIGDLVKSTLGPKGMDKILLSSGRDaaLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELL 110
Cdd:cd03342 20 AAKGLQDVLKTNLGPKGTLKMLVSGAGD--IKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGELL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 111 REAESLIAKKIHPQTIISGWREATKAAREALLSSAVDhgSDEARFWQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRL 190
Cdd:cd03342 98 KQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVP--VEIDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 191 KGSG---NLEAIHVIKKLGGSLADSYLDEGFLLDKKI-GVNQPKRIENAKILIANTGMDTDKIKIFGSRVrvdstakvae 266
Cdd:cd03342 176 YKPDepiDLHMVEIMQMQHKSDSDTKLIRGLVLDHGArHPDMPKRVENAYILTCNVSLEYEKTEVNSGFF---------- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 267 iehaekekmkekverilkhgINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSC 346
Cdd:cd03342 246 --------------------YSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPECLGYA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 347 KLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDPRTVYGGGCSEMLMAHAVTQLAN 426
Cdd:cd03342 306 GLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHLKEFKK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 427 RTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHITAGLDMKEGTIGDMAVLGITESFQVKRQVLLS 506
Cdd:cd03342 386 SVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHS 465
|
490
....*....|....*..
gi 1302188017 507 AAEAAEVILRVDNIIKA 523
Cdd:cd03342 466 ATVIASQLLLVDEIIRA 482
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
157-403 |
1.77e-62 |
|
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: 203.47 E-value: 1.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 157 QDLMNIAGTTLSSKLlTHHKDHFTKLAVEAVLRLKGSG---NLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRI 232
Cdd:cd03333 2 ELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNrmdDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYmPKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 233 ENAKILIANTGMDTdkikifgsrvrvdstakvaeiehaekekmkekverilkhginCFINRQLIYNYPEQLFGAAGVMAI 312
Cdd:cd03333 81 ENAKILLLDCPLEY------------------------------------------VVIAEKGIDDLALHYLAKAGIMAV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 313 EHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHD 392
Cdd:cd03333 119 RRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRSLHD 198
|
250
....*....|.
gi 1302188017 393 ALCVLAQTVKD 403
Cdd:cd03333 199 ALCAVRAAVEE 209
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
9-528 |
3.40e-62 |
|
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: 212.67 E-value: 3.40e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 9 VNIFKAGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDAALmvTNDGATILKNIGVDNPAAKVLVDMS 88
Cdd:TIGR02347 2 VKLLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKL--TKDGNVLLNEMQIQHPTASMIARAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 89 RVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAVdhgSDEARFWQD-LMNIAGTTL 167
Cdd:TIGR02347 80 TAQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKV---KKEDEVDREfLLNVARTSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 168 SSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHVIKKLG---GSLADSYLDEGFLLDKkiGV---NQPKRIENAKILIAN 241
Cdd:TIGR02347 157 RTKLPADLADQLTEIVVDAVLAIKKDGEDIDLFMVEIMEmkhKSATDTTLIRGLVLDH--GArhpDMPRRVKNAYILTCN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 242 TGMDTDKIKIFGSRVRVDSTAKVAEIEhAEKEKMKEKVERILKhgincfINRQLIYNYPEQ----------------LFG 305
Cdd:TIGR02347 235 VSLEYEKTEVNSGFFYSSAEQREKLVK-AERKFVDDRVKKIIE------LKKKVCGKSPDKgfvvinqkgidppsldLLA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 306 AAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDE 385
Cdd:TIGR02347 308 KEGIMALRRAKRRNMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 386 AERSLHDALCVLAQTVKDPRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQL 465
Cdd:TIGR02347 388 IKDAVRDGLRAVKNAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKL 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1302188017 466 RAAHSEGHITAGLDMKEGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKR 528
Cdd:TIGR02347 468 EDEHDEGGEVVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSML 530
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
22-515 |
7.05e-16 |
|
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: 80.19 E-value: 7.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 22 ETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGrdAALMVTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGD 97
Cdd:cd03344 7 EEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSF--GSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 98 GTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAVDHGSDEarfwqDLMNIAgtTLSSklltHHKD 177
Cdd:cd03344 85 GTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKE-----EIAQVA--TISA----NGDE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 178 HFTKLAVEAVLRLKGSGnleAIHVikKLGGSLaDSYLD--EGFLLDKkiG------VNQPKR----IENAKILIantgmd 245
Cdd:cd03344 154 EIGELIAEAMEKVGKDG---VITV--EEGKTL-ETELEvvEGMQFDR--GylspyfVTDPEKmeveLENPYILL------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 246 TDKiKIfgsrvrvdSTAK--VAEIEHaekekmkekverILKHGINCFIN---------RQLIYNypeQLFGAAGVMAIEH 314
Cdd:cd03344 220 TDK-KI--------SSIQelLPILEL------------VAKAGRPLLIIaedvegealATLVVN---KLRGGLKVCAVKA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 315 ADF-----AGVERLALVTGG-----EIASTFDHPELVKLGSCKlieEVMIGEDKLIHFSGValGEACTIVLRgaTQQILD 384
Cdd:cd03344 276 PGFgdrrkAMLEDIAILTGGtviseELGLKLEDVTLEDLGRAK---KVVVTKDDTTIIGGA--GDKAAIKAR--IAQIRK 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 385 EAERS---------------------------------------LHDALCVLAQTVKDPrTVYGGGCSEMLMAHAVTQLA 425
Cdd:cd03344 349 QIEETtsdydkeklqerlaklsggvavikvggatevelkekkdrVEDALNATRAAVEEG-IVPGGGVALLRASPALDKLK 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 426 NRTPGkEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAahSEGHItaGLDMKEGTIGDMAVLGITESFQVKRQVLL 505
Cdd:cd03344 428 ALNGD-EKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLE--SPDGF--GYDAATGEYVDMIEAGIIDPTKVVRSALQ 502
|
570
....*....|
gi 1302188017 506 SAAEAAEVIL 515
Cdd:cd03344 503 NAASVASLLL 512
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
24-530 |
9.66e-13 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 70.52 E-value: 9.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 24 ARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGrdAALMVTNDGATILKNIGVDNPAAKVLVDMSRV----QDDEVGDGT 99
Cdd:PRK12850 12 ARDRLLRGVNILANAVKVTLGPKGRNVVLEKSF--GAPRITKDGVTVAKEIELEDKFENMGAQMVKEvaskTNDLAGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 100 TSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAVDHGSDEarfwqDLMNIAgtTLSSklltHHKDHF 179
Cdd:PRK12850 90 TTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSK-----EIAQVA--TISA----NGDESI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 180 TKLAVEAVLRLKGSGnleaihVIKKLGGSLADSYLD--EGFLLDKkiG------VNQPKR----IENAKILIANtgmdtd 247
Cdd:PRK12850 159 GEMIAEAMDKVGKEG------VITVEEAKTLGTELDvvEGMQFDR--GylspyfVTNPEKmraeLEDPYILLHE------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 248 kIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKhgincfinrQLIYNypeQLFGAAGVMAIEHADF-----AGVER 322
Cdd:PRK12850 225 -KKISNLQDLLPILEAVVQSGRPLLIIAEDVEGEALA---------TLVVN---KLRGGLKSVAVKAPGFgdrrkAMLED 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 323 LALVTGGEIAS-----TFDHPELVKLGSCKLI----EEVMI----GEDKLIH---------------------------- 361
Cdd:PRK12850 292 IAVLTGGQVISedlgiKLENVTLDMLGRAKRVlitkENTTIidgaGDKKNIEarvkqiraqieettsdydreklqerlak 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 362 -FSGVALgeactIVLRGATQQILDEAERSLHDALCVLAQTVKDPrTVYGGGCSeMLMAHAVTQLANRTPGKEAVAMESFA 440
Cdd:PRK12850 372 lAGGVAV-----IRVGGATEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVA-LLRARSALRGLKGANADETAGIDIVR 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 441 KALRMLPTIIADNAGYDSADLVAQLRaahsEGHITAGLDMKEGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNI 520
Cdd:PRK12850 445 RALEEPLRQIATNAGFEGSVVVGKVA----ELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAM 520
|
570
....*....|
gi 1302188017 521 IKAAPRKRVP 530
Cdd:PRK12850 521 VAEAPKKAAA 530
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
24-515 |
2.54e-12 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 69.17 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 24 ARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSgrDAALMVTNDGATILKNI----GVDNPAAKVLVDMSRVQDDEVGDGT 99
Cdd:PTZ00114 23 ARQSLLKGIERLADAVAVTLGPKGRNVIIEQE--YGSPKITKDGVTVAKAIefsdRFENVGAQLIRQVASKTNDKAGDGT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 100 TSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAVDHGSDEarfwqDLMNIAgtTLSS-------KLL 172
Cdd:PTZ00114 101 TTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKE-----DILNVA--TISAngdveigSLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 173 ThhkDHFTKLAVEAVLRLKGSGNLEaiHVIKKLGG-SLADSYLDEGFLLDKKigvNQPKRIENAKILIANTgmdtdKIKI 251
Cdd:PTZ00114 174 A---DAMDKVGKDGTITVEDGKTLE--DELEVVEGmSFDRGYISPYFVTNEK---TQKVELENPLILVTDK-----KISS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 252 FGSRVRVdstakvaeIEHAekekmkekveriLKHGINCFIN---------RQLIYNypeQLFGAAGVMAIEHADF----- 317
Cdd:PTZ00114 241 IQSILPI--------LEHA------------VKNKRPLLIIaedvegealQTLIIN---KLRGGLKVCAVKAPGFgdnrk 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 318 AGVERLALVTGGEIAS------TFDHPELVKLGSCK------------------------------LIEEVMIGEDK--- 358
Cdd:PTZ00114 298 DILQDIAVLTGATVVSednvglKLDDFDPSMLGSAKkvtvtkdetviltgggdkaeikervellrsQIERTTSEYDKekl 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 359 ---LIHFSG-VALgeactIVLRGATQQILDEAERSLHDALCVLAQTVKDPrTVYGGGCSeMLMA---HAVTQLANRTPGK 431
Cdd:PTZ00114 378 kerLAKLSGgVAV-----IKVGGASEVEVNEKKDRIEDALNATRAAVEEG-IVPGGGVA-LLRAsklLDKLEEDNELTPD 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 432 EAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRaahSEGHITAGLDMKEGTIGDMAVLGITESFQVKRQVLLSAAEAA 511
Cdd:PTZ00114 451 QRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKIL---EKKDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVA 527
|
....
gi 1302188017 512 EVIL 515
Cdd:PTZ00114 528 SLML 531
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
22-145 |
2.07e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 66.37 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 22 ETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGrdAALMVTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGD 97
Cdd:PRK12849 9 EEARRALERGVNKLADAVKVTLGPKGRNVVIDKSF--GAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGD 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1302188017 98 GTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSA 145
Cdd:PRK12849 87 GTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALA 134
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
24-527 |
7.14e-11 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 64.67 E-value: 7.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 24 ARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGrdAALMVTNDGATILKNIGVD----NPAAKVLVDMSRVQDDEVGDGT 99
Cdd:PRK14104 12 ARDRMLRGVDILANAVKVTLGPKGRNVVLDKSF--GAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKSADAAGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 100 TSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAVDHGSDEARFWQDLMNIAGTTLSSKLLThhkDHF 179
Cdd:PRK14104 90 TTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFLA---DAM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 180 TKLAVEAVLRLKGSGNLEaihvikklggsladSYLD--EGFLLDKkiGVNQPKRIENAKILiantGMDTDKIKIFGSRVR 257
Cdd:PRK14104 167 KKVGNEGVITVEEAKSLE--------------TELDvvEGMQFDR--GYISPYFVTNADKM----RVEMDDAYILINEKK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 258 VDSTAKVAEIEHAEKEKMKEKVerILKHGINCFINRQLIYNypeQLFGAAGVMAIEHADF-----AGVERLALVTGGEIA 332
Cdd:PRK14104 227 LSSLNELLPLLEAVVQTGKPLV--IVAEDVEGEALATLVVN---RLRGGLKVAAVKAPGFgdrrkAMLQDIAILTGGQAI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 333 S-----TFDHPELVKLGSCKlieEVMIGEDKLIHFSGVA-----------------------------------LGEACT 372
Cdd:PRK14104 302 SedlgiKLENVTLQMLGRAK---KVMIDKENTTIVNGAGkkadiearvaqikaqieettsdydreklqerlaklAGGVAV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 373 IVLRGATQQILDEAERSLHDALCVLAQTVKDPrTVYGGGCSEMLMAHAVTQLANRTPGKEAvAMESFAKALRMLPTIIAD 452
Cdd:PRK14104 379 IRVGGATEVEVKERKDRVDDAMHATRAAVEEG-IVPGGGVALLRASEQLKGIKTKNDDQKT-GVEIVRKALSAPARQIAI 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1302188017 453 NAGYDSADLVAQLRAAHSEGHitaGLDMKEGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRK 527
Cdd:PRK14104 457 NAGEDGSVIVGKILEKEQYSY---GFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKK 528
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
14-534 |
7.30e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 64.48 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 14 AGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGrdAALMVTNDGATILKNIGVD----NPAAKVLVDMSR 89
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSF--GAPRITKDGVTVAKEIELEdkfeNMGAQMVREVAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 90 VQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAVDHGSDEARFWQDLMNIAGTTLSS 169
Cdd:PRK12852 80 KTNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 170 KLLTHHKDhftKLAVEAVLRLKGSGNLEA-IHVIKklGGSLADSYLDEGFLLDKKigvNQPKRIENAKILIANTgmdtdk 248
Cdd:PRK12852 160 KMIAQAMQ---KVGNEGVITVEENKSLETeVDIVE--GMKFDRGYLSPYFVTNAE---KMTVELDDAYILLHEK------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 249 iKIFGSRVRVDSTAKVAEiehaekekmKEKVERILKHGINCFINRQLIYNypeQLFGAAGVMAIEHADF-----AGVERL 323
Cdd:PRK12852 226 -KLSGLQAMLPVLEAVVQ---------SGKPLLIIAEDVEGEALATLVVN---RLRGGLKVAAVKAPGFgdrrkAMLEDI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 324 ALVTGGEIAS-----TFDHPELVKLGSCKlieEVMIGEDKLIHFSGVA-------------------------------- 366
Cdd:PRK12852 293 AILTGGQLISedlgiKLENVTLKMLGRAK---KVVIDKENTTIVNGAGkkadiearvgqikaqieettsdydreklqerl 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 367 ---LGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDPrTVYGGGCSEMLMAHAVTQLANRTPGKEAvAMESFAKAL 443
Cdd:PRK12852 370 aklAGGVAVIRVGGATEVEVKEKKDRVEDALNATRAAVQEG-IVPGGGVALLRAKKAVGRINNDNADVQA-GINIVLKAL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 444 RMLPTIIADNAGYDSADLVAQLRAAHSEghiTAGLDMKEGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKA 523
Cdd:PRK12852 448 EAPIRQIAENAGVEGSIVVGKILENKSE---TFGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAE 524
|
570
....*....|.
gi 1302188017 524 APRKRVPDHHP 534
Cdd:PRK12852 525 LPKKDAAPAMP 535
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
31-531 |
1.39e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 63.61 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 31 GAIAIGDLVKSTLGPKGMDKILLSSGrdAALMVTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLA 106
Cdd:PRK12851 19 GVNILADAVKVTLGPKGRNVVIDKSF--GAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 107 AELLREAESLIAKKIHPQTIISGWREATKAAREAL--LSSAVDHGSDEARFwqdlmniagTTLSSklltHHKDHFTKLAV 184
Cdd:PRK12851 97 QAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELkaNARPVTTNAEIAQV---------ATISA----NGDAEIGRLVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 185 EAVLRLKGSGnleaihVIKKLGGSLADSYLD--EGFLLDK----KIGVNQPKR----IENAKILIANTgmdtdkiKIFGS 254
Cdd:PRK12851 164 EAMEKVGNEG------VITVEESKTAETELEvvEGMQFDRgylsPYFVTDADKmeaeLEDPYILIHEK-------KISNL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 255 RVRVDSTAKVAEIEHAEKEKMKEKVERILKhgincfinrQLIYNYPEQLFGAAGVMAIEHAD--FAGVERLALVTGGEIA 332
Cdd:PRK12851 231 QDLLPVLEAVVQSGKPLLIIAEDVEGEALA---------TLVVNKLRGGLKVAAVKAPGFGDrrKAMLEDIAILTGGTVI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 333 S-----TFDHPELVKLGSCKLI-----EEVMIG-------------------------------EDKLIHFS-GVALgea 370
Cdd:PRK12851 302 SedlgiKLENVTLEQLGRAKKVvvekeNTTIIDgagskteiegrvaqiraqieettsdydreklQERLAKLAgGVAV--- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 371 ctIVLRGATQQILDEAERSLHDALCVLAQTVKDPrTVYGGGCSEMLMAHAVTQLANRTpGKEAVAMESFAKALRMLPTII 450
Cdd:PRK12851 379 --IRVGASTEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRAVKALDKLETAN-GDQRTGVEIVRRALEAPVRQI 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 451 ADNAGYDSADLVAQLRaahsEGHITAGLDMKEGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKRVP 530
Cdd:PRK12851 455 AENAGAEGSVVVGKLR----EKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPA 530
|
.
gi 1302188017 531 D 531
Cdd:PRK12851 531 P 531
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
22-153 |
2.89e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 59.37 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 22 ETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGrdAALMVTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGD 97
Cdd:PRK00013 9 EDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSF--GAPTITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGD 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1302188017 98 GTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAVDHGSDEA 153
Cdd:PRK00013 87 GTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEE 142
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
31-136 |
7.31e-08 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 54.93 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 31 GAIAIGDLVKSTLGPKGMDKILLSsgRDAALMVTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLA 106
Cdd:PLN03167 74 GVNKLADLVGVTLGPKGRNVVLES--KYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLA 151
|
90 100 110
....*....|....*....|....*....|
gi 1302188017 107 AELLREAESLIAKKIHPQTIISGWREATKA 136
Cdd:PLN03167 152 QGLIAEGVKVVAAGANPVQITRGIEKTAKA 181
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
39-135 |
2.62e-06 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 50.10 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 39 VKSTLGPKGMDKILlsSGRDAALMVTNDGATILKNIGVDNPAAKVLVDMSRV----QDDEVGDGTTSVTVLAAELLREAE 114
Cdd:CHL00093 26 VSVTLGPKGRNVVL--EKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQaaskTNDVAGDGTTTATVLAYAIVKQGM 103
|
90 100
....*....|....*....|.
gi 1302188017 115 SLIAKKIHPQTIISGWREATK 135
Cdd:CHL00093 104 KNVAAGANPISLKRGIEKATQ 124
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
320-398 |
6.90e-04 |
|
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: 41.44 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302188017 320 VERLALVTGGEIASTFDHpeLV---KLGSCKLIE-EVMIGEDK----LIHFSG--VALGeaCTIVLRGATQQILDEAERS 389
Cdd:cd03334 164 LERISRCTGADIISSMDD--LLtspKLGTCESFRvRTYVEEHGrsktLMFFEGcpKELG--CTILLRGGDLEELKKVKRV 239
|
....*....
gi 1302188017 390 LHdaLCVLA 398
Cdd:cd03334 240 VE--FMVFA 246
|
|
| |
