|
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: 1014.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 11 IFKAGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRV 90
Cdd:cd03336 1 ILKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILQSVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 91 QDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSSK 170
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEAFREDLLNIARTTLSSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 171 LLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIK 250
Cdd:cd03336 161 ILTQDKEHFAELAVDAVLRLKGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQPKRIENAKILIANTPMDTDKIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 251 IFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGE 330
Cdd:cd03336 241 IFGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTGGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 331 IASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGG 410
Cdd:cd03336 321 IASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRVVLGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 411 GCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAI 490
Cdd:cd03336 401 GCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTVGDMKE 480
|
490 500 510
....*....|....*....|....*....|....*..
gi 5453603 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: 930.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 5 SLAPVNIFKAGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSG---RDASLMVTNDGATILKNIGVDNPAA 81
Cdd:PTZ00212 4 ANVPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMSegpRSGNVTVTNDGATILKSVWLDNPAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 82 KVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSDEVKFRQDLMN 161
Cdd:PTZ00212 84 KILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEKFKEDLLN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 162 IAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIAN 241
Cdd:PTZ00212 164 IARTTLSSKLLTVEKDHFAKLAVDAVLRLKGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVGQPKRLENCKILVAN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 242 TGMDTDKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVE 321
Cdd:PTZ00212 244 TPMDTDKIKIYGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGME 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 322 RLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTV 401
Cdd:PTZ00212 324 RLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 402 KDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMR 481
Cdd:PTZ00212 404 KDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGIDME 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 5453603 482 EGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKRVP 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: 911.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 10 NIFKAGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDASLMVTNDGATILKNIGVDNPAAKVLVDMSR 89
Cdd:TIGR02341 1 QIFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 90 VQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSS 169
Cdd:TIGR02341 81 VQDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVKFRQDLMNIARTTLSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 170 KLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKI 249
Cdd:TIGR02341 161 KILSQHKDHFAQLAVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 250 KIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGG 329
Cdd:TIGR02341 241 KIFGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 330 EIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYG 409
Cdd:TIGR02341 321 EIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 410 GGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMA 489
Cdd:TIGR02341 401 GGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGTIADMR 480
|
490 500 510
....*....|....*....|....*....|....*....
gi 5453603 490 ILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKR 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: 542.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 16 ADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEV 95
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGD--PTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 96 GDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHgsdEVKFRQDLMNIAGTTLSSKLLTHH 175
Cdd:cd00309 79 GDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPI---DVEDREELLKVATTSLNSKLVSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 176 KDHFTKLAVEAVLRLKGSG---NLEAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTdkiki 251
Cdd:cd00309 156 DDFLGELVVDAVLKVGKENgdvDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYmPKRLENAKILLLDCKLEY----- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 252 fgsrvrvdstakvaeiehaekekmkekverilkhginCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEI 331
Cdd:cd00309 231 -------------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 332 ASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGG 411
Cdd:cd00309 274 VSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 412 CSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAIL 491
Cdd:cd00309 354 AAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKEA 433
|
490 500 510
....*....|....*....|....*....|.
gi 5453603 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 |
2.01e-174 |
|
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: 500.96 E-value: 2.01e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 35 IGDLVKSTLGPKGMDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAE 114
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGD--VTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 115 SLIAKKIHPQTIIAGWREATKAAREALLSsaVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLK--- 191
Cdd:pfam00118 79 KLLAAGVHPTTIIEGYEKALEKALEILDS--IISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 192 GSGNLEAIHIIKKLGGSLADSYLDEGFLLDKKI-GVNQPKRIENAKILIANTGMDTDKIKIFGSrVRVDSTAKVAEIEHA 270
Cdd:pfam00118 157 GSFDLGNIGVVKILGGSLEDSELVDGVVLDKGPlHPDMPKRLENAKVLLLNCSLEYEKTETKAT-VVLSDAEQLERFLKA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 271 EKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIE 350
Cdd:pfam00118 236 EEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 351 EVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPG 430
Cdd:pfam00118 316 EEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 431 KEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEA 510
Cdd:pfam00118 396 KEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEA 475
|
490
....*....|...
gi 5453603 511 AEVILRVDNIIKA 523
Cdd:pfam00118 476 ASTILRIDDIIKA 488
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
9-524 |
2.46e-129 |
|
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: 387.00 E-value: 2.46e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 9 VNIFKAGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMS 88
Cdd:cd03343 1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGD--VTITNDGATILKEMDIEHPAAKMLVEVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 89 RVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSDEVKFrqdLMNIAGTTLS 168
Cdd:cd03343 79 KTQDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDT---LRKIAKTSLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 169 SKLLTHHKDHFTKLAVEAVLRL--KGSG----NLEAIHIIKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIAN 241
Cdd:cd03343 156 GKGAEAAKDKLADLVVDAVLQVaeKRDGkyvvDLDNIKIEKKTGGSVDDTELIRGIVIDKeVVHPGMPKRVENAKIALLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 242 TGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVE 321
Cdd:cd03343 236 APLEVKKTEI-DAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDME 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 322 RLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTV 401
Cdd:cd03343 315 KLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADAL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 402 KDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMR 481
Cdd:cd03343 395 EDGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVY 474
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 5453603 482 EGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAA 524
Cdd:cd03343 475 TGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
8-524 |
2.29e-128 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 384.62 E-value: 2.29e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 8 PVNIFKAGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDM 87
Cdd:NF041082 2 PILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGD--VVITNDGVTILKEMDIEHPAAKMIVEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 88 SRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSDEvkfRQDLMNIAGTTL 167
Cdd:NF041082 80 AKTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDD---KETLKKIAATAM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 168 SSKLLTHHKDHFTKLAVEAVLRL---KGSGN--LEAIHIIKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIAN 241
Cdd:NF041082 157 TGKGAEAAKDKLADLVVDAVKAVaekDGGYNvdLDNIKVEKKVGGSIEDSELVEGVVIDKeRVHPGMPKRVENAKIALLD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 242 TGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVE 321
Cdd:NF041082 237 APLEVKKTEI-DAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDME 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 322 RLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTV 401
Cdd:NF041082 316 KLAKATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 402 KDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMR 481
Cdd:NF041082 396 EDGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVY 475
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 5453603 482 EGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAA 524
Cdd:NF041082 476 TGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
7-524 |
5.36e-126 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 378.52 E-value: 5.36e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 7 APVNIFKAGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVD 86
Cdd:NF041083 1 QPVLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGD--IVITNDGATILKEMDVQHPAAKMLVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 87 MSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSDEvkfRQDLMNIAGTT 166
Cdd:NF041083 79 VAKTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDD---RETLKKIAETS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 167 LSSKLLTHHKDHFTKLAVEAVLRL------KGSGNLEAIHIIKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILI 239
Cdd:NF041083 156 LTSKGVEEARDYLAEIAVKAVKQVaekrdgKYYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKeVVHPGMPKRVENAKIAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 240 ANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAG 319
Cdd:NF041083 236 LDAPLEVKKTEI-DAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 320 VERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQ 399
Cdd:NF041083 315 MEKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVAD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 400 TVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLD 479
Cdd:NF041083 395 AVEDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGIN 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 5453603 480 MREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAA 524
Cdd:NF041083 475 VFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
8-523 |
3.99e-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: 371.33 E-value: 3.99e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 8 PVNIFKAGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDM 87
Cdd:TIGR02339 1 PVFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGD--VTITNDGATILKEMDIEHPAAKMLVEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 88 SRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSDEvkfRQDLMNIAGTTL 167
Cdd:TIGR02339 79 AKTQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPED---RDLLKKIAYTSL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 168 SSKLLT-HHKDHFTKLAVEAVLRL-------KGSGNLEAIHIIKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKIL 238
Cdd:TIGR02339 156 TSKASAeVAKDKLADLVVEAVKQVaelrgdgKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKeVVHPGMPKRVENAKIA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 239 IANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFA 318
Cdd:TIGR02339 236 LLDAPLEVEKTEI-DAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 319 GVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLA 398
Cdd:TIGR02339 315 DIEKLARATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 399 QTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGL 478
Cdd:TIGR02339 395 NALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGI 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 5453603 479 DMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKA 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 |
8.52e-123 |
|
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: 370.46 E-value: 8.52e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 8 PVNIFKAGADEERAeTARLTSFIGA-IAIGDLVKSTLGPKGMDKILLSSGRDASlmVTNDGATILKNIGVDNPAAKVLVD 86
Cdd:cd03340 1 PIILLKEGTDTSQG-KGQLISNINAcQAIADAVRTTLGPRGMDKLIVDGRGKVT--ISNDGATILKLLDIVHPAAKTLVD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 87 MSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVD-HGSDEVKFRQDLMNIAGT 165
Cdd:cd03340 78 IAKSQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNiDKEDKEEQRELLEKCAAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 166 TLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKKLGGSLADSYLDEGFLLDKKIGV----NQPKRIENAKILIAN 241
Cdd:cd03340 158 ALNSKLIASEKEFFAKMVVDAVLSLDDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYagfeQQPKKFKNPKILLLN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 242 TGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMA---IEHADFa 318
Cdd:cd03340 238 VELELKAEKD-NAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCagrVPEEDL- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 319 gvERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLA 398
Cdd:cd03340 316 --KRVAQATGGSIQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 399 QTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTT-AG 477
Cdd:cd03340 394 RAIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKwYG 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 5453603 478 LDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKA 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 |
9.15e-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: 347.35 E-value: 9.15e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 22 ETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDASlmVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTS 101
Cdd:cd03335 7 QDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVT--ITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 102 VTVLAAELLREAESLIAKKIHPQTIIAGWR----EATKAAREALLSSAVDHGsdevkfRQDLMNIAGTTLSSKLLTHHKD 177
Cdd:cd03335 85 VVIIAAELLKRANELVKQKIHPTTIISGYRlackEAVKYIKEHLSISVDNLG------KESLINVAKTSMSSKIIGADSD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 178 HFTKLAVEAVLRLKGSGNL-------EAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTDKI 249
Cdd:cd03335 159 FFANMVVDAILAVKTTNEKgktkypiKAVNILKAHGKSAKESYLVNGYALNCTRASQGmPTRVKNAKIACLDFNLQKTKM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 250 KIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGG 329
Cdd:cd03335 239 KL-GVQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 330 EIASTFDHPE------LVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKD 403
Cdd:cd03335 318 TLVSTLANLEgeetfdPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLES 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 404 SRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTA------- 476
Cdd:cd03335 398 NSVVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKPdkkhlkw 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 5453603 477 -GLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAP 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 |
2.47e-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: 345.98 E-value: 2.47e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 8 PVNIFKAGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDASlmVTNDGATILKNIGVDNPAAKVLVDM 87
Cdd:TIGR02345 3 TIVLLKEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKAT--ISNDGATILKLLDIVHPAAKTLVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 88 SRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSDEVKFRQDLMNIAGTTL 167
Cdd:TIGR02345 81 AKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKGEQRELLEKCAATAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 168 SSKLLTHHKDHFTKLAVEAVLRLKGSG-NLEAIHIIKKLGGSLADSYLDEGFLLDKKIGV----NQPKRIENAKILIANT 242
Cdd:TIGR02345 161 SSKLISHNKEFFSKMIVDAVLSLDRDDlDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYagfeQQPKKFANPKILLLNV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 243 GMDTdKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVER 322
Cdd:TIGR02345 241 ELEL-KAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 323 LALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVK 402
Cdd:TIGR02345 320 VIKACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 403 DSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMRE 482
Cdd:TIGR02345 400 NKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINT 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 5453603 483 GTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKA 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 |
3.69e-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: 345.94 E-value: 3.69e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 15 GADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDASlmVTNDGATILKNIGVDNPAAKVLVDMSRVQDDE 94
Cdd:TIGR02340 4 GGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVT--ITNDGATILKLLEVEHPAAKILVELAQLQDRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 95 VGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWR----EATKAAREALLSSAVDHGsdevkfRQDLMNIAGTTLSSK 170
Cdd:TIGR02340 82 VGDGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRlackEAVKYIKENLSVSVDELG------REALINVAKTSMSSK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 171 LLTHHKDHFTKLAVEAVLRLKGSGN-------LEAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANT 242
Cdd:TIGR02340 156 IIGLDSDFFSNIVVDAVLAVKTTNEngetkypIKAINILKAHGKSARESMLVKGYALNCTVASQQmPKRIKNAKIACLDF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 243 GMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVER 322
Cdd:TIGR02340 236 NLQKAKMAL-GVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 323 LALVTGGEIASTFDHPE------LVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCV 396
Cdd:TIGR02340 315 IAKATGATLVSTLADLEgeetfeASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 397 LAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHS------ 470
Cdd:TIGR02340 395 VKRTLESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAaaqlkp 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 5453603 471 --EGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRK 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 |
1.33e-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: 326.18 E-value: 1.33e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 8 PVNIFKAGADEERAE--TARLTSFIGAIAIGDLVKSTLGPKGMDKILLSsgRDASLMVTNDGATILKNIGVDNPAAKVLV 85
Cdd:cd03339 6 PFIIVREQEKKKRLKglEAHKSHILAAKSVANILRTSLGPRGMDKILVS--PDGEVTVTNDGATILEKMDVDHQIAKLLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 86 DMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAvDHGSDEVKFRQDLMNIAGT 165
Cdd:cd03339 84 ELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIA-DKIEFSPDNKEPLIQTAMT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 166 TLSSKLLTHHKDHFTKLAVEAVLRL----KGSGNLEAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIA 240
Cdd:cd03339 163 SLGSKIVSRCHRQFAEIAVDAVLSVadleRKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQmPKEVKDAKIAIL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 241 NTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFI---------NRQLIYNypeqlfgaaGVMA 311
Cdd:cd03339 243 TCPFEPPKPKT-KHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVIcqwgfddeaNHLLLQN---------GLPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 312 IEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIG--EDKLIHFSGVALGEACTIVLRGATQQILDEAERS 389
Cdd:cd03339 313 VRWVGGVEIELIAIATGGRIVPRFEDLSPEKLGKAGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 390 LHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAH 469
Cdd:cd03339 393 LHDALCVVRNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQ 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 5453603 470 -SEGNTTAGLD-MREGTiGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIK 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 |
2.05e-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: 2.05e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 17 DEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVG 96
Cdd:cd03338 2 DKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGE--VIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 97 DGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHgsdEVKFRQDLMNIAGTTLSSKLLTHHK 176
Cdd:cd03338 80 DGTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPV---DLNDRESLIKSATTSLNSKVVSQYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 177 DHFTKLAVEAVLRL-----KGSGNLEAIHIIKKLGGSLADSYLDEGFLLDKKI--GVNQPKRIENAKILIAN-------T 242
Cdd:cd03338 157 SLLAPIAVDAVLKVidpatATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKAskKAGGPTRIEKAKIGLIQfclsppkT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 243 GMDtdkikifgSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCF-----INRQLIYNYPEQLFGAAGVMAIEHADF 317
Cdd:cd03338 237 DMD--------NNIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLliqksILRDAVSDLALHFLAKLKIMVVKDIER 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 318 AGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVA-LGEACTIVLRGATQQILDEAERSLHDALCV 396
Cdd:cd03338 309 EEIEFICKTIGCKPVASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKnPGKTVTILVRGSNKLVLDEAERSLHDALCV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 397 LAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTA 476
Cdd:cd03338 389 IRCLVKKRALIPGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNA 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 5453603 477 GLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNII 521
Cdd:cd03338 469 GINVRKGAITNILEENVVQPLLVSTSAITLATETVRMILKIDDIV 513
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
24-522 |
4.80e-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: 307.11 E-value: 4.80e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 24 ARLTSFIGAIAIGDLVKSTLGPKGMDKILLSsgRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVT 103
Cdd:TIGR02343 28 AKKSNIAAAKSVASILRTSLGPKGMDKMLIS--PDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 104 VLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALlSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLA 183
Cdd:TIGR02343 106 VLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHL-EEISDEISADNNNREPLIQAAKTSLGSKIVSKCHRRFAEIA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 184 VEAVLRL----KGSGNLEAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTDKIKIfGSRVRV 258
Cdd:TIGR02343 185 VDAVLNVadmeRRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQmPKEVEDAKIAILTCPFEPPKPKT-KHKLDI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 259 DSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHP 338
Cdd:TIGR02343 264 SSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPRFQEL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 339 ELVKLGSCKLIEEVMIG--EDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEML 416
Cdd:TIGR02343 344 SKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGGGAAEIS 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 417 MAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAH-SEGNTTAGLD-MREGTiGDMAILGIT 494
Cdd:TIGR02343 424 CSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQlKEKNPNLGVDcLGYGT-NDMKEQFVF 502
|
490 500
....*....|....*....|....*...
gi 5453603 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 |
1.41e-93 |
|
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: 293.82 E-value: 1.41e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 8 PVNIFKAGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGrdASLMVTNDGATILKNIGVDNPAAKVLVDM 87
Cdd:cd03337 1 PVLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPM--GGIVLTNDGNAILREIDVAHPAAKSMIEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 88 SRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREAL--LSSAVDhgsdeVKFRQDLMNIAGT 165
Cdd:cd03337 79 SRTQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILeeISIPVD-----VNDRAQMLKIIKS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 166 TLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHI-IKK-------LGGSLADSYLDEGFLLDKKigVNQPK---RIEN 234
Cdd:cd03337 154 CIGTKFVSRWSDLMCNLALDAVKTVAVEENGRKKEIdIKRyakvekiPGGEIEDSRVLDGVMLNKD--VTHPKmrrRIEN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 235 AKILIantgmdtdkikifgsrvrVDSTakvaeIEHAEkekmkekverILKHGINcfinrQLIYNYpeqlFGAAGVMAIEH 314
Cdd:cd03337 232 PRIVL------------------LDCP-----LEYLV----------ITEKGVS-----DLAQHY----LVKAGITALRR 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 315 ADFAGVERLALVTGGEIASTFDHPELVKLG-SCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDA 393
Cdd:cd03337 270 VRKTDNNRIARACGATIVNRPEELTESDVGtGAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 394 LCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAH-SEG 472
Cdd:cd03337 350 MAVARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHaQGE 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 5453603 473 NTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNII 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 |
6.62e-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: 293.23 E-value: 6.62e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 17 DEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVG 96
Cdd:TIGR02342 3 DKDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGE--VIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 97 DGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREAL--LSSAVDHGSDEVkfrqdLMNIAGTTLSSKLLTH 174
Cdd:TIGR02342 81 DGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILdeMSIPVDLSDREQ-----LLKSATTSLSSKVVSQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 175 HKDHFTKLAVEAVLRLKGSG-----NLEAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQ--PKRIENAKILIANTGMDTD 247
Cdd:TIGR02342 156 YSSLLAPLAVDAVLKVIDPEnaknvDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAggPTRIEKAKIGLIQFQISPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 248 KIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCF-----INRQLIYNYPEQLFGAAGVMAIEHADFAGVER 322
Cdd:TIGR02342 236 KTDM-ENQIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLliqksILRDAVNDLALHFLAKMKIMVVKDIEREEIEF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 323 LALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVA-LGEACTIVLRGATQQILDEAERSLHDALCVLAQTV 401
Cdd:TIGR02342 315 ICKTIGCKPIASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQnAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 402 KDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMR 481
Cdd:TIGR02342 395 KKRGLIAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVR 474
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 5453603 482 EGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAA 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 |
1.64e-87 |
|
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: 277.56 E-value: 1.64e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 35 IGDLVKSTLGPKGMDKILLSSGRdaSLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAE 114
Cdd:cd03341 20 LSQITRTSYGPNGMNKMVINHLE--KLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGELLEKAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 115 SLIAKKIHPQTIIAGWREATKAAREALLSSAVdHGSDEVKFRQDLMNIAGTTLSSKLLtHHKDHFTKLAVEAVLRLK--- 191
Cdd:cd03341 98 ELLRMGLHPSEIIEGYEKALKKALEILEELVV-YKIEDLRNKEEVSKALKTAIASKQY-GNEDFLSPLVAEACISVLpen 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 192 -GSGNLEAIHIIKKLGGSLADSYLDEGFLLDKKIgVNQPKRIENAKILIANTGMDtdkikiFGSRVRVdSTAKVAEIeha 270
Cdd:cd03341 176 iGNFNVDNIRVVKILGGSLEDSKVVRGMVFKREP-EGSVKRVKKAKVAVFSCPFD------IGVNVIV-AGGSVGDL--- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 271 ekekmkekveriLKHgincFINRqliynypeqlfgaAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIE 350
Cdd:cd03341 245 ------------ALH----YCNK-------------YGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEEIGYCDSVY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 351 EVMIGEDKLIHFSGV-ALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTP 429
Cdd:cd03341 296 VEEIGDTKVVVFRQNkEDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAKKLKEYGEKTP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 430 GKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIG--DMAILGITESFQVKRQVLLSA 507
Cdd:cd03341 376 GLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDEGtkDAKEAGIFDHLATKKWAIKLA 455
|
490
....*....|....*.
gi 5453603 508 AEAAEVILRVDNIIKA 523
Cdd:cd03341 456 TEAAVTVLRVDQIIMA 471
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
22-527 |
3.91e-83 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 266.94 E-value: 3.91e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 22 ETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSgrDASLMVTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGD 97
Cdd:COG0459 9 EDARRANIRGVKALADAVKVTLGPKGRNVMLVKS--FGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 98 GTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDhgsdeVKFRQDLMNIAGTTLSSkllthhKD 177
Cdd:COG0459 87 GTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKP-----VDDKEELAQVATISANG------DE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 178 HFTKLAVEAVLRLKGSGNLeaihIIKKLGGSLADSYLDEGFLLDKKI--------GVNQPKRIENAKILIANtgmdtDKI 249
Cdd:COG0459 156 EIGELIAEAMEKVGKDGVI----TVEEGKGLETELEVVEGMQFDKGYlspyfvtdPEKMPAELENAYILLTD-----KKI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 250 KIFGSRVrvdstaKVAEiehaekekmkekveRILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHAdfAGV--------- 320
Cdd:COG0459 227 SSIQDLL------PLLE--------------KVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRV--VAVkapgfgdrr 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 321 ----ERLALVTGGEIAS-----TFDHPELVKLGSCKLIEevmIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLH 391
Cdd:COG0459 285 kamlEDIAILTGGRVISedlglKLEDVTLDDLGRAKRVE---VDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 392 DALCVLAQTVKDsRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAhse 471
Cdd:COG0459 362 DALHATRAAVEE-GIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA--- 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 5453603 472 GNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRK 527
Cdd:COG0459 438 KDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEK 493
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
8-527 |
1.58e-82 |
|
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: 266.22 E-value: 1.58e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 8 PVNIFKAGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGrdASLMVTNDGATILKNIGVDNPAAKVLVDM 87
Cdd:TIGR02344 1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPM--GGIVMTNDGNAILREIDVAHPAAKSMIEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 88 SRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREAL--LSSAVDhgsdeVKFRQDLMNIAGT 165
Cdd:TIGR02344 79 SRTQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLeeISIPVD-----VNDDAAMLKLIQS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 166 TLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKKL-------GGSLADSYLDEGFLLDKKigVNQPK---RIENA 235
Cdd:TIGR02344 154 CIGTKFVSRWSDLMCDLALDAVRTVQRDENGRKEIDIKRYakvekipGGDIEDSCVLKGVMINKD--VTHPKmrrYIENP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 236 KILIANTGMDTDKIKifgSRVRVDST-----AKVAEIEHaekEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVM 310
Cdd:TIGR02344 232 RIVLLDCPLEYKKGE---SQTNIEITkeedwNRILQMEE---EYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANIT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 311 AIEHADFAGVERLALVTGGEIASTFDHPELVKLGS-CKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERS 389
Cdd:TIGR02344 306 AIRRVRKTDNNRIARACGATIVNRPEELRESDVGTgCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 390 LHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAH 469
Cdd:TIGR02344 386 LQDAMAVARNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKH 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 5453603 470 S-EGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRK 527
Cdd:TIGR02344 466 AqENNCTWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVSGVKKK 524
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
10-525 |
2.74e-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: 252.71 E-value: 2.74e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 10 NIFKAGADEERAETARLTSFIGAIA-IGDLVKSTLGPKGMDKILLSsgRDASLMVTNDGATILKNIGVDNPAAKVLVDMS 88
Cdd:TIGR02346 4 SLLKEGYRHFSGLEEAVIKNIEACKeLSQITRTSLGPNGMNKMVIN--HLEKLFVTNDAATILRELEVQHPAAKLLVMAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 89 RVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSDeVKFRQDLMNIAGTTLS 168
Cdd:TIGR02346 82 EMQENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKD-LRDKDELIKALKASIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 169 SKLLtHHKDHFTKLAVEAVLRLK----GSGNLEAIHIIKKLGGSLADSYLDEGFLLdKKIGVNQPKRIENAKILIANTGM 244
Cdd:TIGR02346 161 SKQY-GNEDFLAQLVAQACSTVLpknpQNFNVDNIRVCKILGGSLSNSEVLKGMVF-NREAEGSVKSVKNAKVAVFSCPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 245 DTDKIKIFGSrVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRqliynypeqlfGAAGVMAIEHADFAGV---- 320
Cdd:TIGR02346 239 DTATTETKGT-VLIHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTG-----------GSVGDMALHYLNKYNImvlk 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 321 -------ERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGV-ALGEACTIVLRGATQQILDEAERSLHD 392
Cdd:TIGR02346 307 ipskfelRRLCKTVGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQEnGDSKISTIILRGSTDNLLDDIERAIDD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 393 ALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEG 472
Cdd:TIGR02346 387 GVNTVKALVKDGRLLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKG 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 5453603 473 NTTAGLDMREGTIG--DMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAP 525
Cdd:TIGR02346 467 NKSKGIDIEAESDGvkDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKP 521
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
16-523 |
8.89e-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: 215.97 E-value: 8.89e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 16 ADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEV 95
Cdd:cd03342 5 AEVLRRGQALAVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGD--IKLTKDGNVLLSEMQIQHPTASMIARAATAQDDIT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 96 GDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDhgSDEVKFRQDLMNIAGTTLSSKLLTHH 175
Cdd:cd03342 83 GDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVP--VEIDTDRELLLSVARTSLRTKLHADL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 176 KDHFTKLAVEAVLRLKGSG---NLEAIHIIKKLGGSLADSYLDEGFLLDKKI-GVNQPKRIENAKILIANTGMDTDKIKI 251
Cdd:cd03342 161 ADQLTEIVVDAVLAIYKPDepiDLHMVEIMQMQHKSDSDTKLIRGLVLDHGArHPDMPKRVENAYILTCNVSLEYEKTEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 252 FGSRVrvdstakvaeiehaekekmkekverilkhgINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEI 331
Cdd:cd03342 241 NSGFF------------------------------YSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 332 ASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGG 411
Cdd:cd03342 291 MNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 412 CSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAIL 491
Cdd:cd03342 371 AFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESE 450
|
490 500 510
....*....|....*....|....*....|..
gi 5453603 492 GITESFQVKRQVLLSAAEAAEVILRVDNIIKA 523
Cdd:cd03342 451 GIWDNYSVKRQILHSATVIASQLLLVDEIIRA 482
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
9-528 |
9.04e-64 |
|
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: 216.91 E-value: 9.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 9 VNIFKAGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDASLmvTNDGATILKNIGVDNPAAKVLVDMS 88
Cdd:TIGR02347 2 VKLLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKL--TKDGNVLLNEMQIQHPTASMIARAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 89 RVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREaLLSSAVDHGSDEVKfRQDLMNIAGTTLS 168
Cdd:TIGR02347 80 TAQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQ-FLDKFKVKKEDEVD-REFLLNVARTSLR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 169 SKLLTHHKDHFTKLAVEAVLRLKGSG---NLEAIHIIKKLGGSLADSYLDEGFLLDKkiGV---NQPKRIENAKILIANT 242
Cdd:TIGR02347 158 TKLPADLADQLTEIVVDAVLAIKKDGediDLFMVEIMEMKHKSATDTTLIRGLVLDH--GArhpDMPRRVKNAYILTCNV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 243 GMDTDKIKIFGSRVRVDSTAKVAEIEhAEKEKMKEKVERILKhgincfINRQLIYNYPEQ----------------LFGA 306
Cdd:TIGR02347 236 SLEYEKTEVNSGFFYSSAEQREKLVK-AERKFVDDRVKKIIE------LKKKVCGKSPDKgfvvinqkgidppsldLLAK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 307 AGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEA 386
Cdd:TIGR02347 309 EGIMALRRAKRRNMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 387 ERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLR 466
Cdd:TIGR02347 389 KDAVRDGLRAVKNAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLE 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5453603 467 AAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKR 528
Cdd:TIGR02347 469 DEHDEGGEVVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSML 530
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
156-403 |
6.00e-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: 205.01 E-value: 6.00e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 156 RQDLMNIAGTTLSSKLlTHHKDHFTKLAVEAVLRLKGSG---NLEAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKR 231
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNrmdDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYmPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 232 IENAKILIANTGMDTdkikifgsrvrvdstakvaeiehaekekmkekverilkhginCFINRQLIYNYPEQLFGAAGVMA 311
Cdd:cd03333 80 LENAKILLLDCPLEY------------------------------------------VVIAEKGIDDLALHYLAKAGIMA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 312 IEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLH 391
Cdd:cd03333 118 VRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRSLH 197
|
250
....*....|..
gi 5453603 392 DALCVLAQTVKD 403
Cdd:cd03333 198 DALCAVRAAVEE 209
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
31-515 |
4.71e-17 |
|
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: 84.05 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 31 GAIAIGDLVKSTLGPKGMDKILLSSGrdASLMVTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLA 106
Cdd:cd03344 16 GVNKLADAVKVTLGPKGRNVVIEKSF--GSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 107 AELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVdhgsdEVKFRQDLMNIAgtTLSSklltHHKDHFTKLAVEA 186
Cdd:cd03344 94 RAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSK-----PVKTKEEIAQVA--TISA----NGDEEIGELIAEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 187 VLRLKGSGNleaihIIKKLGGSLaDSYLD--EGFLLDKkiG------VNQPKR----IENAKILIantgmdTDKiKIfgs 254
Cdd:cd03344 163 MEKVGKDGV-----ITVEEGKTL-ETELEvvEGMQFDR--GylspyfVTDPEKmeveLENPYILL------TDK-KI--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 255 rvrvdSTAK--VAEIEHaekekmkekverILKHGINCFIN---------RQLIYNypeQLFGAAGVMAIEHADF-----A 318
Cdd:cd03344 225 -----SSIQelLPILEL------------VAKAGRPLLIIaedvegealATLVVN---KLRGGLKVCAVKAPGFgdrrkA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 319 GVERLALVTGG-----EIASTFDHPELVKLGSCKlieEVMIGEDKLIHFSGValGEACTIVLRgaTQQILDEAERS---- 389
Cdd:cd03344 285 MLEDIAILTGGtviseELGLKLEDVTLEDLGRAK---KVVVTKDDTTIIGGA--GDKAAIKAR--IAQIRKQIEETtsdy 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 390 -----------------------------------LHDALCVLAQTVKDSrTVYGGGCSEMLMAHAVTQLANRTPGkEAV 434
Cdd:cd03344 358 dkeklqerlaklsggvavikvggatevelkekkdrVEDALNATRAAVEEG-IVPGGGVALLRASPALDKLKALNGD-EKL 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 435 AMESYAKALRMLPTIIADNAGYDSADLVAQLRaahsEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVI 514
Cdd:cd03344 436 GIEIVRRALEAPLRQIAENAGVDGSVVVEKVL----ESPDGFGYDAATGEYVDMIEAGIIDPTKVVRSALQNAASVASLL 511
|
.
gi 5453603 515 L 515
Cdd:cd03344 512 L 512
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
31-515 |
3.13e-13 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 72.25 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 31 GAIAIGDLVKSTLGPKGMDKILLSSgrDASLMVTNDGATILKNI----GVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLA 106
Cdd:PTZ00114 30 GIERLADAVAVTLGPKGRNVIIEQE--YGSPKITKDGVTVAKAIefsdRFENVGAQLIRQVASKTNDKAGDGTTTATILA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 107 AELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSavdhgSDEVKFRQDLMNIAgtTLSS-------KLLThhkDHF 179
Cdd:PTZ00114 108 RAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQ-----SRPVKTKEDILNVA--TISAngdveigSLIA---DAM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 180 TKLAVEAVLRLKGSGNLEaiHIIKKLGG-SLADSYLDEGFLLDKKigvNQPKRIENAKILIANTgmdtdKIKIFGSRVRV 258
Cdd:PTZ00114 178 DKVGKDGTITVEDGKTLE--DELEVVEGmSFDRGYISPYFVTNEK---TQKVELENPLILVTDK-----KISSIQSILPI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 259 dstakvaeIEHAekekmkekveriLKHGINCFIN---------RQLIYNypeQLFGAAGVMAIEHADF-----AGVERLA 324
Cdd:PTZ00114 248 --------LEHA------------VKNKRPLLIIaedvegealQTLIIN---KLRGGLKVCAVKAPGFgdnrkDILQDIA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 325 LVTGGEIAS------TFDHPELVKLGSCK------------------------------LIEEVMIGEDK------LIHF 362
Cdd:PTZ00114 305 VLTGATVVSednvglKLDDFDPSMLGSAKkvtvtkdetviltgggdkaeikervellrsQIERTTSEYDKeklkerLAKL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 363 SG-VALgeactIVLRGATQQILDEAERSLHDALCVLAQTVKDSrTVYGGGCSeMLMA---HAVTQLANRTPGKEAVAMES 438
Cdd:PTZ00114 385 SGgVAV-----IKVGGASEVEVNEKKDRIEDALNATRAAVEEG-IVPGGGVA-LLRAsklLDKLEEDNELTPDQRTGVKI 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5453603 439 YAKALRMLPTIIADNAGYDSADLVAQLRaahSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVIL 515
Cdd:PTZ00114 458 VRNALRLPTKQIAENAGVEGAVVVEKIL---EKKDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLML 531
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
24-530 |
1.38e-12 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 70.13 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 24 ARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGrdASLMVTNDGATILKNIGVDNPAAKVLVDMSR----VQDDEVGDGT 99
Cdd:PRK12850 12 ARDRLLRGVNILANAVKVTLGPKGRNVVLEKSF--GAPRITKDGVTVAKEIELEDKFENMGAQMVKevasKTNDLAGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 100 TSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVdhgsdEVKFRQDLMNIAgtTLSSklltHHKDHF 179
Cdd:PRK12850 90 TTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAK-----KVTSSKEIAQVA--TISA----NGDESI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 180 TKLAVEAVLRLKGSGnleaihIIKKLGGSLADSYLD--EGFLLDKkiG------VNQPKR----IENAKILIANtgmdtd 247
Cdd:PRK12850 159 GEMIAEAMDKVGKEG------VITVEEAKTLGTELDvvEGMQFDR--GylspyfVTNPEKmraeLEDPYILLHE------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 248 kIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKhgincfinrQLIYNypeQLFGAAGVMAIEHADF-----AGVER 322
Cdd:PRK12850 225 -KKISNLQDLLPILEAVVQSGRPLLIIAEDVEGEALA---------TLVVN---KLRGGLKSVAVKAPGFgdrrkAMLED 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 323 LALVTGGEIAS-----TFDHPELVKLGSCKLI----EEVMI----GEDKLIH---------------------------- 361
Cdd:PRK12850 292 IAVLTGGQVISedlgiKLENVTLDMLGRAKRVlitkENTTIidgaGDKKNIEarvkqiraqieettsdydreklqerlak 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 362 -FSGVALgeactIVLRGATQQILDEAERSLHDALCVLAQTVKDSrTVYGGGCSeMLMAHAVTQLANRTPGKEAVAMESYA 440
Cdd:PRK12850 372 lAGGVAV-----IRVGGATEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVA-LLRARSALRGLKGANADETAGIDIVR 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 441 KALRMLPTIIADNAGYDSADLVAQLRaahsEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNI 520
Cdd:PRK12850 445 RALEEPLRQIATNAGFEGSVVVGKVA----ELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAM 520
|
570
....*....|
gi 5453603 521 IKAAPRKRVP 530
Cdd:PRK12850 521 VAEAPKKAAA 530
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
31-531 |
2.68e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 65.92 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 31 GAIAIGDLVKSTLGPKGMDkILLSSGRDASlMVTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLA 106
Cdd:PRK12851 19 GVNILADAVKVTLGPKGRN-VVIDKSFGAP-TITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 107 AELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAvdhgsDEVKFRQDLMNIAgtTLSSklltHHKDHFTKLAVEA 186
Cdd:PRK12851 97 QAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANA-----RPVTTNAEIAQVA--TISA----NGDAEIGRLVAEA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 187 VLRLKGSGnleaihIIKKLGGSLADSYLD--EGFLLDK----KIGVNQPKR----IENAKILIANTgmdtdkiKIFGSRV 256
Cdd:PRK12851 166 MEKVGNEG------VITVEESKTAETELEvvEGMQFDRgylsPYFVTDADKmeaeLEDPYILIHEK-------KISNLQD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 257 RVDSTAKVAEIEHAEKEKMKEKVERILKhgincfinrQLIYNYPEQLFGAAGVMAIEHAD--FAGVERLALVTGGEIAS- 333
Cdd:PRK12851 233 LLPVLEAVVQSGKPLLIIAEDVEGEALA---------TLVVNKLRGGLKVAAVKAPGFGDrrKAMLEDIAILTGGTVISe 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 334 ----TFDHPELVKLGSCKLI-----EEVMIG-------------------------------EDKLIHFS-GVALgeact 372
Cdd:PRK12851 304 dlgiKLENVTLEQLGRAKKVvvekeNTTIIDgagskteiegrvaqiraqieettsdydreklQERLAKLAgGVAV----- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 373 IVLRGATQQILDEAERSLHDALCVLAQTVKDSrTVYGGGCSEMLMAHAVTQLANRTpGKEAVAMESYAKALRMLPTIIAD 452
Cdd:PRK12851 379 IRVGASTEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRAVKALDKLETAN-GDQRTGVEIVRRALEAPVRQIAE 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5453603 453 NAGYDSADLVAQLRaahsEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKRVPD 531
Cdd:PRK12851 457 NAGAEGSVVVGKLR----EKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAP 531
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
37-153 |
3.18e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 65.60 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 37 DLVKSTLGPKGMDKILLSSGrdASLMVTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLAAELLRE 112
Cdd:PRK12849 24 DAVKVTLGPKGRNVVIDKSF--GAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQALVQE 101
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 5453603 113 AESLIAKKIHPQTIIAGWREATKAAREALLSSAVD-HGSDEV 153
Cdd:PRK12849 102 GLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPvSGSEEI 143
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
14-534 |
2.73e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 62.94 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 14 AGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGrdASLMVTNDGATILKNIGVD----NPAAKVLVDMSR 89
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSF--GAPRITKDGVTVAKEIELEdkfeNMGAQMVREVAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 90 VQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSS 169
Cdd:PRK12852 80 KTNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 170 KLLTHHKDhftKLAVEAVLRLKGSGNLEA-IHIIKklGGSLADSYLDEGFLLDKKigvNQPKRIENAKILIANTgmdtdk 248
Cdd:PRK12852 160 KMIAQAMQ---KVGNEGVITVEENKSLETeVDIVE--GMKFDRGYLSPYFVTNAE---KMTVELDDAYILLHEK------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 249 iKIFGSRVRVDSTAKVAEiehaekekmKEKVERILKHGINCFINRQLIYNypeQLFGAAGVMAIEHADF-----AGVERL 323
Cdd:PRK12852 226 -KLSGLQAMLPVLEAVVQ---------SGKPLLIIAEDVEGEALATLVVN---RLRGGLKVAAVKAPGFgdrrkAMLEDI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 324 ALVTGGEIAS-----TFDHPELVKLGSCKlieEVMIGEDKLIHFSGVA-------------------------------- 366
Cdd:PRK12852 293 AILTGGQLISedlgiKLENVTLKMLGRAK---KVVIDKENTTIVNGAGkkadiearvgqikaqieettsdydreklqerl 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 367 ---LGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSrTVYGGGCSEMLMAHAVTQLANRTPGKEAvAMESYAKAL 443
Cdd:PRK12852 370 aklAGGVAVIRVGGATEVEVKEKKDRVEDALNATRAAVQEG-IVPGGGVALLRAKKAVGRINNDNADVQA-GINIVLKAL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 444 RMLPTIIADNAGYDSADLVAQLRAAHSEgntTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKA 523
Cdd:PRK12852 448 EAPIRQIAENAGVEGSIVVGKILENKSE---TFGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAE 524
|
570
....*....|.
gi 5453603 524 APRKRVPDHHP 534
Cdd:PRK12852 525 LPKKDAAPAMP 535
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
24-527 |
2.84e-10 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 62.74 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 24 ARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGrdASLMVTNDGATILKNIGVD----NPAAKVLVDMSRVQDDEVGDGT 99
Cdd:PRK14104 12 ARDRMLRGVDILANAVKVTLGPKGRNVVLDKSF--GAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKSADAAGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 100 TSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLThhkDHF 179
Cdd:PRK14104 90 TTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFLA---DAM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 180 TKLAVEAVLRLKGSGNLEaihiikklggsladSYLD--EGFLLDKkiGVNQPKRIENAKILiantGMDTDKIKIFGSRVR 257
Cdd:PRK14104 167 KKVGNEGVITVEEAKSLE--------------TELDvvEGMQFDR--GYISPYFVTNADKM----RVEMDDAYILINEKK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 258 VDSTAKVAEIEHAEKEKMKEKVerILKHGINCFINRQLIYNypeQLFGAAGVMAIEHADF-----AGVERLALVTGGEIA 332
Cdd:PRK14104 227 LSSLNELLPLLEAVVQTGKPLV--IVAEDVEGEALATLVVN---RLRGGLKVAAVKAPGFgdrrkAMLQDIAILTGGQAI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 333 S-----TFDHPELVKLGSCKlieEVMIGEDKLIHFSGVA-----------------------------------LGEACT 372
Cdd:PRK14104 302 SedlgiKLENVTLQMLGRAK---KVMIDKENTTIVNGAGkkadiearvaqikaqieettsdydreklqerlaklAGGVAV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 373 IVLRGATQQILDEAERSLHDALCVLAQTVKDSrTVYGGGCSEMLMAHAVTQLANRTPGKEAvAMESYAKALRMLPTIIAD 452
Cdd:PRK14104 379 IRVGGATEVEVKERKDRVDDAMHATRAAVEEG-IVPGGGVALLRASEQLKGIKTKNDDQKT-GVEIVRKALSAPARQIAI 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5453603 453 NAGYDSADLVAQLRaahSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRK 527
Cdd:PRK14104 457 NAGEDGSVIVGKIL---EKEQYSYGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKK 528
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
37-147 |
1.83e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 57.06 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 37 DLVKSTLGPKGMDKILLSSGrdASLMVTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLAAELLRE 112
Cdd:PRK00013 24 DAVKVTLGPKGRNVVLEKSF--GAPTITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLAQAIVRE 101
|
90 100 110
....*....|....*....|....*....|....*
gi 5453603 113 AESLIAKKIHPQTIIAGWREATKAAREALLSSAVD 147
Cdd:PRK00013 102 GLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKP 136
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
31-136 |
3.44e-08 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 56.09 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 31 GAIAIGDLVKSTLGPKGMDKILLSsgRDASLMVTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLA 106
Cdd:PLN03167 74 GVNKLADLVGVTLGPKGRNVVLES--KYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLA 151
|
90 100 110
....*....|....*....|....*....|
gi 5453603 107 AELLREAESLIAKKIHPQTIIAGWREATKA 136
Cdd:PLN03167 152 QGLIAEGVKVVAAGANPVQITRGIEKTAKA 181
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
39-135 |
3.25e-06 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 49.72 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 39 VKSTLGPKGMDKILlsSGRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRV----QDDEVGDGTTSVTVLAAELLREAE 114
Cdd:CHL00093 26 VSVTLGPKGRNVVL--EKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQaaskTNDVAGDGTTTATVLAYAIVKQGM 103
|
90 100
....*....|....*....|.
gi 5453603 115 SLIAKKIHPQTIIAGWREATK 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 |
7.48e-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: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453603 320 VERLALVTGGEIASTFDHpeLV---KLGSCKLIE-EVMIGEDK----LIHFSG--VALGeaCTIVLRGATQQILDEAERS 389
Cdd:cd03334 164 LERISRCTGADIISSMDD--LLtspKLGTCESFRvRTYVEEHGrsktLMFFEGcpKELG--CTILLRGGDLEELKKVKRV 239
|
....*....
gi 5453603 390 LHdaLCVLA 398
Cdd:cd03334 240 VE--FMVFA 246
|
|
| |
