|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
1-513 |
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: 994.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 1 AGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDD 80
Cdd:cd03336 4 DGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILQSVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 81 EVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAVDHGSDEVKFRQDLMNIAGTTLSSKLLT 160
Cdd:cd03336 84 EVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEAFREDLLNIARTTLSSKILT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 161 HHKDHFTKLAVEAVLRLKGSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFG 240
Cdd:cd03336 164 QDKEHFAELAVDAVLRLKGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQPKRIENAKILIANTPMDTDKIKIFG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 241 SRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFVGVERLALVTGGEIAS 320
Cdd:cd03336 244 AKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTGGEIAS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 321 TFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCS 400
Cdd:cd03336 324 TFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRVVLGGGCS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 401 EMLMAHAVTQLASRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTTAGLDMKEGTIGDMSVLGI 480
Cdd:cd03336 404 EMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTVGDMKELGI 483
|
490 500 510
....*....|....*....|....*....|...
4A0V_D 481 TESFQVKRQVLLSAAEAAEVILRVDNIIKAAPR 513
Cdd:cd03336 484 TESFKVKRQVLLSASEAAEMILRVDDIIKCAPR 516
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
2-513 |
0e+00 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 914.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 2 GADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSG---RDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQ 78
Cdd:PTZ00212 14 GAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMSegpRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 79 DDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAVDHGSDEVKFRQDLMNIAGTTLSSKL 158
Cdd:PTZ00212 94 DEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEKFKEDLLNIARTTLSSKL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 159 LTHHKDHFTKLAVEAVLRLKGSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKI 238
Cdd:PTZ00212 174 LTVEKDHFAKLAVDAVLRLKGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVGQPKRLENCKILVANTPMDTDKIKI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 239 FGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFVGVERLALVTGGEI 318
Cdd:PTZ00212 254 YGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 319 ASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGG 398
Cdd:PTZ00212 334 VSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKDTRVVLGGG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 399 CSEMLMAHAVTQLASRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTTAGLDMKEGTIGDMSVL 478
Cdd:PTZ00212 414 CSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGIDMEKGTVGDMKEL 493
|
490 500 510
....*....|....*....|....*....|....*
4A0V_D 479 GITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPR 513
Cdd:PTZ00212 494 GITESYKVKLSQLCSATEAAEMILRVDDIIRCAPR 528
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
1-513 |
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: 903.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 1 AGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDD 80
Cdd:TIGR02341 5 DGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 81 EVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAVDHGSDEVKFRQDLMNIAGTTLSSKLLT 160
Cdd:TIGR02341 85 EVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVKFRQDLMNIARTTLSSKILS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 161 HHKDHFTKLAVEAVLRLKGSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFG 240
Cdd:TIGR02341 165 QHKDHFAQLAVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKVKIFG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 241 SRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFVGVERLALVTGGEIAS 320
Cdd:TIGR02341 245 SRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIVS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 321 TFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCS 400
Cdd:TIGR02341 325 TFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGGGCS 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 401 EMLMAHAVTQLASRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTTAGLDMKEGTIGDMSVLGI 480
Cdd:TIGR02341 405 EMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGTIADMRQLGI 484
|
490 500 510
....*....|....*....|....*....|...
4A0V_D 481 TESFQVKRQVLLSAAEAAEVILRVDNIIKAAPR 513
Cdd:TIGR02341 485 TESYKVKRAVVSSAAEAAEVILRVDNIIKAAPR 517
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
3-509 |
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: 536.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 3 ADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEV 82
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGD--PTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 83 GDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAVDHgsdEVKFRQDLMNIAGTTLSSKLLTHH 162
Cdd:cd00309 79 GDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPI---DVEDREELLKVATTSLNSKLVSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 163 KDHFTKLAVEAVLRLKGSG---NLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTdkiki 238
Cdd:cd00309 156 DDFLGELVVDAVLKVGKENgdvDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYmPKRLENAKILLLDCKLEY----- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 239 fgsrvrvdstakvaeiehaekekmkekverilkhginCFINRQLIYNYPEQLFGAAGVMAIEHADFVGVERLALVTGGEI 318
Cdd:cd00309 231 -------------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 319 ASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGG 398
Cdd:cd00309 274 VSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 399 CSEMLMAHAVTQLASRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTTAGLDMKEGTIGDMSVL 478
Cdd:cd00309 354 AAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKEA 433
|
490 500 510
....*....|....*....|....*....|.
4A0V_D 479 GITESFQVKRQVLLSAAEAAEVILRVDNIIK 509
Cdd:cd00309 434 GIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
22-510 |
9.86e-172 |
|
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: 493.26 E-value: 9.86e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 22 IGDLVKSTLGPKGMDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAE 101
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGD--VTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 102 SLIAKKIHPQTIIAGWREATKAARQALlnSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLK--- 178
Cdd:pfam00118 79 KLLAAGVHPTTIIEGYEKALEKALEIL--DSIISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 179 GSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKI-GVNQPKRIENAKILIANTGMDTDKIKIFGSrVRVDSTAKVAEIEHA 257
Cdd:pfam00118 157 GSFDLGNIGVVKILGGSLEDSELVDGVVLDKGPlHPDMPKRLENAKVLLLNCSLEYEKTETKAT-VVLSDAEQLERFLKA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 258 EKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFVGVERLALVTGGEIASTFDHPELVKLGSCKLIE 337
Cdd:pfam00118 236 EEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 338 EVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLASRTPG 417
Cdd:pfam00118 316 EEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 418 KEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTTAGLDMKEGTIGDMSVLGITESFQVKRQVLLSAAEA 497
Cdd:pfam00118 396 KEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEA 475
|
490
....*....|...
4A0V_D 498 AEVILRVDNIIKA 510
Cdd:pfam00118 476 ASTILRIDDIIKA 488
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
2-511 |
9.03e-126 |
|
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: 376.99 E-value: 9.03e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 2 GADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDE 81
Cdd:cd03343 7 GTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGD--VTITNDGATILKEMDIEHPAAKMLVEVAKTQDEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 82 VGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAVDHGSDEVKFrqdLMNIAGTTLSSKLLTH 161
Cdd:cd03343 85 VGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDT---LRKIAKTSLTGKGAEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 162 HKDHFTKLAVEAVLRL--KGSG----NLEAIHVIKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIANTGMDTD 234
Cdd:cd03343 162 AKDKLADLVVDAVLQVaeKRDGkyvvDLDNIKIEKKTGGSVDDTELIRGIVIDKeVVHPGMPKRVENAKIALLDAPLEVK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 235 KIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFVGVERLALVT 314
Cdd:cd03343 242 KTEI-DAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 315 GGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTV 394
Cdd:cd03343 321 GAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 395 YGGGCSEMLMAHAVTQLASRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTTAGLDMKEGTIGD 474
Cdd:cd03343 401 AGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVD 480
|
490 500 510
....*....|....*....|....*....|....*..
4A0V_D 475 MSVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAA 511
Cdd:cd03343 481 MLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
2-511 |
9.88e-124 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 371.91 E-value: 9.88e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 2 GADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDE 81
Cdd:NF041082 9 GTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGD--VVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 82 VGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAVDHGSDEvkfRQDLMNIAGTTLSSKLLTH 161
Cdd:NF041082 87 VGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDD---KETLKKIAATAMTGKGAEA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 162 HKDHFTKLAVEAVLRL---KGSGN--LEAIHVIKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIANTGMDTDK 235
Cdd:NF041082 164 AKDKLADLVVDAVKAVaekDGGYNvdLDNIKVEKKVGGSIEDSELVEGVVIDKeRVHPGMPKRVENAKIALLDAPLEVKK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 236 IKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFVGVERLALVTG 315
Cdd:NF041082 244 TEI-DAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 316 GEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVY 395
Cdd:NF041082 323 ARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 396 GGGCSEMLMAHAVTQLASRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTTAGLDMKEGTIGDM 475
Cdd:NF041082 403 GGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDM 482
|
490 500 510
....*....|....*....|....*....|....*.
4A0V_D 476 SVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAA 511
Cdd:NF041082 483 LEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
2-511 |
2.52e-122 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 368.12 E-value: 2.52e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 2 GADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDE 81
Cdd:NF041083 9 GTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGD--IVITNDGATILKEMDVQHPAAKMLVEVAKTQDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 82 VGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAVDHGSDEvkfRQDLMNIAGTTLSSKLLTH 161
Cdd:NF041083 87 VGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDD---RETLKKIAETSLTSKGVEE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 162 HKDHFTKLAVEAVLRL------KGSGNLEAIHVIKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIANTGMDTD 234
Cdd:NF041083 164 ARDYLAEIAVKAVKQVaekrdgKYYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKeVVHPGMPKRVENAKIALLDAPLEVK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 235 KIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFVGVERLALVT 314
Cdd:NF041083 244 KTEI-DAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKAT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 315 GGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTV 394
Cdd:NF041083 323 GARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 395 YGGGCSEMLMAHAVTQLASRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTTAGLDMKEGTIGD 474
Cdd:NF041083 403 AGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVD 482
|
490 500 510
....*....|....*....|....*....|....*..
4A0V_D 475 MSVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAA 511
Cdd:NF041083 483 MWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
21-510 |
1.19e-121 |
|
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: 366.61 E-value: 1.19e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 21 AIGDLVKSTLGPKGMDKILLSSGRDASlmVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREA 100
Cdd:cd03340 27 AIADAVRTTLGPRGMDKLIVDGRGKVT--ISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLKEA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 101 ESLIAKKIHPQTIIAGWREATKAARQALLNSAVD-HGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKG 179
Cdd:cd03340 105 KPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNiDKEDKEEQRELLEKCAATALNSKLIASEKEFFAKMVVDAVLSLDD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 180 SGNLEAIHVIKKLGGSLADSYLDEGFLLDKKIGV----NQPKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIE 255
Cdd:cd03340 185 DLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYagfeQQPKKFKNPKILLLNVELELKAEKD-NAEVRVEDPEEYQAIV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 256 HAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMA---IEHADFvgvERLALVTGGEIASTFDHPELVKLGS 332
Cdd:cd03340 264 DAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCagrVPEEDL---KRVAQATGGSIQTTVSNITDDVLGT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 333 CKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLA 412
Cdd:cd03340 341 CGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLRDYS 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 413 SRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTT-AGLDMKEGTIGDMSVLGITESFQVKRQVL 491
Cdd:cd03340 421 RTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKwYGVDINNEGIADNFEAFVWEPSLVKINAL 500
|
490
....*....|....*....
4A0V_D 492 LSAAEAAEVILRVDNIIKA 510
Cdd:cd03340 501 TAATEAACLILSVDETIKN 519
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
2-510 |
1.47e-118 |
|
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: 358.61 E-value: 1.47e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 2 GADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDE 81
Cdd:TIGR02339 8 GTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGD--VTITNDGATILKEMDIEHPAAKMLVEVAKTQDEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 82 VGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAVDHGSDEvkfRQDLMNIAGTTLSSKLLT- 160
Cdd:TIGR02339 86 VGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPED---RDLLKKIAYTSLTSKASAe 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 161 HHKDHFTKLAVEAVLRL-------KGSGNLEAIHVIKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIANTGMD 232
Cdd:TIGR02339 163 VAKDKLADLVVEAVKQVaelrgdgKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKeVVHPGMPKRVENAKIALLDAPLE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 233 TDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFVGVERLAL 312
Cdd:TIGR02339 243 VEKTEI-DAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 313 VTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSR 392
Cdd:TIGR02339 322 ATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 393 TVYGGGCSEMLMAHAVTQLASRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTTAGLDMKEGTI 472
Cdd:TIGR02339 402 IVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTGEI 481
|
490 500 510
....*....|....*....|....*....|....*...
4A0V_D 473 GDMSVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKA 510
Cdd:TIGR02339 482 EDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
9-512 |
8.42e-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: 346.58 E-value: 8.42e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 9 ETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDASlmVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTS 88
Cdd:cd03335 7 QDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVT--ITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 89 VTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQaLLNSAVDHGSDEVKfRQDLMNIAGTTLSSKLLTHHKDHFTK 168
Cdd:cd03335 85 VVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVK-YIKEHLSISVDNLG-KESLINVAKTSMSSKIIGADSDFFAN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 169 LAVEAVLRLKGSGNL-------EAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTDKIKIfG 240
Cdd:cd03335 163 MVVDAILAVKTTNEKgktkypiKAVNILKAHGKSAKESYLVNGYALNCTRASQGmPTRVKNAKIACLDFNLQKTKMKL-G 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 241 SRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFVGVERLALVTGGEIAS 320
Cdd:cd03335 242 VQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 321 TFDHPE------LVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTV 394
Cdd:cd03335 322 TLANLEgeetfdPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 395 YGGGCSEMLMAHAVTQLASRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTTA--------GLD 466
Cdd:cd03335 402 PGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKPdkkhlkwyGLD 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
4A0V_D 467 MKEGTIGDMSVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAP 512
Cdd:cd03335 482 LINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIKLNP 527
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
2-512 |
1.67e-112 |
|
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: 343.63 E-value: 1.67e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 2 GADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDASlmVTNDGATILKNIGVDNPAAKVLVDMSRVQDDE 81
Cdd:TIGR02340 4 GGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVT--ITNDGATILKLLEVEHPAAKILVELAQLQDRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 82 VGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQaLLNSAVDHGSDEVKfRQDLMNIAGTTLSSKLLTH 161
Cdd:TIGR02340 82 VGDGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVK-YIKENLSVSVDELG-REALINVAKTSMSSKIIGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 162 HKDHFTKLAVEAVLRLKGSGN-------LEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDT 233
Cdd:TIGR02340 160 DSDFFSNIVVDAVLAVKTTNEngetkypIKAINILKAHGKSARESMLVKGYALNCTVASQQmPKRIKNAKIACLDFNLQK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 234 DKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFVGVERLALV 313
Cdd:TIGR02340 240 AKMAL-GVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 314 TGGEIASTFDHPE------LVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQT 387
Cdd:TIGR02340 319 TGATLVSTLADLEgeetfeASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 388 VKDSRTVYGGGCSEMLMAHAVTQLASRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTTA---- 463
Cdd:TIGR02340 399 LESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAQLKPekkh 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
4A0V_D 464 ----GLDMKEGTIGDMSVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAP 512
Cdd:TIGR02340 479 lkwyGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIKLNP 531
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
21-510 |
6.76e-112 |
|
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT eta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274086 [Multi-domain] Cd Length: 523 Bit Score: 341.74 E-value: 6.76e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 21 AIGDLVKSTLGPKGMDKILLSSGRDASlmVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREA 100
Cdd:TIGR02345 29 AIAEALKTTLGPRGMDKLIVGSNGKAT--ISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGELLKEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 101 ESLIAKKIHPQTIIAGWREATKAARQALLNSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGS 180
Cdd:TIGR02345 107 KPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKGEQRELLEKCAATALSSKLISHNKEFFSKMIVDAVLSLDRD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 181 G-NLEAIHVIKKLGGSLADSYLDEGFLLDKKIGV----NQPKRIENAKILIANTGMDTdKIKIFGSRVRVDSTAKVAEIE 255
Cdd:TIGR02345 187 DlDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYagfeQQPKKFANPKILLLNVELEL-KAEKDNAEIRVEDVEDYQAIV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 256 HAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFVGVERLALVTGGEIASTFDHPELVKLGSCKL 335
Cdd:TIGR02345 266 DAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTTSDLEADVLGTCAL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 336 IEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLASRT 415
Cdd:TIGR02345 346 FEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIEMELSKCLRDYSKTI 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 416 PGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTTAGLDMKEGTIGDMSVLGITESFQVKRQVLLSAA 495
Cdd:TIGR02345 426 DGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFEAFVWEPALVKINALKAAF 505
|
490
....*....|....*
4A0V_D 496 EAAEVILRVDNIIKA 510
Cdd:TIGR02345 506 EAACTILSVDETITN 520
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
11-509 |
7.11e-106 |
|
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: 7.11e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 11 ARLSSFIGAIAIGDLVKSTLGPKGMDKILLSsgRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVT 90
Cdd:cd03339 24 AHKSHILAAKSVANILRTSLGPRGMDKILVS--PDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 91 VLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALlNSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLA 170
Cdd:cd03339 102 VLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHL-EEIADKIEFSPDNKEPLIQTAMTSLGSKIVSRCHRQFAEIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 171 VEAVLRL----KGSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTDKIKIfGSRVRV 245
Cdd:cd03339 181 VDAVLSVadleRKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQmPKEVKDAKIAILTCPFEPPKPKT-KHKLDI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 246 DSTAKVAEIEHAEKEKMKEKVERILKHGINCFI---------NRQLIYNypeqlfgaaGVMAIEHADFVGVERLALVTGG 316
Cdd:cd03339 260 TSVEDYKKLQEYEQKYFREMVEQVKDAGANLVIcqwgfddeaNHLLLQN---------GLPAVRWVGGVEIELIAIATGG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 317 EIASTFDHPELVKLGSCKLIEEVMIG--EDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTV 394
Cdd:cd03339 331 RIVPRFEDLSPEKLGKAGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIV 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 395 YGGGCSEMLMAHAVTQLASRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAH-SEGKTTAGLD-MKEGTi 472
Cdd:cd03339 411 YGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPHLGIDcLGRGT- 489
|
490 500 510
....*....|....*....|....*....|....*..
4A0V_D 473 GDMSVLGITESFQVKRQVLLSAAEAAEVILRVDNIIK 509
Cdd:cd03339 490 NDMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
4-508 |
6.03e-102 |
|
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: 315.77 E-value: 6.03e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 4 DEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVG 83
Cdd:cd03338 2 DKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGE--VIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 84 DGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAVDHgsdEVKFRQDLMNIAGTTLSSKLLTHHK 163
Cdd:cd03338 80 DGTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPV---DLNDRESLIKSATTSLNSKVVSQYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 164 DHFTKLAVEAVLRL-----KGSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKI--GVNQPKRIENAKILIAN-------T 229
Cdd:cd03338 157 SLLAPIAVDAVLKVidpatATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKAskKAGGPTRIEKAKIGLIQfclsppkT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 230 GMDtdkikifgSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCF-----INRQLIYNYPEQLFGAAGVMAIEHADF 304
Cdd:cd03338 237 DMD--------NNIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLliqksILRDAVSDLALHFLAKLKIMVVKDIER 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 305 VGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVA-LGEACTIVLRGATQQILDEAERSLHDALCV 383
Cdd:cd03338 309 EEIEFICKTIGCKPVASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKnPGKTVTILVRGSNKLVLDEAERSLHDALCV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 384 LAQTVKDSRTVYGGGCSEMLMAHAVTQLASRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTTA 463
Cdd:cd03338 389 IRCLVKKRALIPGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNA 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
4A0V_D 464 GLDMKEGTIGDMSVLGITESFQVKRQVLLSAAEAAEVILRVDNII 508
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 ... |
11-509 |
2.11e-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: 304.42 E-value: 2.11e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 11 ARLSSFIGAIAIGDLVKSTLGPKGMDKILLSsgRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVT 90
Cdd:TIGR02343 28 AKKSNIAAAKSVASILRTSLGPKGMDKMLIS--PDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 91 VLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAvDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLA 170
Cdd:TIGR02343 106 VLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEIS-DEISADNNNREPLIQAAKTSLGSKIVSKCHRRFAEIA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 171 VEAVLRL----KGSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTDKIKIfGSRVRV 245
Cdd:TIGR02343 185 VDAVLNVadmeRRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQmPKEVEDAKIAILTCPFEPPKPKT-KHKLDI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 246 DSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFVGVERLALVTGGEIASTFDHP 325
Cdd:TIGR02343 264 SSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPRFQEL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 326 ELVKLGSCKLIEEVMIG--EDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEML 403
Cdd:TIGR02343 344 SKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGGGAAEIS 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 404 MAHAVTQLASRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTTA-GLD-MKEGTiGDMSVLGIT 481
Cdd:TIGR02343 424 CSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNlGVDcLGYGT-NDMKEQFVF 502
|
490 500
....*....|....*....|....*...
4A0V_D 482 ESFQVKRQVLLSAAEAAEVILRVDNIIK 509
Cdd:TIGR02343 503 ETLIGKKQQILLATQLVRMILKIDDVIS 530
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
6-508 |
5.37e-92 |
|
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: 288.81 E-value: 5.37e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 6 ERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGrdASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDG 85
Cdd:cd03337 12 ESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPM--GGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 86 TTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAVDHgsdEVKFRQDLMNIAGTTLSSKLLTHHKDH 165
Cdd:cd03337 90 TTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPV---DVNDRAQMLKIIKSCIGTKFVSRWSDL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 166 FTKLAVEAVLRLKGSGNLEAIHV-IKK-------LGGSLADSYLDEGFLLDKKigVNQPK---RIENAKILIANTGMD-- 232
Cdd:cd03337 167 MCNLALDAVKTVAVEENGRKKEIdIKRyakvekiPGGEIEDSRVLDGVMLNKD--VTHPKmrrRIENPRIVLLDCPLEyl 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 233 --TDKikifgsrvRVDSTAkvaeiEHAekekmkekverILKHGINCfINRqliynypeqlfgaagvmaIEHADFVgveRL 310
Cdd:cd03337 245 viTEK--------GVSDLA-----QHY-----------LVKAGITA-LRR------------------VRKTDNN---RI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 311 ALVTGGEIASTFDHPELVKLG-SCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVK 389
Cdd:cd03337 279 ARACGATIVNRPEELTESDVGtGAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIIL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 390 DSRTVYGGGCSEMLMAHAVTQLASRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAH-SEGKTTAGLDMK 468
Cdd:cd03337 359 NPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHaQGENSTWGIDGE 438
|
490 500 510 520
....*....|....*....|....*....|....*....|
4A0V_D 469 EGTIGDMSVLGITESFQVKRQVLLSAAEAAEVILRVDNII 508
Cdd:cd03337 439 TGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
4-511 |
3.06e-91 |
|
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: 288.22 E-value: 3.06e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 4 DEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVG 83
Cdd:TIGR02342 3 DKDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGE--VIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 84 DGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQAL--LNSAVDHGSDEVkfrqdLMNIAGTTLSSKLLTH 161
Cdd:TIGR02342 81 DGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILdeMSIPVDLSDREQ-----LLKSATTSLSSKVVSQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 162 HKDHFTKLAVEAVLRLKGSG-----NLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQ--PKRIENAKILIANTGMDTD 234
Cdd:TIGR02342 156 YSSLLAPLAVDAVLKVIDPEnaknvDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAggPTRIEKAKIGLIQFQISPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 235 KIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCF-----INRQLIYNYPEQLFGAAGVMAIEHADFVGVER 309
Cdd:TIGR02342 236 KTDM-ENQIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLliqksILRDAVNDLALHFLAKMKIMVVKDIEREEIEF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 310 LALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVA-LGEACTIVLRGATQQILDEAERSLHDALCVLAQTV 388
Cdd:TIGR02342 315 ICKTIGCKPIASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQnAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 389 KDSRTVYGGGCSEMLMAHAVTQLASRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTTAGLDMK 468
Cdd:TIGR02342 395 KKRGLIAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVR 474
|
490 500 510 520
....*....|....*....|....*....|....*....|...
4A0V_D 469 EGTIGDMSVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAA 511
Cdd:TIGR02342 475 KGGITNMLEEHVLQPLLVTTSAITLASETVRSILKIDDIVFTR 517
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
22-510 |
3.49e-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: 278.72 E-value: 3.49e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 22 IGDLVKSTLGPKGMDKILLSSGRdaSLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAE 101
Cdd:cd03341 20 LSQITRTSYGPNGMNKMVINHLE--KLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGELLEKAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 102 SLIAKKIHPQTIIAGWREATKAArQALLNSAVDHGSDEVKFRQDLMNIAGTTLSSKLLtHHKDHFTKLAVEAVLRLK--- 178
Cdd:cd03341 98 ELLRMGLHPSEIIEGYEKALKKA-LEILEELVVYKIEDLRNKEEVSKALKTAIASKQY-GNEDFLSPLVAEACISVLpen 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 179 -GSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKIgVNQPKRIENAKILIANTGMDtdkikiFGSRVRVdSTAKVAEIeha 257
Cdd:cd03341 176 iGNFNVDNIRVVKILGGSLEDSKVVRGMVFKREP-EGSVKRVKKAKVAVFSCPFD------IGVNVIV-AGGSVGDL--- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 258 ekekmkekveriLKHgincFINRqliynypeqlfgaAGVMAIEHADFVGVERLALVTGGEIASTFDHPELVKLGSCKLIE 337
Cdd:cd03341 245 ------------ALH----YCNK-------------YGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEEIGYCDSVY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 338 EVMIGEDKLIHFSGV-ALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLASRTP 416
Cdd:cd03341 296 VEEIGDTKVVVFRQNkEDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAKKLKEYGEKTP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 417 GKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTTAGLDMKEGTIG--DMSVLGITESFQVKRQVLLSA 494
Cdd:cd03341 376 GLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDEGtkDAKEAGIFDHLATKKWAIKLA 455
|
490
....*....|....*.
4A0V_D 495 AEAAEVILRVDNIIKA 510
Cdd:cd03341 456 TEAAVTVLRVDQIIMA 471
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
9-512 |
7.25e-82 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 263.09 E-value: 7.25e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 9 ETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSgrDASLMVTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGD 84
Cdd:COG0459 9 EDARRANIRGVKALADAVKVTLGPKGRNVMLVKS--FGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 85 GTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAVDhgsdeVKFRQDLMNIAGTTLSSkllthhKD 164
Cdd:COG0459 87 GTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKP-----VDDKEELAQVATISANG------DE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 165 HFTKLAVEAVLRLKGSGNLeaihVIKKLGGSLADSYLDEGFLLDKKI--------GVNQPKRIENAKILIANtgmdtDKI 236
Cdd:COG0459 156 EIGELIAEAMEKVGKDGVI----TVEEGKGLETELEVVEGMQFDKGYlspyfvtdPEKMPAELENAYILLTD-----KKI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 237 KIFGSRVrvdstaKVAEiehaekekmkekveRILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFVGV--------- 307
Cdd:COG0459 227 SSIQDLL------PLLE--------------KVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKApgfgdrrka 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 308 --ERLALVTGGEIAS-----TFDHPELVKLGSCKLIEevmIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDA 380
Cdd:COG0459 287 mlEDIAILTGGRVISedlglKLEDVTLDDLGRAKRVE---VDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 381 LCVLAQTVKDsRTVYGGGCSEMLMAHAVTQLASRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAhseGK 460
Cdd:COG0459 364 LHATRAAVEE-GIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA---KD 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
4A0V_D 461 TTAGLDMKEGTIGDMSVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAP 512
Cdd:COG0459 440 KGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKP 491
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
6-508 |
3.24e-81 |
|
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: 262.37 E-value: 3.24e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 6 ERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGrdASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDG 85
Cdd:TIGR02344 12 ESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPM--GGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 86 TTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAVDHgsdEVKFRQDLMNIAGTTLSSKLLTHHKDH 165
Cdd:TIGR02344 90 TTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPV---DVNDDAAMLKLIQSCIGTKFVSRWSDL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 166 FTKLAVEAVLRLKGSGNLEAIHVIKKL-------GGSLADSYLDEGFLLDKKigVNQPK---RIENAKILIANTGMDTDK 235
Cdd:TIGR02344 167 MCDLALDAVRTVQRDENGRKEIDIKRYakvekipGGDIEDSCVLKGVMINKD--VTHPKmrrYIENPRIVLLDCPLEYKK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 236 IKifgSRVRVDST-----AKVAEIEHaekEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFVGVERL 310
Cdd:TIGR02344 245 GE---SQTNIEITkeedwNRILQMEE---EYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 311 ALVTGGEIASTFDHPELVKLGS-CKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVK 389
Cdd:TIGR02344 319 ARACGATIVNRPEELRESDVGTgCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 390 DSRTVYGGGCSEMLMAHAVTQLASRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHS-EGKTTAGLDMK 468
Cdd:TIGR02344 399 DPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAqENNCTWGIDGE 478
|
490 500 510 520
....*....|....*....|....*....|....*....|
4A0V_D 469 EGTIGDMSVLGITESFQVKRQVLLSAAEAAEVILRVDNII 508
Cdd:TIGR02344 479 TGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
22-512 |
6.54e-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: 6.54e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 22 IGDLVKSTLGPKGMDKILLSsgRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAE 101
Cdd:TIGR02346 30 LSQITRTSLGPNGMNKMVIN--HLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGELLNKAE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 102 SLIAKKIHPQTIIAGWREATKAArQALLNSAVDHGSDEVKFRQDLMNIAGTTLSSKLLtHHKDHFTKLAVEAVLRLK--- 178
Cdd:TIGR02346 108 ELIRMGLHPSEIIKGYEMALKKA-MEILEELVVWEVKDLRDKDELIKALKASISSKQY-GNEDFLAQLVAQACSTVLpkn 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 179 -GSGNLEAIHVIKKLGGSLADSYLDEGFLLdKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSrVRVDSTAKVAEIEHA 257
Cdd:TIGR02346 186 pQNFNVDNIRVCKILGGSLSNSEVLKGMVF-NREAEGSVKSVKNAKVAVFSCPLDTATTETKGT-VLIHNAEELLNYSKG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 258 EKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFVGVERLALVTGGEIASTFDHPELVKLGSCKLIE 337
Cdd:TIGR02346 264 EENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPEEIGYVDSVY 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 338 EVMIGEDKLIHFSGV-ALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLASRTP 416
Cdd:TIGR02346 344 VSEIGGDKVTVFKQEnGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELASRLTKYGEKLP 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 417 GKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTTAGLDMKEGTIG--DMSVLGITESFQVKRQVLLSA 494
Cdd:TIGR02346 424 GLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAESDGvkDASEAGIYDMLATKKWAIKLA 503
|
490
....*....|....*...
4A0V_D 495 AEAAEVILRVDNIIKAAP 512
Cdd:TIGR02346 504 TEAAVTVLRVDQIIMAKP 521
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
18-510 |
2.35e-62 |
|
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: 211.35 E-value: 2.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 18 GAIAIGDLVKSTLGPKGMDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELL 97
Cdd:cd03342 20 AAKGLQDVLKTNLGPKGTLKMLVSGAGD--IKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGELL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 98 REAESLIAKKIHPQTIIAGWREATKAARQALlnSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRL 177
Cdd:cd03342 98 KQAERYIQEGVHPRIITEGFELAKNKALKFL--ESFKVPVEIDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 178 KGSG---NLEAIHVIKKLGGSLADSYLDEGFLLDKKI-GVNQPKRIENAKILIANTGMDTDKIKIFGSRVrvdstakvae 253
Cdd:cd03342 176 YKPDepiDLHMVEIMQMQHKSDSDTKLIRGLVLDHGArHPDMPKRVENAYILTCNVSLEYEKTEVNSGFF---------- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 254 iehaekekmkekverilkhgINCFINRQLIYNYPEQLFGAAGVMAIEHADFVGVERLALVTGGEIASTFDHPELVKLGSC 333
Cdd:cd03342 246 --------------------YSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPECLGYA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 334 KLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLAS 413
Cdd:cd03342 306 GLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHLKEFKK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 414 RTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTTAGLDMKEGTIGDMSVLGITESFQVKRQVLLS 493
Cdd:cd03342 386 SVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHS 465
|
490
....*....|....*..
4A0V_D 494 AAEAAEVILRVDNIIKA 510
Cdd:cd03342 466 ATVIASQLLLVDEIIRA 482
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
3-510 |
2.55e-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: 2.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 3 ADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDASLmvTNDGATILKNIGVDNPAAKVLVDMSRVQDDEV 82
Cdd:TIGR02347 9 AESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKL--TKDGNVLLNEMQIQHPTASMIARAATAQDDIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 83 GDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQaLLNSAVDHGSDEVKfRQDLMNIAGTTLSSKLLTHH 162
Cdd:TIGR02347 87 GDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQ-FLDKFKVKKEDEVD-REFLLNVARTSLRTKLPADL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 163 KDHFTKLAVEAVLRLKGSGNLEAIHVIKKLG---GSLADSYLDEGFLLDKkiGV---NQPKRIENAKILIANTGMDTDKI 236
Cdd:TIGR02347 165 ADQLTEIVVDAVLAIKKDGEDIDLFMVEIMEmkhKSATDTTLIRGLVLDH--GArhpDMPRRVKNAYILTCNVSLEYEKT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 237 KIFGSRVRVDSTAKVAEIEhAEKEKMKEKVERILKhgincfINRQLIYNYPEQ----------------LFGAAGVMAIE 300
Cdd:TIGR02347 243 EVNSGFFYSSAEQREKLVK-AERKFVDDRVKKIIE------LKKKVCGKSPDKgfvvinqkgidppsldLLAKEGIMALR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 301 HADFVGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDA 380
Cdd:TIGR02347 316 RAKRRNMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 381 LCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLASRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGK 460
Cdd:TIGR02347 396 LRAVKNAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGG 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
4A0V_D 461 TTAGLDMKEGTIGDMSVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKA 510
Cdd:TIGR02347 476 EVVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRA 525
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
143-390 |
3.44e-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: 202.31 E-value: 3.44e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 143 RQDLMNIAGTTLSSKLlTHHKDHFTKLAVEAVLRLKGSG---NLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKR 218
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNrmdDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYmPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 219 IENAKILIANTGMDTdkikifgsrvrvdstakvaeiehaekekmkekverilkhginCFINRQLIYNYPEQLFGAAGVMA 298
Cdd:cd03333 80 LENAKILLLDCPLEY------------------------------------------VVIAEKGIDDLALHYLAKAGIMA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 299 IEHADFVGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLH 378
Cdd:cd03333 118 VRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRSLH 197
|
250
....*....|..
4A0V_D 379 DALCVLAQTVKD 390
Cdd:cd03333 198 DALCAVRAAVEE 209
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
9-502 |
2.41e-15 |
|
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: 78.65 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 9 ETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGrdASLMVTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGD 84
Cdd:cd03344 7 EEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSF--GSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 85 GTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAVdhgsdEVKFRQDLMNIAgtTLSSklltHHKD 164
Cdd:cd03344 85 GTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSK-----PVKTKEEIAQVA--TISA----NGDE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 165 HFTKLAVEAVLRLKGSGnleAIHVikKLGGSLaDSYLD--EGFLLDKkiG------VNQPKR----IENAKILIantgmd 232
Cdd:cd03344 154 EIGELIAEAMEKVGKDG---VITV--EEGKTL-ETELEvvEGMQFDR--GylspyfVTDPEKmeveLENPYILL------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 233 TDKiKIfgsrvrvdSTAK--VAEIEHaekekmkekverILKHGINCFIN---------RQLIYNypeQLFGAAGVMAIEH 301
Cdd:cd03344 220 TDK-KI--------SSIQelLPILEL------------VAKAGRPLLIIaedvegealATLVVN---KLRGGLKVCAVKA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 302 ADFvGVER------LALVTGG-----EIASTFDHPELVKLGSCKlieEVMIGEDKLIHFSGValGEACTIVLRgaTQQIL 370
Cdd:cd03344 276 PGF-GDRRkamledIAILTGGtviseELGLKLEDVTLEDLGRAK---KVVVTKDDTTIIGGA--GDKAAIKAR--IAQIR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 371 DEAERS---------------------------------------LHDALCVLAQTVKDSrTVYGGGCSEMLMAHAVTQL 411
Cdd:cd03344 348 KQIEETtsdydkeklqerlaklsggvavikvggatevelkekkdrVEDALNATRAAVEEG-IVPGGGVALLRASPALDKL 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 412 ASRTPGkEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRaahsEGKTTAGLDMKEGTIGDMSVLGITESFQVKRQVL 491
Cdd:cd03344 427 KALNGD-EKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVL----ESPDGFGYDAATGEYVDMIEAGIIDPTKVVRSAL 501
|
570
....*....|.
4A0V_D 492 LSAAEAAEVIL 502
Cdd:cd03344 502 QNAASVASLLL 512
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
11-502 |
1.39e-12 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 69.94 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 11 ARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSgrDASLMVTNDGATILKNI----GVDNPAAKVLVDMSRVQDDEVGDGT 86
Cdd:PTZ00114 23 ARQSLLKGIERLADAVAVTLGPKGRNVIIEQE--YGSPKITKDGVTVAKAIefsdRFENVGAQLIRQVASKTNDKAGDGT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 87 TSVTVLAAELLREAESLIAKKIHPQTIIAGwreaTKAARQALLNSaVDHGSDEVKFRQDLMNIAgtTLSS-------KLL 159
Cdd:PTZ00114 101 TTATILARAIFREGCKAVAAGLNPMDLKRG----IDLAVKVVLES-LKEQSRPVKTKEDILNVA--TISAngdveigSLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 160 ThhkDHFTKLAVEAVLRLKGSGNLEaiHVIKKLGG-SLADSYLDEGFLLDKKigvNQPKRIENAKILIANTgmdtdKIKI 238
Cdd:PTZ00114 174 A---DAMDKVGKDGTITVEDGKTLE--DELEVVEGmSFDRGYISPYFVTNEK---TQKVELENPLILVTDK-----KISS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 239 FGSRVRVdstakvaeIEHAekekmkekveriLKHGINCFIN---------RQLIYNypeQLFGAAGVMAIEHADFvGVER 309
Cdd:PTZ00114 241 IQSILPI--------LEHA------------VKNKRPLLIIaedvegealQTLIIN---KLRGGLKVCAVKAPGF-GDNR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 310 ------LALVTGGEIAS------TFDHPELVKLGSCK------------------------------LIEEVMIGEDK-- 345
Cdd:PTZ00114 297 kdilqdIAVLTGATVVSednvglKLDDFDPSMLGSAKkvtvtkdetviltgggdkaeikervellrsQIERTTSEYDKek 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 346 ----LIHFSG-VALgeactIVLRGATQQILDEAERSLHDALCVLAQTVKDSrTVYGGGCSemlMAHAVTQLASRTPGKEA 420
Cdd:PTZ00114 377 lkerLAKLSGgVAV-----IKVGGASEVEVNEKKDRIEDALNATRAAVEEG-IVPGGGVA---LLRASKLLDKLEEDNEL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 421 VAMESYA-----KALRMLPTIIADNAGYDSADLVAQLRaahSEGKTTAGLDMKEGTIGDMSVLGITESFQVKRQVLLSAA 495
Cdd:PTZ00114 448 TPDQRTGvkivrNALRLPTKQIAENAGVEGAVVVEKIL---EKKDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAA 524
|
....*..
4A0V_D 496 EAAEVIL 502
Cdd:PTZ00114 525 SVASLML 531
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
11-512 |
7.80e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 64.35 E-value: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 11 ARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGrdASLMVTNDGATILKNIGVDNPAAKVLVDMSRV----QDDEVGDGT 86
Cdd:PRK12850 12 ARDRLLRGVNILANAVKVTLGPKGRNVVLEKSF--GAPRITKDGVTVAKEIELEDKFENMGAQMVKEvaskTNDLAGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 87 TSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAVdhgsdEVKFRQDLMNIAgtTLSSklltHHKDHF 166
Cdd:PRK12850 90 TTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAK-----KVTSSKEIAQVA--TISA----NGDESI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 167 TKLAVEAVLRLKGSGnleaihVIKKLGGSLADSYLD--EGFLLDKkiG------VNQPKR----IENAKILIANtgmdtd 234
Cdd:PRK12850 159 GEMIAEAMDKVGKEG------VITVEEAKTLGTELDvvEGMQFDR--GylspyfVTNPEKmraeLEDPYILLHE------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 235 kIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKhgincfinrQLIYNypeQLFGAAGVMAIEHADF-----VGVER 309
Cdd:PRK12850 225 -KKISNLQDLLPILEAVVQSGRPLLIIAEDVEGEALA---------TLVVN---KLRGGLKSVAVKAPGFgdrrkAMLED 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 310 LALVTGGEIAS-----TFDHPELVKLGSCKLI----EEVMI----GEDKLIH---------------------------- 348
Cdd:PRK12850 292 IAVLTGGQVISedlgiKLENVTLDMLGRAKRVlitkENTTIidgaGDKKNIEarvkqiraqieettsdydreklqerlak 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 349 -FSGVALgeactIVLRGATQQILDEAERSLHDALCVLAQTVKDSrTVYGGGCSeMLMAHAVTQLASRTPGKEAVAMESYA 427
Cdd:PRK12850 372 lAGGVAV-----IRVGGATEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVA-LLRARSALRGLKGANADETAGIDIVR 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 428 KALRMLPTIIADNAGYDSADLVAQLRaahsEGKTTAGLDMKEGTIGDMSVLGITESFQVKRQVLLSAAEAAEVILRVDNI 507
Cdd:PRK12850 445 RALEEPLRQIATNAGFEGSVVVGKVA----ELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAM 520
|
....*
4A0V_D 508 IKAAP 512
Cdd:PRK12850 521 VAEAP 525
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
9-140 |
1.63e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 63.29 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 9 ETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGrdASLMVTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGD 84
Cdd:PRK12849 9 EEARRALERGVNKLADAVKVTLGPKGRNVVIDKSF--GAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGD 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
4A0V_D 85 GTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAVD-HGSDEV 140
Cdd:PRK12849 87 GTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPvSGSEEI 143
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
18-512 |
2.91e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 62.45 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 18 GAIAIGDLVKSTLGPKGMDkILLSSGRDASlMVTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLA 93
Cdd:PRK12851 19 GVNILADAVKVTLGPKGRN-VVIDKSFGAP-TITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 94 AELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAvdhgsDEVKFRQDLMNIAgtTLSSklltHHKDHFTKLAVEA 173
Cdd:PRK12851 97 QAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANA-----RPVTTNAEIAQVA--TISA----NGDAEIGRLVAEA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 174 VLRLKGSGnleaihVIKKLGGSLADSYLD--EGFLLDK----KIGVNQPKR----IENAKILIANTgmdtdkiKIFGSRV 243
Cdd:PRK12851 166 MEKVGNEG------VITVEESKTAETELEvvEGMQFDRgylsPYFVTDADKmeaeLEDPYILIHEK-------KISNLQD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 244 RVDSTAKVAEIEHAEKEKMKEKVERILKhgincfinrQLIYNYPEQLFGAAGVMAIEHAD--FVGVERLALVTGGEIAS- 320
Cdd:PRK12851 233 LLPVLEAVVQSGKPLLIIAEDVEGEALA---------TLVVNKLRGGLKVAAVKAPGFGDrrKAMLEDIAILTGGTVISe 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 321 ----TFDHPELVKLGSCKLI-----EEVMIG---------------------------EDKLIHFSGVALGEACTIVLRG 364
Cdd:PRK12851 304 dlgiKLENVTLEQLGRAKKVvvekeNTTIIDgagskteiegrvaqiraqieettsdydREKLQERLAKLAGGVAVIRVGA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 365 ATQQILDEAERSLHDALCVLAQTVKDSrTVYGGGCSEMLMAHAVTQLASRTpGKEAVAMESYAKALRMLPTIIADNAGYD 444
Cdd:PRK12851 384 STEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRAVKALDKLETAN-GDQRTGVEIVRRALEAPVRQIAENAGAE 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
4A0V_D 445 SADLVAQLRaahsEGKTTAGLDMKEGTIGDMSVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAP 512
Cdd:PRK12851 462 GSVVVGKLR----EKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKP 525
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
11-513 |
5.47e-09 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 58.50 E-value: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 11 ARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGrdASLMVTNDGATILKNIGVD----NPAAKVLVDMSRVQDDEVGDGT 86
Cdd:PRK14104 12 ARDRMLRGVDILANAVKVTLGPKGRNVVLDKSF--GAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKSADAAGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 87 TSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAVDHGSDEVKFRQDLMNIAGTTLSSKLLThhkDHF 166
Cdd:PRK14104 90 TTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFLA---DAM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 167 TKLAVEAVLRLKGSGNLEaihvikklggsladSYLD--EGFLLDKkiGVNQPKRIENAKILiantGMDTDKIKIFGSRVR 244
Cdd:PRK14104 167 KKVGNEGVITVEEAKSLE--------------TELDvvEGMQFDR--GYISPYFVTNADKM----RVEMDDAYILINEKK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 245 VDSTAKVAEIEHAEKEKMKEKVerILKHGINCFINRQLIYNypeQLFGAAGVMAIEHADF-----VGVERLALVTGGEIA 319
Cdd:PRK14104 227 LSSLNELLPLLEAVVQTGKPLV--IVAEDVEGEALATLVVN---RLRGGLKVAAVKAPGFgdrrkAMLQDIAILTGGQAI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 320 S-----TFDHPELVKLGSCKlieEVMIGEDKLIHFSGVA-----------------------------------LGEACT 359
Cdd:PRK14104 302 SedlgiKLENVTLQMLGRAK---KVMIDKENTTIVNGAGkkadiearvaqikaqieettsdydreklqerlaklAGGVAV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 360 IVLRGATQQILDEAERSLHDALCVLAQTVKDSrTVYGGGCSEMLMAHAVTQLASRTPGKEAvAMESYAKALRMLPTIIAD 439
Cdd:PRK14104 379 IRVGGATEVEVKERKDRVDDAMHATRAAVEEG-IVPGGGVALLRASEQLKGIKTKNDDQKT-GVEIVRKALSAPARQIAI 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
4A0V_D 440 NAGYDSADLVAQLRaahSEGKTTAGLDMKEGTIGDMSVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPR 513
Cdd:PRK14104 457 NAGEDGSVIVGKIL---EKEQYSYGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPK 527
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-513 |
1.80e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 56.78 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 1 AGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGrdASLMVTNDGATILKNIGVD----NPAAKVLVDMSR 76
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSF--GAPRITKDGVTVAKEIELEdkfeNMGAQMVREVAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 77 VQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAvdhgsDEVKFRQDLMNIAgtTLSS 156
Cdd:PRK12852 80 KTNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRA-----KPVASSAEIAQVG--TISA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 157 klltHHKDHFTKLAVEAVLRLKGSGnleaihVIKKLGGSLADSYLD--EGFLLDKkiGVNQPKRIENAKILIAntgmDTD 234
Cdd:PRK12852 153 ----NGDAAIGKMIAQAMQKVGNEG------VITVEENKSLETEVDivEGMKFDR--GYLSPYFVTNAEKMTV----ELD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 235 KIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVerILKHGINCFINRQLIYNypeQLFGAAGVMAIEHADF-----VGVER 309
Cdd:PRK12852 217 DAYILLHEKKLSGLQAMLPVLEAVVQSGKPLL--IIAEDVEGEALATLVVN---RLRGGLKVAAVKAPGFgdrrkAMLED 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 310 LALVTGGEIAS-----TFDHPELVKLGSCKlieEVMIGEDKLIHFSGVA------------------------------- 353
Cdd:PRK12852 292 IAILTGGQLISedlgiKLENVTLKMLGRAK---KVVIDKENTTIVNGAGkkadiearvgqikaqieettsdydreklqer 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 354 ----LGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSrTVYGGGCSEMLMAHAVTQLASRTPGKEAvAMESYAKA 429
Cdd:PRK12852 369 laklAGGVAVIRVGGATEVEVKEKKDRVEDALNATRAAVQEG-IVPGGGVALLRAKKAVGRINNDNADVQA-GINIVLKA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 430 LRMLPTIIADNAGYDSADLVAQLRAAHSEgktTAGLDMKEGTIGDMSVLGITESFQVKRQVLLSAAEAAEVILRVDNIIK 509
Cdd:PRK12852 447 LEAPIRQIAENAGVEGSIVVGKILENKSE---TFGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVA 523
|
....
4A0V_D 510 AAPR 513
Cdd:PRK12852 524 ELPK 527
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
9-134 |
2.52e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 56.29 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 9 ETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGrdASLMVTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGD 84
Cdd:PRK00013 9 EDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSF--GAPTITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGD 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
4A0V_D 85 GTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAVD 134
Cdd:PRK00013 87 GTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKP 136
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
18-123 |
4.19e-08 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 55.70 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 18 GAIAIGDLVKSTLGPKGMDKILLSsgRDASLMVTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLA 93
Cdd:PLN03167 74 GVNKLADLVGVTLGPKGRNVVLES--KYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLA 151
|
90 100 110
....*....|....*....|....*....|
4A0V_D 94 AELLREAESLIAKKIHPQTIIAGWREATKA 123
Cdd:PLN03167 152 QGLIAEGVKVVAAGANPVQITRGIEKTAKA 181
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
26-122 |
3.75e-06 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 49.33 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 26 VKSTLGPKGMDKILlsSGRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRV----QDDEVGDGTTSVTVLAAELLREAE 101
Cdd:CHL00093 26 VSVTLGPKGRNVVL--EKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQaaskTNDVAGDGTTTATVLAYAIVKQGM 103
|
90 100
....*....|....*....|.
4A0V_D 102 SLIAKKIHPQTIIAGWREATK 122
Cdd:CHL00093 104 KNVAAGANPISLKRGIEKATQ 124
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
307-385 |
7.81e-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: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4A0V_D 307 VERLALVTGGEIASTFDHpeLV---KLGSCKLIE-EVMIGEDK----LIHFSG--VALGeaCTIVLRGATQQILDEAERS 376
Cdd:cd03334 164 LERISRCTGADIISSMDD--LLtspKLGTCESFRvRTYVEEHGrsktLMFFEGcpKELG--CTILLRGGDLEELKKVKRV 239
|
....*....
4A0V_D 377 LHdaLCVLA 385
Cdd:cd03334 240 VE--FMVFA 246
|
|
| |
