|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
1-480 |
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: 942.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 1 MDKILLSSGRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:cd03336 38 MDKILQSVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTII 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 81 AGWREATKAAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKKLGG 160
Cdd:cd03336 118 EGYRMATAAAREALLSSAVDHSSDEEAFREDLLNIARTTLSSKILTQDKEHFAELAVDAVLRLKGSGNLDAIQIIKKLGG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 161 SLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGI 240
Cdd:cd03336 198 SLKDSYLDEGFLLDKKIGVNQPKRIENAKILIANTPMDTDKIKIFGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 241 NCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVAL 320
Cdd:cd03336 278 NCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAA 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 321 GEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLP 400
Cdd:cd03336 358 GEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLP 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 401 TIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRK 480
Cdd:cd03336 438 TIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKCAPRK 517
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-483 |
0e+00 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 860.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 1 MDKILLSSG---RDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQ 77
Cdd:PTZ00212 47 MDKILQPMSegpRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 78 TIIAGWREATKAAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKK 157
Cdd:PTZ00212 127 TIIEGWRMALDVARKALEEIAFDHGSDEEKFKEDLLNIARTTLSSKLLTVEKDHFAKLAVDAVLRLKGSGNLDYIQIIKK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 158 LGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILK 237
Cdd:PTZ00212 207 PGGTLRDSYLEDGFILEKKIGVGQPKRLENCKILVANTPMDTDKIKIYGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 238 HGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSG 317
Cdd:PTZ00212 287 HGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 318 VALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALR 397
Cdd:PTZ00212 367 CAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALR 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 398 MLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAA 477
Cdd:PTZ00212 447 QIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRCA 526
|
....*.
gi 311771535 478 PRKRVP 483
Cdd:PTZ00212 527 PRQREQ 532
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
1-481 |
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: 845.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 1 MDKILLSSGRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:TIGR02341 39 MDKILQSSSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTII 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 81 AGWREATKAAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKKLGG 160
Cdd:TIGR02341 119 AGYREATKAARDALLKSAVDNGSDEVKFRQDLMNIARTTLSSKILSQHKDHFAQLAVDAVLRLKGSGNLEAIQIIKKLGG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 161 SLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGI 240
Cdd:TIGR02341 199 SLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKVKIFGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGI 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 241 NCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVAL 320
Cdd:TIGR02341 279 NCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 321 GEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLP 400
Cdd:TIGR02341 359 GEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLP 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 401 TIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRK 480
Cdd:TIGR02341 439 TIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPRK 518
|
.
gi 311771535 481 R 481
Cdd:TIGR02341 519 R 519
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
1-475 |
2.46e-177 |
|
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: 505.43 E-value: 2.46e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 1 MDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:cd00309 33 MDKMLVDSLGD--PTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEII 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 81 AGWREATKAAREALLSSAVDHgsdEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSG---NLEAIHIIKK 157
Cdd:cd00309 111 RGYEKAVEKALEILKEIAVPI---DVEDREELLKVATTSLNSKLVSGGDDFLGELVVDAVLKVGKENgdvDLGVIRVEKK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 158 LGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTdkikifgsrvrvdstakvaeiehaekekmkekveril 236
Cdd:cd00309 188 KGGSLEDSELVVGMVFDKGYLSPYmPKRLENAKILLLDCKLEY------------------------------------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 237 khginCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFS 316
Cdd:cd00309 231 -----VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 317 GVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKAL 396
Cdd:cd00309 306 GCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGAAEIELSKALEELAKTLPGKEQLGIEAFADAL 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 311771535 397 RMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIK 475
Cdd:cd00309 386 EVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
1-476 |
1.81e-166 |
|
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: 479.01 E-value: 1.81e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 1 MDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:pfam00118 14 MDKMLVNSGGD--VTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKLLAAGVHPTTII 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 81 AGWREATKAAREALLSsaVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLK---GSGNLEAIHIIKK 157
Cdd:pfam00118 92 EGYEKALEKALEILDS--IISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPkndGSFDLGNIGVVKI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 158 LGGSLADSYLDEGFLLDKKI-GVNQPKRIENAKILIANTGMDTDKIKIFGSrVRVDSTAKVAEIEHAEKEKMKEKVERIL 236
Cdd:pfam00118 170 LGGSLEDSELVDGVVLDKGPlHPDMPKRLENAKVLLLNCSLEYEKTETKAT-VVLSDAEQLERFLKAEEEQILEIVEKII 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 237 KHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFS 316
Cdd:pfam00118 249 DSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEKIGDEKYTFIE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 317 GVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKAL 396
Cdd:pfam00118 329 GCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGKEQLAIEAFAEAL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 397 RMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKA 476
Cdd:pfam00118 409 EVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKA 488
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
1-477 |
2.94e-119 |
|
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: 359.27 E-value: 2.94e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 1 MDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:cd03343 40 MDKMLVDSLGD--VTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVII 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 81 AGWREATKAAREALLSSAVDHGSDEVKFrqdLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRL--KGSG----NLEAIHI 154
Cdd:cd03343 118 EGYRLAAEKALELLDEIAIKVDPDDKDT---LRKIAKTSLTGKGAEAAKDKLADLVVDAVLQVaeKRDGkyvvDLDNIKI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 155 IKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVE 233
Cdd:cd03343 195 EKKTGGSVDDTELIRGIVIDKeVVHPGMPKRVENAKIALLDAPLEVKKTEI-DAKIRITSPDQLQAFLEQEEAMLKEMVD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 234 RILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLI 313
Cdd:cd03343 274 KIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 314 HFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYA 393
Cdd:cd03343 354 FVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFA 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 394 KALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNI 473
Cdd:cd03343 434 DALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDV 513
|
....
gi 311771535 474 IKAA 477
Cdd:cd03343 514 IAAK 517
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
1-477 |
5.32e-117 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 353.81 E-value: 5.32e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 1 MDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:NF041082 42 MDKMLVDSLGD--VVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 81 AGWREATKAAREALLSSAVDHGSDEvkfRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRL---KGSGN--LEAIHII 155
Cdd:NF041082 120 EGYRLAAEKALEILDEIAIKVDPDD---KETLKKIAATAMTGKGAEAAKDKLADLVVDAVKAVaekDGGYNvdLDNIKVE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 156 KKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVER 234
Cdd:NF041082 197 KKVGGSIEDSELVEGVVIDKeRVHPGMPKRVENAKIALLDAPLEVKKTEI-DAKISITDPDQLQAFLDQEEKMLKEMVDK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 235 ILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIH 314
Cdd:NF041082 276 IADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIF 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 315 FSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAK 394
Cdd:NF041082 356 VEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 395 ALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNII 474
Cdd:NF041082 436 ALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVI 515
|
...
gi 311771535 475 KAA 477
Cdd:NF041082 516 AAA 518
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
1-477 |
1.08e-114 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 347.71 E-value: 1.08e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 1 MDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:NF041083 42 MDKMLVDSLGD--IVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 81 AGWREATKAAREALLSSAVDHGSDEvkfRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRL------KGSGNLEAIHI 154
Cdd:NF041083 120 NGYRLAAEKAIEILDEIAEKVDPDD---RETLKKIAETSLTSKGVEEARDYLAEIAVKAVKQVaekrdgKYYVDLDNIQI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 155 IKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVE 233
Cdd:NF041083 197 EKKHGGSIEDTQLIYGIVIDKeVVHPGMPKRVENAKIALLDAPLEVKKTEI-DAEIRITDPDQLQKFLDQEEKMLKEMVD 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 234 RILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLI 313
Cdd:NF041083 276 KIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMV 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 314 HFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYA 393
Cdd:NF041083 356 FVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFA 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 394 KALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNI 473
Cdd:NF041083 436 EALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDV 515
|
....
gi 311771535 474 IKAA 477
Cdd:NF041083 516 IAAK 519
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
1-476 |
6.80e-114 |
|
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: 345.81 E-value: 6.80e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 1 MDKILLSSGRDASlmVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:cd03340 41 MDKLIVDGRGKVT--ISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIII 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 81 AGWREATKAAREALLSSAVD-HGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKKLG 159
Cdd:cd03340 119 RGYRKALQLAIEKIKEIAVNiDKEDKEEQRELLEKCAATALNSKLIASEKEFFAKMVVDAVLSLDDDLDLDMIGIKKVPG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 160 GSLADSYLDEGFLLDKKIGV----NQPKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERI 235
Cdd:cd03340 199 GSLEDSQLVNGVAFKKTFSYagfeQQPKKFKNPKILLLNVELELKAEKD-NAEVRVEDPEEYQAIVDAEWKIIYDKLEKI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 236 LKHGINCFINRQLIYNYPEQLFGAAGVMA---IEHADFagvERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKL 312
Cdd:cd03340 278 VKSGANVVLSKLPIGDLATQYFADRDIFCagrVPEEDL---KRVAQATGGSIQTTVSNITDDVLGTCGLFEERQVGGERY 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 313 IHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESY 392
Cdd:cd03340 355 NIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAF 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 393 AKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTT-AGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVD 471
Cdd:cd03340 435 AKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKwYGVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLILSVD 514
|
....*
gi 311771535 472 NIIKA 476
Cdd:cd03340 515 ETIKN 519
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
1-476 |
2.69e-112 |
|
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: 341.66 E-value: 2.69e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 1 MDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:TIGR02339 41 MDKMLVDSLGD--VTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVII 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 81 AGWREATKAAREALLSSAVDHGSDEvkfRQDLMNIAGTTLSSKLLT-HHKDHFTKLAVEAVLRL-------KGSGNLEAI 152
Cdd:TIGR02339 119 EGYRKAAEKALEIIDEIATKISPED---RDLLKKIAYTSLTSKASAeVAKDKLADLVVEAVKQVaelrgdgKYYVDLDNI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 153 HIIKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEK 231
Cdd:TIGR02339 196 KIVKKKGGSIEDTELVEGIVVDKeVVHPGMPKRVENAKIALLDAPLEVEKTEI-DAKIRITDPDQIKKFLDQEEAMLKEM 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 232 VERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDK 311
Cdd:TIGR02339 275 VDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVSSIDEITESDLGYAELVEERKVGEDK 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 312 LIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMES 391
Cdd:TIGR02339 355 MVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 392 YAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVD 471
Cdd:TIGR02339 435 FADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRID 514
|
....*
gi 311771535 472 NIIKA 476
Cdd:TIGR02339 515 DVIAA 519
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
1-480 |
3.82e-106 |
|
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: 326.29 E-value: 3.82e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 1 MDKILLSSGRDASlmVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:TIGR02340 37 LDKMLVDDIGDVT--ITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVIIAAELLKRADELVKNKIHPTSVI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 81 AGWR----EATKAAREALLSSAVDHGsdevkfRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGN-------L 149
Cdd:TIGR02340 115 SGYRlackEAVKYIKENLSVSVDELG------REALINVAKTSMSSKIIGLDSDFFSNIVVDAVLAVKTTNEngetkypI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 150 EAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKM 228
Cdd:TIGR02340 189 KAINILKAHGKSARESMLVKGYALNCTVASQQmPKRIKNAKIACLDFNLQKAKMAL-GVQIVVDDPEKLEQIRQREADIT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 229 KEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPE------LVKLGSCKLI 302
Cdd:TIGR02340 268 KERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVSTLADLEgeetfeASYLGFADEV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 303 EEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTP 382
Cdd:TIGR02340 348 VQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGGAVEAALSIYLENFATTLG 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 383 GKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHS--------EGNTTAGLDMREGTIGDMAILGITESFQVKR 454
Cdd:TIGR02340 428 SREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAaaqlkpekKHLKWYGLDLVNGKIRDNKEAGVLEPTVSKV 507
|
490 500
....*....|....*....|....*.
gi 311771535 455 QVLLSAAEAAEVILRVDNIIKAAPRK 480
Cdd:TIGR02340 508 KSLKFATEAAITILRIDDLIKLNPEQ 533
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
1-478 |
4.95e-106 |
|
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: 325.78 E-value: 4.95e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 1 MDKILLSSGRDASlmVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:cd03335 33 LDKMLVDDIGDVT--ITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAELLKRANELVKQKIHPTTII 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 81 AGWR----EATKAAREALLSSAVDHGsdevkfRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNL------- 149
Cdd:cd03335 111 SGYRlackEAVKYIKEHLSISVDNLG------KESLINVAKTSMSSKIIGADSDFFANMVVDAILAVKTTNEKgktkypi 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 150 EAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKM 228
Cdd:cd03335 185 KAVNILKAHGKSAKESYLVNGYALNCTRASQGmPTRVKNAKIACLDFNLQKTKMKL-GVQVVVTDPEKLEKIRQRESDIT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 229 KEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPE------LVKLGSCKLI 302
Cdd:cd03335 264 KERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVSTLANLEgeetfdPSYLGEAEEV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 303 EEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTP 382
Cdd:cd03335 344 VQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGGAVETALSIYLENFATTLG 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 383 GKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTA--------GLDMREGTIGDMAILGITESFQVKR 454
Cdd:cd03335 424 SREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKPdkkhlkwyGLDLINGKVRDNLEAGVLEPTVSKI 503
|
490 500
....*....|....*....|....
gi 311771535 455 QVLLSAAEAAEVILRVDNIIKAAP 478
Cdd:cd03335 504 KSLKFATEAAITILRIDDLIKLNP 527
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
1-476 |
3.97e-105 |
|
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: 323.25 E-value: 3.97e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 1 MDKILLSSGRDASlmVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:TIGR02345 43 MDKLIVGSNGKAT--ISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLII 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 81 AGWREATKAAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSG-NLEAIHIIKKLG 159
Cdd:TIGR02345 121 RCYREALSLAVEKIKEIAVTIDEEKGEQRELLEKCAATALSSKLISHNKEFFSKMIVDAVLSLDRDDlDLKLIGIKKVQG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 160 GSLADSYLDEGFLLDKKIGV----NQPKRIENAKILIANTGMDTdKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERI 235
Cdd:TIGR02345 201 GALEDSQLVNGVAFKKTFSYagfeQQPKKFANPKILLLNVELEL-KAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 236 LKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHF 315
Cdd:TIGR02345 280 VESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYF 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 316 SGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKA 395
Cdd:TIGR02345 360 TGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKA 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 396 LRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIK 475
Cdd:TIGR02345 440 LEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETIT 519
|
.
gi 311771535 476 A 476
Cdd:TIGR02345 520 N 520
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
1-475 |
2.66e-98 |
|
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: 305.76 E-value: 2.66e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 1 MDKILLSsgRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:cd03339 48 MDKILVS--PDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 81 AGWREATKAAREALLSSAvDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRL----KGSGNLEAIHIIK 156
Cdd:cd03339 126 DGYEQACKIAVEHLEEIA-DKIEFSPDNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAVLSVadleRKDVNFELIKVEG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 157 KLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERI 235
Cdd:cd03339 205 KVGGRLEDTKLVKGIVIDKDFSHPQmPKEVKDAKIAILTCPFEPPKPKT-KHKLDITSVEDYKKLQEYEQKYFREMVEQV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 236 LKHGINCFI---------NRQLIYNypeqlfgaaGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVM 306
Cdd:cd03339 284 KDAGANLVIcqwgfddeaNHLLLQN---------GLPAVRWVGGVEIELIAIATGGRIVPRFEDLSPEKLGKAGLVREIS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 307 IG--EDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGK 384
Cdd:cd03339 355 FGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGI 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 385 EAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAH-SEGNTTAGLD-MREGTiGDMAILGITESFQVKRQVLLSAAE 462
Cdd:cd03339 435 EQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPHLGIDcLGRGT-NDMKEQKVFETLISKKQQILLATQ 513
|
490
....*....|...
gi 311771535 463 AAEVILRVDNIIK 475
Cdd:cd03339 514 VVKMILKIDDVIV 526
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
1-474 |
5.06e-94 |
|
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: 294.19 E-value: 5.06e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 1 MDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:cd03338 33 MDKMIQTGKGE--VIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGALLSACESLLKKGIHPTVIS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 81 AGWREATKAAREALLSSAVDHgsdEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRL-----KGSGNLEAIHII 155
Cdd:cd03338 111 ESFQIAAKKAVEILDSMSIPV---DLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVidpatATNVDLKDIRIV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 156 KKLGGSLADSYLDEGFLLDKKI--GVNQPKRIENAKILIAN-------TGMDtdkikifgSRVRVDSTAKVAEIEHAEKE 226
Cdd:cd03338 188 KKLGGTIEDTELVDGLVFTQKAskKAGGPTRIEKAKIGLIQfclsppkTDMD--------NNIVVNDYAQMDRILREERK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 227 KMKEKVERILKHGINCF-----INRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKL 301
Cdd:cd03338 260 YILNMCKKIKKSGCNVLliqksILRDAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVASIDHFTEDKLGSADL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 302 IEEVMIGEDKLIHFSGVA-LGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANR 380
Cdd:cd03338 340 VEEVSLGDGKIVKITGVKnPGKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGAPEIEIALQLSEWART 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 381 TPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSA 460
Cdd:cd03338 420 LTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITNILEENVVQPLLVSTSAITLA 499
|
490
....*....|....
gi 311771535 461 AEAAEVILRVDNII 474
Cdd:cd03338 500 TETVRMILKIDDIV 513
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
1-475 |
1.16e-91 |
|
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: 288.62 E-value: 1.16e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 1 MDKILLSsgRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:TIGR02343 52 MDKMLIS--PDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 81 AGWREATKAAREALlSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRL----KGSGNLEAIHIIK 156
Cdd:TIGR02343 130 DGFEEAARIAVEHL-EEISDEISADNNNREPLIQAAKTSLGSKIVSKCHRRFAEIAVDAVLNVadmeRRDVDFDLIKVEG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 157 KLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERI 235
Cdd:TIGR02343 209 KVGGSLEDTKLIKGIIIDKDFSHPQmPKEVEDAKIAILTCPFEPPKPKT-KHKLDISSVEEYKKLQKYEQQKFKEMIDDI 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 236 LKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIG--EDKLI 313
Cdd:TIGR02343 288 KKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPRFQELSKDKLGKAGLVREISFGttKDRML 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 314 HFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYA 393
Cdd:TIGR02343 368 VIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 394 KALRMLPTIIADNAGYDSADLVAQLRAAH-SEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDN 472
Cdd:TIGR02343 448 DALETIPMALAENSGLDPIGTLSTLKSLQlKEKNPNLGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDD 527
|
...
gi 311771535 473 IIK 475
Cdd:TIGR02343 528 VIS 530
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
14-476 |
1.87e-83 |
|
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: 265.62 E-value: 1.87e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 14 LMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREA 93
Cdd:cd03341 44 LFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 94 LLSSAVdHGSDEVKFRQDLMNIAGTTLSSKLLtHHKDHFTKLAVEAVLRLK----GSGNLEAIHIIKKLGGSLADSYLDE 169
Cdd:cd03341 124 LEELVV-YKIEDLRNKEEVSKALKTAIASKQY-GNEDFLSPLVAEACISVLpeniGNFNVDNIRVVKILGGSLEDSKVVR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 170 GFLLDKKIgVNQPKRIENAKILIANTGMDtdkikiFGSRVRVdSTAKVAEIehaekekmkekveriLKHgincFINRqli 249
Cdd:cd03341 202 GMVFKREP-EGSVKRVKKAKVAVFSCPFD------IGVNVIV-AGGSVGDL---------------ALH----YCNK--- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 250 ynypeqlfgaAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGV-ALGEACTIVL 328
Cdd:cd03341 252 ----------YGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEEIGYCDSVYVEEIGDTKVVVFRQNkEDSKIATIVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 329 RGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAG 408
Cdd:cd03341 322 RGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAG 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 409 YDSADLVAQLRAAHSEGNTTAGLDMREGTIG--DMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKA 476
Cdd:cd03341 402 LDATEVLSELYAAHQKGNKSAGVDIESGDEGtkDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMA 471
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
1-477 |
1.94e-83 |
|
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: 267.03 E-value: 1.94e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 1 MDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:TIGR02342 34 MDKMIQDGKGE--VIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGALLGACERLLNKGIHPTIIS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 81 AGWREATKAAREAL--LSSAVDHGSDEVkfrqdLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSG-----NLEAIH 153
Cdd:TIGR02342 112 ESFQSAADEAIKILdeMSIPVDLSDREQ-----LLKSATTSLSSKVVSQYSSLLAPLAVDAVLKVIDPEnaknvDLNDIK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 154 IIKKLGGSLADSYLDEGFLLDKKIGVNQ--PKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEK 231
Cdd:TIGR02342 187 VVKKLGGTIDDTELIEGLVFTQKASKSAggPTRIEKAKIGLIQFQISPPKTDM-ENQIIVNDYAQMDRVLKEERAYILNI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 232 VERILKHGINCF-----INRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVM 306
Cdd:TIGR02342 266 VKKIKKTGCNVLliqksILRDAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASIDHFTADKLGSAELVEEVD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 307 IGEDKLIHFSGVA-LGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKE 385
Cdd:TIGR02342 346 SDGGKIIKITGIQnAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGAPEIEIARRLSKYARTMKGVE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 386 AVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAE 465
Cdd:TIGR02342 426 SYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITNMLEEHVLQPLLVTTSAITLASETVR 505
|
490
....*....|..
gi 311771535 466 VILRVDNIIKAA 477
Cdd:TIGR02342 506 SILKIDDIVFTR 517
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
1-474 |
3.57e-83 |
|
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: 265.31 E-value: 3.57e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 1 MDKILLSSGrdASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:cd03337 41 MLKMLLDPM--GGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVII 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 81 AGWREATKAAREAL--LSSAVDhgsdeVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHI-IKK 157
Cdd:cd03337 119 KAYRKALEDALKILeeISIPVD-----VNDRAQMLKIIKSCIGTKFVSRWSDLMCNLALDAVKTVAVEENGRKKEIdIKR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 158 -------LGGSLADSYLDEGFLLDKKigVNQPK---RIENAKILIantgmdtdkikifgsrvrVDSTakvaeIEHAEkek 227
Cdd:cd03337 194 yakvekiPGGEIEDSRVLDGVMLNKD--VTHPKmrrRIENPRIVL------------------LDCP-----LEYLV--- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 228 mkekverILKHGINcfinrQLIYNYpeqlFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLG-SCKLIEEVM 306
Cdd:cd03337 246 -------ITEKGVS-----DLAQHY----LVKAGITALRRVRKTDNNRIARACGATIVNRPEELTESDVGtGAGLFEVKK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 307 IGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEA 386
Cdd:cd03337 310 IGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 387 VAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAH-SEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAE 465
Cdd:cd03337 390 WPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHaQGENSTWGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAAC 469
|
....*....
gi 311771535 466 VILRVDNII 474
Cdd:cd03337 470 MLLRIDDIV 478
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
14-478 |
7.63e-74 |
|
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: 242.31 E-value: 7.63e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 14 LMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREA 93
Cdd:TIGR02346 54 LFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 94 LLSSAVDHGSDeVKFRQDLMNIAGTTLSSKLLtHHKDHFTKLAVEAVLRLK----GSGNLEAIHIIKKLGGSLADSYLDE 169
Cdd:TIGR02346 134 LEELVVWEVKD-LRDKDELIKALKASISSKQY-GNEDFLAQLVAQACSTVLpknpQNFNVDNIRVCKILGGSLSNSEVLK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 170 GFLLdKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSrVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRqli 249
Cdd:TIGR02346 212 GMVF-NREAEGSVKSVKNAKVAVFSCPLDTATTETKGT-VLIHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTG--- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 250 ynypeqlfGAAGVMAIEHADFAGV-----------ERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGV 318
Cdd:TIGR02346 287 --------GSVGDMALHYLNKYNImvlkipskfelRRLCKTVGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 319 -ALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALR 397
Cdd:TIGR02346 359 nGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 398 MLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIG--DMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIK 475
Cdd:TIGR02346 439 IIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAESDGvkDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIM 518
|
...
gi 311771535 476 AAP 478
Cdd:TIGR02346 519 AKP 521
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
1-480 |
1.93e-73 |
|
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: 241.18 E-value: 1.93e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 1 MDKILLSSGrdASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:TIGR02344 41 MLKMLLDPM--GGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVII 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 81 AGWREATKAAREAL--LSSAVDhgsdeVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKKL 158
Cdd:TIGR02344 119 RAYRKALDDALSVLeeISIPVD-----VNDDAAMLKLIQSCIGTKFVSRWSDLMCDLALDAVRTVQRDENGRKEIDIKRY 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 159 -------GGSLADSYLDEGFLLDKKigVNQPK---RIENAKILIANTGMDTDKIKifgSRVRVDST-----AKVAEIEHa 223
Cdd:TIGR02344 194 akvekipGGDIEDSCVLKGVMINKD--VTHPKmrrYIENPRIVLLDCPLEYKKGE---SQTNIEITkeedwNRILQMEE- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 224 ekEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGS-CKLI 302
Cdd:TIGR02344 268 --EYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACGATIVNRPEELRESDVGTgCGLF 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 303 EEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTP 382
Cdd:TIGR02344 346 EVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDPKLVPGGGATEMAVSVALTEKSKKLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 383 GKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHS-EGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAA 461
Cdd:TIGR02344 426 GVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAqENNCTWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAI 505
|
490
....*....|....*....
gi 311771535 462 EAAEVILRVDNIIKAAPRK 480
Cdd:TIGR02344 506 ESACLLLRIDDIVSGVKKK 524
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
16-480 |
2.75e-73 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 239.98 E-value: 2.75e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 16 VTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAR 91
Cdd:COG0459 48 ITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 92 EALLSSAVDhgsdeVKFRQDLMNIAGTTLSSkllthhKDHFTKLAVEAVLRLKGSGNLeaihIIKKLGGSLADSYLDEGF 171
Cdd:COG0459 128 EELKKIAKP-----VDDKEELAQVATISANG------DEEIGELIAEAMEKVGKDGVI----TVEEGKGLETELEVVEGM 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 172 LLDKKI--------GVNQPKRIENAKILIANtgmdtDKIKIFGSRVrvdstaKVAEiehaekekmkekveRILKHGINCF 243
Cdd:COG0459 193 QFDKGYlspyfvtdPEKMPAELENAYILLTD-----KKISSIQDLL------PLLE--------------KVAQSGKPLL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 244 INRQLIYNYPEQLFGAAGVMAIEHAdfAGV-------------ERLALVTGGEIAS-----TFDHPELVKLGSCKLIEev 305
Cdd:COG0459 248 IIAEDIDGEALATLVVNGIRGVLRV--VAVkapgfgdrrkamlEDIAILTGGRVISedlglKLEDVTLDDLGRAKRVE-- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 306 mIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDsRTVYGGGCSEMLMAHAVTQLANRTPGKE 385
Cdd:COG0459 324 -VDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALHATRAAVEE-GIVPGGGAALLRAARALRELAAKLEGDE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 386 AVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAhseGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAE 465
Cdd:COG0459 402 QLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA---KDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAG 478
|
490
....*....|....*
gi 311771535 466 VILRVDNIIKAAPRK 480
Cdd:COG0459 479 LILTTEAVIADKPEK 493
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
109-356 |
2.66e-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: 204.62 E-value: 2.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 109 RQDLMNIAGTTLSSKLlTHHKDHFTKLAVEAVLRLKGSG---NLEAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKR 184
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNrmdDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYmPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 185 IENAKILIANTGMDTdkikifgsrvrvdstakvaeiehaekekmkekverilkhginCFINRQLIYNYPEQLFGAAGVMA 264
Cdd:cd03333 80 LENAKILLLDCPLEY------------------------------------------VVIAEKGIDDLALHYLAKAGIMA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 265 IEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLH 344
Cdd:cd03333 118 VRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRSLH 197
|
250
....*....|..
gi 311771535 345 DALCVLAQTVKD 356
Cdd:cd03333 198 DALCAVRAAVEE 209
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
3-476 |
3.93e-58 |
|
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: 199.41 E-value: 3.93e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 3 KILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAG 82
Cdd:cd03342 39 KMLVSGAGD--IKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 83 WREATKAAREALLSSAVDhgSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSG---NLEAIHIIKKLG 159
Cdd:cd03342 117 FELAKNKALKFLESFKVP--VEIDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIYKPDepiDLHMVEIMQMQH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 160 GSLADSYLDEGFLLDKKI-GVNQPKRIENAKILIANTGMDTDKIKIFGSRVrvdstakvaeiehaekekmkekverilkh 238
Cdd:cd03342 195 KSDSDTKLIRGLVLDHGArHPDMPKRVENAYILTCNVSLEYEKTEVNSGFF----------------------------- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 239 gINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGV 318
Cdd:cd03342 246 -YSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 319 ALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRM 398
Cdd:cd03342 325 KNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLV 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311771535 399 LPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKA 476
Cdd:cd03342 405 IPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASQLLLVDEIIRA 482
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
3-481 |
1.85e-57 |
|
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: 198.80 E-value: 1.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 3 KILLSSGRDASLmvTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAG 82
Cdd:TIGR02347 43 KMLVSGAGDIKL--TKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 83 WREATKAAREaLLSSAVDHGSDEVKfRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSG---NLEAIHIIKKLG 159
Cdd:TIGR02347 121 FEIARKEALQ-FLDKFKVKKEDEVD-REFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIKKDGediDLFMVEIMEMKH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 160 GSLADSYLDEGFLLDKkiGV---NQPKRIENAKILIANTGMDTDKIKIFGSRVRVDSTAKVAEIEhAEKEKMKEKVERIL 236
Cdd:TIGR02347 199 KSATDTTLIRGLVLDH--GArhpDMPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAEQREKLVK-AERKFVDDRVKKII 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 237 KhgincfINRQLIYNYPEQ----------------LFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCK 300
Cdd:TIGR02347 276 E------LKKKVCGKSPDKgfvvinqkgidppsldLLAKEGIMALRRAKRRNMERLTLACGGEALNSVEDLTPECLGWAG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 301 LIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANR 380
Cdd:TIGR02347 350 LVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAGAFEIAAYRHLKEYKKS 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 381 TPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSA 460
Cdd:TIGR02347 430 VKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSA 509
|
490 500
....*....|....*....|.
gi 311771535 461 AEAAEVILRVDNIIKAAPRKR 481
Cdd:TIGR02347 510 TVIASQLLLVDEVMRAGRSML 530
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
16-468 |
1.02e-12 |
|
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: 70.18 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 16 VTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAR 91
Cdd:cd03344 46 ITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 92 EALLSSAVdhgsdEVKFRQDLMNIAgtTLSSklltHHKDHFTKLAVEAVLRLKGSGNleaihIIKKLGGSLaDSYLD--E 169
Cdd:cd03344 126 EELKKLSK-----PVKTKEEIAQVA--TISA----NGDEEIGELIAEAMEKVGKDGV-----ITVEEGKTL-ETELEvvE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 170 GFLLDKkiG------VNQPKR----IENAKILIantgmdTDKiKIfgsrvrvdSTAK--VAEIEHaekekmkekverILK 237
Cdd:cd03344 189 GMQFDR--GylspyfVTDPEKmeveLENPYILL------TDK-KI--------SSIQelLPILEL------------VAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 238 HGINCFIN---------RQLIYNypeQLFGAAGVMAIEHADF-----AGVERLALVTGG-----EIASTFDHPELVKLGS 298
Cdd:cd03344 240 AGRPLLIIaedvegealATLVVN---KLRGGLKVCAVKAPGFgdrrkAMLEDIAILTGGtviseELGLKLEDVTLEDLGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 299 CKlieEVMIGEDKLIHFSGValGEACTIVLRgaTQQILDEAERS------------------------------------ 342
Cdd:cd03344 317 AK---KVVVTKDDTTIIGGA--GDKAAIKAR--IAQIRKQIEETtsdydkeklqerlaklsggvavikvggatevelkek 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 343 ---LHDALCVLAQTVKDSrTVYGGGCSEMLMAHAVTQLANRTPGkEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLR 419
Cdd:cd03344 390 kdrVEDALNATRAAVEEG-IVPGGGVALLRASPALDKLKALNGD-EKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVL 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 311771535 420 AahSEGNTtaGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVIL 468
Cdd:cd03344 468 E--SPDGF--GYDAATGEYVDMIEAGIIDPTKVVRSALQNAASVASLLL 512
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
15-468 |
2.44e-09 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 59.54 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 15 MVTNDGATILKNI----GVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAA 90
Cdd:PTZ00114 59 KITKDGVTVAKAIefsdRFENVGAQLIRQVASKTNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 91 REALLSSavdhgSDEVKFRQDLMNIAgtTLSS-------KLLThhkDHFTKLAVEAVLRLKGSGNLEaiHIIKKLGG-SL 162
Cdd:PTZ00114 139 LESLKEQ-----SRPVKTKEDILNVA--TISAngdveigSLIA---DAMDKVGKDGTITVEDGKTLE--DELEVVEGmSF 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 163 ADSYLDEGFLLDKKigvNQPKRIENAKILIANTgmdtdKIKIFGSRVRVdstakvaeIEHAekekmkekveriLKHGINC 242
Cdd:PTZ00114 207 DRGYISPYFVTNEK---TQKVELENPLILVTDK-----KISSIQSILPI--------LEHA------------VKNKRPL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 243 FIN---------RQLIYNypeQLFGAAGVMAIEHADF-----AGVERLALVTGGEIAS------TFDHPELVKLGSCK-- 300
Cdd:PTZ00114 259 LIIaedvegealQTLIIN---KLRGGLKVCAVKAPGFgdnrkDILQDIAVLTGATVVSednvglKLDDFDPSMLGSAKkv 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 301 ----------------------------LIEEVMIGEDK------LIHFSG-VALgeactIVLRGATQQILDEAERSLHD 345
Cdd:PTZ00114 336 tvtkdetviltgggdkaeikervellrsQIERTTSEYDKeklkerLAKLSGgVAV-----IKVGGASEVEVNEKKDRIED 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 346 ALCVLAQTVKDSrTVYGGGCSeMLMA---HAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRaah 422
Cdd:PTZ00114 411 ALNATRAAVEEG-IVPGGGVA-LLRAsklLDKLEEDNELTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKIL--- 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 311771535 423 SEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVIL 468
Cdd:PTZ00114 486 EKKDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLML 531
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
16-483 |
3.18e-09 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 58.96 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 16 VTNDGATILKNIGVDNPAAKVLVDMSRV----QDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAR 91
Cdd:PRK12850 49 ITKDGVTVAKEIELEDKFENMGAQMVKEvaskTNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 92 EALLSSAVdhgsdEVKFRQDLMNIAgtTLSSklltHHKDHFTKLAVEAVLRLKGSGnleaihIIKKLGGSLADSYLD--E 169
Cdd:PRK12850 129 DELKKIAK-----KVTSSKEIAQVA--TISA----NGDESIGEMIAEAMDKVGKEG------VITVEEAKTLGTELDvvE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 170 GFLLDKkiG------VNQPKR----IENAKILIANtgmdtdkIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKhg 239
Cdd:PRK12850 192 GMQFDR--GylspyfVTNPEKmraeLEDPYILLHE-------KKISNLQDLLPILEAVVQSGRPLLIIAEDVEGEALA-- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 240 incfinrQLIYNypeQLFGAAGVMAIEHADF-----AGVERLALVTGGEIAS-----TFDHPELVKLGSCKLI----EEV 305
Cdd:PRK12850 261 -------TLVVN---KLRGGLKSVAVKAPGFgdrrkAMLEDIAVLTGGQVISedlgiKLENVTLDMLGRAKRVlitkENT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 306 MI----GEDKLIH-----------------------------FSGVALgeactIVLRGATQQILDEAERSLHDALCVLAQ 352
Cdd:PRK12850 331 TIidgaGDKKNIEarvkqiraqieettsdydreklqerlaklAGGVAV-----IRVGGATEVEVKEKKDRVDDALHATRA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 353 TVKDSrTVYGGGCSeMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRaahsEGNTTAGLD 432
Cdd:PRK12850 406 AVEEG-IVPGGGVA-LLRARSALRGLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVA----ELPGNFGFN 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 311771535 433 MREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKRVP 483
Cdd:PRK12850 480 AQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAAA 530
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
16-484 |
5.06e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 55.13 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 16 VTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAR 91
Cdd:PRK12851 49 ITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 92 EALLSSAvdhgsDEVKFRQDLMNIAgtTLSSklltHHKDHFTKLAVEAVLRLKGSGnleaihIIKKLGGSLADSYLD--E 169
Cdd:PRK12851 129 EELKANA-----RPVTTNAEIAQVA--TISA----NGDAEIGRLVAEAMEKVGNEG------VITVEESKTAETELEvvE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 170 GFLLDK----KIGVNQPKR----IENAKILIANTgmdtdkiKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKhgin 241
Cdd:PRK12851 192 GMQFDRgylsPYFVTDADKmeaeLEDPYILIHEK-------KISNLQDLLPVLEAVVQSGKPLLIIAEDVEGEALA---- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 242 cfinrQLIYNYPEQLFGAAGVMAIEHAD--FAGVERLALVTGGEIAS-----TFDHPELVKLGSCKLI-----EEVMIG- 308
Cdd:PRK12851 261 -----TLVVNKLRGGLKVAAVKAPGFGDrrKAMLEDIAILTGGTVISedlgiKLENVTLEQLGRAKKVvvekeNTTIIDg 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 309 ------------------------------EDKLIHFS-GVALgeactIVLRGATQQILDEAERSLHDALCVLAQTVKDS 357
Cdd:PRK12851 336 agskteiegrvaqiraqieettsdydreklQERLAKLAgGVAV-----IRVGASTEVEVKEKKDRVDDALHATRAAVEEG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 358 rTVYGGGCSEMLMAHAVTQLANRTpGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRaahsEGNTTAGLDMREGT 437
Cdd:PRK12851 411 -IVPGGGVALLRAVKALDKLETAN-GDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLR----EKPGGYGFNAATNE 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 311771535 438 IGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKRVPD 484
Cdd:PRK12851 485 YGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAP 531
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
15-106 |
1.68e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 53.66 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 15 MVTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAA 90
Cdd:PRK12849 47 TITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAV 126
|
90
....*....|....*..
gi 311771535 91 REALLSSAVD-HGSDEV 106
Cdd:PRK12849 127 VEELKALARPvSGSEEI 143
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
16-480 |
2.42e-07 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 53.11 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 16 VTNDGATILKNIGVD----NPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAR 91
Cdd:PRK14104 49 ITKDGVTVAKEIELEdkfeNMGAQMVREVASKSADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 92 EALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLThhkDHFTKLAVEAVLRLKGSGNLEaihiikklggsladSYLD--E 169
Cdd:PRK14104 129 ADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFLA---DAMKKVGNEGVITVEEAKSLE--------------TELDvvE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 170 GFLLDKkiGVNQPKRIENAKILiantGMDTDKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVerILKHGINCFINRQLI 249
Cdd:PRK14104 192 GMQFDR--GYISPYFVTNADKM----RVEMDDAYILINEKKLSSLNELLPLLEAVVQTGKPLV--IVAEDVEGEALATLV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 250 YNypeQLFGAAGVMAIEHADF-----AGVERLALVTGGEIAS-----TFDHPELVKLGSCKlieEVMIGEDKLIHFSGVA 319
Cdd:PRK14104 264 VN---RLRGGLKVAAVKAPGFgdrrkAMLQDIAILTGGQAISedlgiKLENVTLQMLGRAK---KVMIDKENTTIVNGAG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 320 -----------------------------------LGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSrTVYGGG 364
Cdd:PRK14104 338 kkadiearvaqikaqieettsdydreklqerlaklAGGVAVIRVGGATEVEVKERKDRVDDAMHATRAAVEEG-IVPGGG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 365 CSEMLMAHAVTQLANRTPGKEAvAMESYAKALRMLPTIIADNAGYDSADLVAQLRaahSEGNTTAGLDMREGTIGDMAIL 444
Cdd:PRK14104 417 VALLRASEQLKGIKTKNDDQKT-GVEIVRKALSAPARQIAINAGEDGSVIVGKIL---EKEQYSYGFDSQTGEYGNLVSK 492
|
490 500 510
....*....|....*....|....*....|....*.
gi 311771535 445 GITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRK 480
Cdd:PRK14104 493 GIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKK 528
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
16-487 |
2.45e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 53.31 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 16 VTNDGATILKNIGVD----NPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAR 91
Cdd:PRK12852 49 ITKDGVTVAKEIELEdkfeNMGAQMVREVASKTNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 92 EALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDhftKLAVEAVLRLKGSGNLEA-IHIIKklGGSLADSYLDEG 170
Cdd:PRK12852 129 KDIEKRAKPVASSAEIAQVGTISANGDAAIGKMIAQAMQ---KVGNEGVITVEENKSLETeVDIVE--GMKFDRGYLSPY 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 171 FLLDKKigvNQPKRIENAKILIANTgmdtdkiKIFGSRVRVDSTAKVAEiehaekekmKEKVERILKHGINCFINRQLIY 250
Cdd:PRK12852 204 FVTNAE---KMTVELDDAYILLHEK-------KLSGLQAMLPVLEAVVQ---------SGKPLLIIAEDVEGEALATLVV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 251 NypeQLFGAAGVMAIEHADF-----AGVERLALVTGGEIAS-----TFDHPELVKLGSCKlieEVMIGEDKLIHFSGVA- 319
Cdd:PRK12852 265 N---RLRGGLKVAAVKAPGFgdrrkAMLEDIAILTGGQLISedlgiKLENVTLKMLGRAK---KVVIDKENTTIVNGAGk 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 320 ----------------------------------LGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSrTVYGGGC 365
Cdd:PRK12852 339 kadiearvgqikaqieettsdydreklqerlaklAGGVAVIRVGGATEVEVKEKKDRVEDALNATRAAVQEG-IVPGGGV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 366 SEMLMAHAVTQLANRTPGKEAvAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEgntTAGLDMREGTIGDMAILG 445
Cdd:PRK12852 418 ALLRAKKAVGRINNDNADVQA-GINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSE---TFGFDAQTEEYVDMVAKG 493
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 311771535 446 ITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKRVPDHHP 487
Cdd:PRK12852 494 IIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDAAPAMP 535
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
16-100 |
1.55e-05 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 47.43 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 16 VTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAR 91
Cdd:PRK00013 48 ITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAV 127
|
....*....
gi 311771535 92 EALLSSAVD 100
Cdd:PRK00013 128 EELKKISKP 136
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
16-88 |
6.79e-04 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 42.01 E-value: 6.79e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 311771535 16 VTNDGATILKNIGVDNPAAKVLVDMSRV----QDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATK 88
Cdd:CHL00093 48 IVNDGVTIAKEIELEDHIENTGVALIRQaaskTNDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQ 124
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
273-351 |
7.57e-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: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771535 273 VERLALVTGGEIASTFDHpeLV---KLGSCKLIE-EVMIGEDK----LIHFSG--VALGeaCTIVLRGATQQILDEAERS 342
Cdd:cd03334 164 LERISRCTGADIISSMDD--LLtspKLGTCESFRvRTYVEEHGrsktLMFFEGcpKELG--CTILLRGGDLEELKKVKRV 239
|
....*....
gi 311771535 343 LHdaLCVLA 351
Cdd:cd03334 240 VE--FMVFA 246
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
16-89 |
1.46e-03 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 41.06 E-value: 1.46e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311771535 16 VTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKA 89
Cdd:PLN03167 104 IVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKA 181
|
|
| |
