|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
1-418 |
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: 780.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 1 MDKILLSSGRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:cd03336 38 MDKILQSVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTII 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 81 AGWREATKAAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKKLGG 160
Cdd:cd03336 118 EGYRMATAAAREALLSSAVDHSSDEEAFREDLLNIARTTLSSKILTQDKEHFAELAVDAVLRLKGSGNLDAIQIIKKLGG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 161 SLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGI 240
Cdd:cd03336 198 SLKDSYLDEGFLLDKKIGVNQPKRIENAKILIANTPMDTDKIKIFGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 241 NCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVAL 320
Cdd:cd03336 278 NCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAA 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 321 --------------------------------------------------------------GKEAVAMESYAKALRMLP 338
Cdd:cd03336 358 geactivlrgasqqildeaerslhdalcvlaqtvkdtrvvlgggcsemlmakaveelakktpGKKSLAIEAFAKALRQLP 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 339 TIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRK 418
Cdd:cd03336 438 TIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIKCAPRK 517
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
1-421 |
0e+00 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 709.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 1 MDKILLSSG---RDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQ 77
Cdd:PTZ00212 47 MDKILQPMSegpRSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 78 TIIAGWREATKAAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKK 157
Cdd:PTZ00212 127 TIIEGWRMALDVARKALEEIAFDHGSDEEKFKEDLLNIARTTLSSKLLTVEKDHFAKLAVDAVLRLKGSGNLDYIQIIKK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 158 LGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILK 237
Cdd:PTZ00212 207 PGGTLRDSYLEDGFILEKKIGVGQPKRLENCKILVANTPMDTDKIKIYGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 238 HGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSG 317
Cdd:PTZ00212 287 HGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 318 VAL--------------------------------------------------------------GKEAVAMESYAKALR 335
Cdd:PTZ00212 367 CAKgeactivlrgasthildeaerslhdalcvlsqtvkdtrvvlgggcsemlmanaveelakkveGKKSLAIEAFAKALR 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 336 MLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAA 415
Cdd:PTZ00212 447 QIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRCA 526
|
....*.
gi 119617634 416 PRKRVP 421
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 ... |
1-419 |
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: 700.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 1 MDKILLSSGRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:TIGR02341 39 MDKILQSSSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSKVQDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTII 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 81 AGWREATKAAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKKLGG 160
Cdd:TIGR02341 119 AGYREATKAARDALLKSAVDNGSDEVKFRQDLMNIARTTLSSKILSQHKDHFAQLAVDAVLRLKGSGNLEAIQIIKKLGG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 161 SLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGI 240
Cdd:TIGR02341 199 SLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKVKIFGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGI 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 241 NCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVAL 320
Cdd:TIGR02341 279 NCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 321 --------------------------------------------------------------GKEAVAMESYAKALRMLP 338
Cdd:TIGR02341 359 geactivlrgatqqildeaerslhdalcvlsqtvkesrtvlgggcsemlmskavtqeaqrtpGKEALAVEAFARALRQLP 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 339 TIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRK 418
Cdd:TIGR02341 439 TIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPRK 518
|
.
gi 119617634 419 R 419
Cdd:TIGR02341 519 R 519
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
1-413 |
4.69e-132 |
|
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: 387.94 E-value: 4.69e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 1 MDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:cd00309 33 MDKMLVDSLGD--PTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEII 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 81 AGWREATKAAREALLSSAVDHgsdEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSG---NLEAIHIIKK 157
Cdd:cd00309 111 RGYEKAVEKALEILKEIAVPI---DVEDREELLKVATTSLNSKLVSGGDDFLGELVVDAVLKVGKENgdvDLGVIRVEKK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 158 LGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTdkikifgsrvrvdstakvaeiehaekekmkekveril 236
Cdd:cd00309 188 KGGSLEDSELVVGMVFDKGYLSPYmPKRLENAKILLLDCKLEY------------------------------------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 237 khginCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFS 316
Cdd:cd00309 231 -----VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 317 GV---------------------------AL-----------------------------------GKEAVAMESYAKAL 334
Cdd:cd00309 306 GCkggkvatillrgateveldeaerslhdALcavraavedggivpgggaaeielskaleelaktlpGKEQLGIEAFADAL 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119617634 335 RMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIK 413
Cdd:cd00309 386 EVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
1-414 |
6.09e-124 |
|
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: 368.07 E-value: 6.09e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 1 MDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:pfam00118 14 MDKMLVNSGGD--VTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKLLAAGVHPTTII 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 81 AGWREATKAAREALLSsaVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLK---GSGNLEAIHIIKK 157
Cdd:pfam00118 92 EGYEKALEKALEILDS--IISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPkndGSFDLGNIGVVKI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 158 LGGSLADSYLDEGFLLDKKI-GVNQPKRIENAKILIANTGMDTDKIKIFGSrVRVDSTAKVAEIEHAEKEKMKEKVERIL 236
Cdd:pfam00118 170 LGGSLEDSELVDGVVLDKGPlHPDMPKRLENAKVLLLNCSLEYEKTETKAT-VVLSDAEQLERFLKAEEEQILEIVEKII 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 237 KHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFS 316
Cdd:pfam00118 249 DSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEKIGDEKYTFIE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 317 GV---------------------------AL-----------------------------------GKEAVAMESYAKAL 334
Cdd:pfam00118 329 GCkspkaatillrgatdhvldeiersihdALcvvknaiedprvvpgggavemelaralreyaksvsGKEQLAIEAFAEAL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 335 RMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKA 414
Cdd:pfam00118 409 EVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDIIKA 488
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
1-415 |
5.81e-89 |
|
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: 279.15 E-value: 5.81e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 1 MDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:cd03343 40 MDKMLVDSLGD--VTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVII 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 81 AGWREATKAAREALLSSAVDHGSDEVKFrqdLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRL--KGSG----NLEAIHI 154
Cdd:cd03343 118 EGYRLAAEKALELLDEIAIKVDPDDKDT---LRKIAKTSLTGKGAEAAKDKLADLVVDAVLQVaeKRDGkyvvDLDNIKI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 155 IKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVE 233
Cdd:cd03343 195 EKKTGGSVDDTELIRGIVIDKeVVHPGMPKRVENAKIALLDAPLEVKKTEI-DAKIRITSPDQLQAFLEQEEAMLKEMVD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 234 RILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLI 313
Cdd:cd03343 274 KIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 314 HFSG----------------------------------------------------VAL----------GKEAVAMESYA 331
Cdd:cd03343 354 FVEGcknpkavtillrggtehvvdeleraledalrvvadaledgkvvagggaveieLAKrlreyarsvgGREQLAVEAFA 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 332 KALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNI 411
Cdd:cd03343 434 DALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDV 513
|
....
gi 119617634 412 IKAA 415
Cdd:cd03343 514 IAAK 517
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
1-415 |
3.29e-86 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 272.14 E-value: 3.29e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 1 MDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:NF041082 42 MDKMLVDSLGD--VVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 81 AGWREATKAAREALLSSAVDHGSDEvkfRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRL---KGSGN--LEAIHII 155
Cdd:NF041082 120 EGYRLAAEKALEILDEIAIKVDPDD---KETLKKIAATAMTGKGAEAAKDKLADLVVDAVKAVaekDGGYNvdLDNIKVE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 156 KKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVER 234
Cdd:NF041082 197 KKVGGSIEDSELVEGVVIDKeRVHPGMPKRVENAKIALLDAPLEVKKTEI-DAKISITDPDQLQAFLDQEEKMLKEMVDK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 235 ILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIH 314
Cdd:NF041082 276 IADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAKATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIF 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 315 FSGV---------------------------AL-----------------------------------GKEAVAMESYAK 332
Cdd:NF041082 356 VEGCknpkavtillrggtehvvdeveraledALrvvrvvledgkvvagggapevelalrlreyaasvgGREQLAIEAFAE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 333 ALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNII 412
Cdd:NF041082 436 ALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVI 515
|
...
gi 119617634 413 KAA 415
Cdd:NF041082 516 AAA 518
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
1-415 |
5.59e-84 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 266.43 E-value: 5.59e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 1 MDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:NF041083 42 MDKMLVDSLGD--IVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 81 AGWREATKAAREALLSSAVDHGSDEvkfRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRL------KGSGNLEAIHI 154
Cdd:NF041083 120 NGYRLAAEKAIEILDEIAEKVDPDD---RETLKKIAETSLTSKGVEEARDYLAEIAVKAVKQVaekrdgKYYVDLDNIQI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 155 IKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVE 233
Cdd:NF041083 197 EKKHGGSIEDTQLIYGIVIDKeVVHPGMPKRVENAKIALLDAPLEVKKTEI-DAEIRITDPDQLQKFLDQEEKMLKEMVD 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 234 RILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLI 313
Cdd:NF041083 276 KIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMV 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 314 HFSG----------------------------------------------------VAL----------GKEAVAMESYA 331
Cdd:NF041083 356 FVEGcknpkavtilirggtehvvdeaeraledalsvvadavedgkivagggapeveLAKrlreyaatvgGREQLAVEAFA 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 332 KALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNI 411
Cdd:NF041083 436 EALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGINVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDV 515
|
....
gi 119617634 412 IKAA 415
Cdd:NF041083 516 IAAK 519
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
1-414 |
5.22e-83 |
|
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: 263.85 E-value: 5.22e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 1 MDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:TIGR02339 41 MDKMLVDSLGD--VTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVII 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 81 AGWREATKAAREALLSSAVDHGSDEvkfRQDLMNIAGTTLSSKLLT-HHKDHFTKLAVEAVLRL-------KGSGNLEAI 152
Cdd:TIGR02339 119 EGYRKAAEKALEIIDEIATKISPED---RDLLKKIAYTSLTSKASAeVAKDKLADLVVEAVKQVaelrgdgKYYVDLDNI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 153 HIIKKLGGSLADSYLDEGFLLDK-KIGVNQPKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEK 231
Cdd:TIGR02339 196 KIVKKKGGSIEDTELVEGIVVDKeVVHPGMPKRVENAKIALLDAPLEVEKTEI-DAKIRITDPDQIKKFLDQEEAMLKEM 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 232 VERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDK 311
Cdd:TIGR02339 275 VDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKLARATGARIVSSIDEITESDLGYAELVEERKVGEDK 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 312 LIHFSG----------------------------------------------------VAL----------GKEAVAMES 329
Cdd:TIGR02339 355 MVFVEGcknpkavtillrggtehvvdelersiqdalhvvanaledgkivagggaveieLALrlrsyarsvgGREQLAIEA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 330 YAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVD 409
Cdd:TIGR02339 435 FADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGINVFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRID 514
|
....*
gi 119617634 410 NIIKA 414
Cdd:TIGR02339 515 DVIAA 519
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
1-414 |
1.38e-81 |
|
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: 260.30 E-value: 1.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 1 MDKILLSSGRDASlmVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:cd03340 41 MDKLIVDGRGKVT--ISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIII 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 81 AGWREATKAAREALLSSAVD-HGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKKLG 159
Cdd:cd03340 119 RGYRKALQLAIEKIKEIAVNiDKEDKEEQRELLEKCAATALNSKLIASEKEFFAKMVVDAVLSLDDDLDLDMIGIKKVPG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 160 GSLADSYLDEGFLLDKKIGV----NQPKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERI 235
Cdd:cd03340 199 GSLEDSQLVNGVAFKKTFSYagfeQQPKKFKNPKILLLNVELELKAEKD-NAEVRVEDPEEYQAIVDAEWKIIYDKLEKI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 236 LKHGINCFINRQLIYNYPEQLFGAAGVMA---IEHADFagvERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKL 312
Cdd:cd03340 278 VKSGANVVLSKLPIGDLATQYFADRDIFCagrVPEEDL---KRVAQATGGSIQTTVSNITDDVLGTCGLFEERQVGGERY 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 313 IHFSG------------------------------------------VA--------------------LGKEAVAMESY 330
Cdd:cd03340 355 NIFTGcpkaktctiilrggaeqfieeaerslhdaimivrraikndsvVAgggaiemelskylrdysrtiAGKQQLVINAF 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 331 AKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTT-AGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVD 409
Cdd:cd03340 435 AKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKwYGVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLILSVD 514
|
....*
gi 119617634 410 NIIKA 414
Cdd:cd03340 515 ETIKN 519
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
1-418 |
7.13e-78 |
|
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: 250.79 E-value: 7.13e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 1 MDKILLSSGRDASlmVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:TIGR02340 37 LDKMLVDDIGDVT--ITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVIIAAELLKRADELVKNKIHPTSVI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 81 AGWR----EATKAAREALLSSAVDHGsdevkfRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGN-------L 149
Cdd:TIGR02340 115 SGYRlackEAVKYIKENLSVSVDELG------REALINVAKTSMSSKIIGLDSDFFSNIVVDAVLAVKTTNEngetkypI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 150 EAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKM 228
Cdd:TIGR02340 189 KAINILKAHGKSARESMLVKGYALNCTVASQQmPKRIKNAKIACLDFNLQKAKMAL-GVQIVVDDPEKLEQIRQREADIT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 229 KEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPE------LVKLGSCKLI 302
Cdd:TIGR02340 268 KERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLVSTLADLEgeetfeASYLGFADEV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 303 EEVMIGEDKLIHFSG------------------------------------------VALG------------------- 321
Cdd:TIGR02340 348 VQERIADDECILIKGtkkrksasiilrgandfmldemerslhdalcvvkrtlesnsvVPGGgaveaalsiylenfattlg 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 322 -KEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHS--------EGNTTAGLDMREGTIGDMAILGITESFQVKR 392
Cdd:TIGR02340 428 sREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAaaqlkpekKHLKWYGLDLVNGKIRDNKEAGVLEPTVSKV 507
|
490 500
....*....|....*....|....*.
gi 119617634 393 QVLLSAAEAAEVILRVDNIIKAAPRK 418
Cdd:TIGR02340 508 KSLKFATEAAITILRIDDLIKLNPEQ 533
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
1-416 |
5.47e-77 |
|
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: 248.35 E-value: 5.47e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 1 MDKILLSSGRDASlmVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:cd03335 33 LDKMLVDDIGDVT--ITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAELLKRANELVKQKIHPTTII 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 81 AGWR----EATKAAREALLSSAVDHGsdevkfRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNL------- 149
Cdd:cd03335 111 SGYRlackEAVKYIKEHLSISVDNLG------KESLINVAKTSMSSKIIGADSDFFANMVVDAILAVKTTNEKgktkypi 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 150 EAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKM 228
Cdd:cd03335 185 KAVNILKAHGKSAKESYLVNGYALNCTRASQGmPTRVKNAKIACLDFNLQKTKMKL-GVQVVVTDPEKLEKIRQRESDIT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 229 KEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPE------LVKLGSCKLI 302
Cdd:cd03335 264 KERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVSTLANLEgeetfdPSYLGEAEEV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 303 EEVMIGEDKLIHFSG--------------------------------------------------VAL------------ 320
Cdd:cd03335 344 VQERIGDDELILIKGtkkrssasiilrgandfmldemerslhdalcvvkrtlesnsvvpgggaveTALsiylenfattlg 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 321 GKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTA--------GLDMREGTIGDMAILGITESFQVKR 392
Cdd:cd03335 424 SREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKPdkkhlkwyGLDLINGKVRDNLEAGVLEPTVSKI 503
|
490 500
....*....|....*....|....
gi 119617634 393 QVLLSAAEAAEVILRVDNIIKAAP 416
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 ... |
1-414 |
5.27e-73 |
|
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: 237.73 E-value: 5.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 1 MDKILLSSGRDASlmVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:TIGR02345 43 MDKLIVGSNGKAT--ISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLII 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 81 AGWREATKAAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSG-NLEAIHIIKKLG 159
Cdd:TIGR02345 121 RCYREALSLAVEKIKEIAVTIDEEKGEQRELLEKCAATALSSKLISHNKEFFSKMIVDAVLSLDRDDlDLKLIGIKKVQG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 160 GSLADSYLDEGFLLDKKIGV----NQPKRIENAKILIANTGMDTdKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERI 235
Cdd:TIGR02345 201 GALEDSQLVNGVAFKKTFSYagfeQQPKKFANPKILLLNVELEL-KAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 236 LKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHF 315
Cdd:TIGR02345 280 VESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYF 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 316 SG-----------------------------------------VALGKEAVAME---------------------SYAKA 333
Cdd:TIGR02345 360 TGcphaktctiilrggaeqfieeaerslhdaimivrralknkkIVAGGGAIEMElskclrdysktidgkqqliinAFAKA 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 334 LRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIK 413
Cdd:TIGR02345 440 LEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETIT 519
|
.
gi 119617634 414 A 414
Cdd:TIGR02345 520 N 520
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
1-412 |
1.70e-62 |
|
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: 210.22 E-value: 1.70e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 1 MDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:cd03338 33 MDKMIQTGKGE--VIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGALLSACESLLKKGIHPTVIS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 81 AGWREATKAAREALLSSAVDHgsdEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRL-----KGSGNLEAIHII 155
Cdd:cd03338 111 ESFQIAAKKAVEILDSMSIPV---DLNDRESLIKSATTSLNSKVVSQYSSLLAPIAVDAVLKVidpatATNVDLKDIRIV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 156 KKLGGSLADSYLDEGFLLDKKI--GVNQPKRIENAKILIAN-------TGMDtdkikifgSRVRVDSTAKVAEIEHAEKE 226
Cdd:cd03338 188 KKLGGTIEDTELVDGLVFTQKAskKAGGPTRIEKAKIGLIQfclsppkTDMD--------NNIVVNDYAQMDRILREERK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 227 KMKEKVERILKHGINCF-----INRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKL 301
Cdd:cd03338 260 YILNMCKKIKKSGCNVLliqksILRDAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVASIDHFTEDKLGSADL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 302 IEEVMIGEDKLIHFSGV----------------------------AL--------------------------------- 320
Cdd:cd03338 340 VEEVSLGDGKIVKITGVknpgktvtilvrgsnklvldeaerslhdALcvirclvkkralipgggapeieialqlsewart 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 321 --GKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSA 398
Cdd:cd03338 420 ltGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGINVRKGAITNILEENVVQPLLVSTSAITLA 499
|
490
....*....|....
gi 119617634 399 AEAAEVILRVDNII 412
Cdd:cd03338 500 TETVRMILKIDDIV 513
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
1-413 |
4.47e-61 |
|
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: 206.38 E-value: 4.47e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 1 MDKILLSsgRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:cd03339 48 MDKILVS--PDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 81 AGWREATKAAREALLSSAvDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRL----KGSGNLEAIHIIK 156
Cdd:cd03339 126 DGYEQACKIAVEHLEEIA-DKIEFSPDNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAVLSVadleRKDVNFELIKVEG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 157 KLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERI 235
Cdd:cd03339 205 KVGGRLEDTKLVKGIVIDKDFSHPQmPKEVKDAKIAILTCPFEPPKPKT-KHKLDITSVEDYKKLQEYEQKYFREMVEQV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 236 LKHGINCFI---------NRQLIYNypeqlfgaaGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVM 306
Cdd:cd03339 284 KDAGANLVIcqwgfddeaNHLLLQN---------GLPAVRWVGGVEIELIAIATGGRIVPRFEDLSPEKLGKAGLVREIS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 307 IG--EDKLIHFSG------------------------------------------------------VALGKEAV----- 325
Cdd:cd03339 355 FGttKDKMLVIEGcpnskavtifirggnkmiieeakrslhdalcvvrnlirdnrivygggaaeiscsLAVEKAADkcsgi 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 326 ---AMESYAKALRMLPTIIADNAGYDSADLVAQLRAAH-SEGNTTAGLD-MREGTiGDMAILGITESFQVKRQVLLSAAE 400
Cdd:cd03339 435 eqyAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPHLGIDcLGRGT-NDMKEQKVFETLISKKQQILLATQ 513
|
490
....*....|...
gi 119617634 401 AAEVILRVDNIIK 413
Cdd:cd03339 514 VVKMILKIDDVIV 526
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
1-413 |
3.46e-55 |
|
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: 191.17 E-value: 3.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 1 MDKILLSsgRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:TIGR02343 52 MDKMLIS--PDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 81 AGWREATKAAREAlLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRL----KGSGNLEAIHIIK 156
Cdd:TIGR02343 130 DGFEEAARIAVEH-LEEISDEISADNNNREPLIQAAKTSLGSKIVSKCHRRFAEIAVDAVLNVadmeRRDVDFDLIKVEG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 157 KLGGSLADSYLDEGFLLDKKIGVNQ-PKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEKVERI 235
Cdd:TIGR02343 209 KVGGSLEDTKLIKGIIIDKDFSHPQmPKEVEDAKIAILTCPFEPPKPKT-KHKLDISSVEEYKKLQKYEQQKFKEMIDDI 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 236 LKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIG------- 308
Cdd:TIGR02343 288 KKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPRFQELSKDKLGKAGLVREISFGttkdrml 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 309 -----------------------------------------EDKLIHFSG--------VALGKEA--------VAMESYA 331
Cdd:TIGR02343 368 vieqcknskavtifirggnkmiieeakrsihdalcvvrnliKDSRIVYGGgaaeiscsLAVSQEAdkypgveqYAIRAFA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 332 KALRMLPTIIADNAGYDSADLVAQLRAAH-SEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDN 410
Cdd:TIGR02343 448 DALETIPMALAENSGLDPIGTLSTLKSLQlKEKNPNLGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDD 527
|
...
gi 119617634 411 IIK 413
Cdd:TIGR02343 528 VIS 530
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
1-415 |
3.56e-54 |
|
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: 188.07 E-value: 3.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 1 MDKILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:TIGR02342 34 MDKMIQDGKGE--VIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGALLGACERLLNKGIHPTIIS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 81 AGWREATKAAREAL--LSSAVDHGSDEVkfrqdLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSG-----NLEAIH 153
Cdd:TIGR02342 112 ESFQSAADEAIKILdeMSIPVDLSDREQ-----LLKSATTSLSSKVVSQYSSLLAPLAVDAVLKVIDPEnaknvDLNDIK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 154 IIKKLGGSLADSYLDEGFLLDKKIGVNQ--PKRIENAKILIANTGMDTDKIKIfGSRVRVDSTAKVAEIEHAEKEKMKEK 231
Cdd:TIGR02342 187 VVKKLGGTIDDTELIEGLVFTQKASKSAggPTRIEKAKIGLIQFQISPPKTDM-ENQIIVNDYAQMDRVLKEERAYILNI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 232 VERILKHGINCF-----INRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVM 306
Cdd:TIGR02342 266 VKKIKKTGCNVLliqksILRDAVNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIASIDHFTADKLGSAELVEEVD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 307 IGEDKLIHFSGVA-------------------------------------------------------LGKEAVAME--- 328
Cdd:TIGR02342 346 SDGGKIIKITGIQnagktvtvvvrgsnklvideaerslhdalcvirclvkkrgliagggapeieiarrLSKYARTMKgve 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 329 -----SYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAE 403
Cdd:TIGR02342 426 sycvrAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVRKGGITNMLEEHVLQPLLVTTSAITLASETVR 505
|
490
....*....|..
gi 119617634 404 VILRVDNIIKAA 415
Cdd:TIGR02342 506 SILKIDDIVFTR 517
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
16-418 |
1.53e-49 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 175.27 E-value: 1.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 16 VTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAR 91
Cdd:COG0459 48 ITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 92 EALLSSAVDhgsdeVKFRQDLMNIAGTTLSSkllthhKDHFTKLAVEAVLRLKGSGNLeaihIIKKLGGSLADSYLDEGF 171
Cdd:COG0459 128 EELKKIAKP-----VDDKEELAQVATISANG------DEEIGELIAEAMEKVGKDGVI----TVEEGKGLETELEVVEGM 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 172 LLDKKI--------GVNQPKRIENAKILIANtgmdtDKIKIFGSRVrvdstaKVAEiehaekekmkekveRILKHGINCF 243
Cdd:COG0459 193 QFDKGYlspyfvtdPEKMPAELENAYILLTD-----KKISSIQDLL------PLLE--------------KVAQSGKPLL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 244 INRQLIYNYPEQLFGAAGVMAIEHAdfAGV-------------ERLALVTGGEIAS-----TFDHPELVKLGSCKLIEE- 304
Cdd:COG0459 248 IIAEDIDGEALATLVVNGIRGVLRV--VAVkapgfgdrrkamlEDIAILTGGRVISedlglKLEDVTLDDLGRAKRVEVd 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 305 -----------------VMIG-------------------------EDKLIHFSGVAL---------------GKEAVAM 327
Cdd:COG0459 326 kdnttivegagnpkaivILVGaatevevkerkrrvedalhatraavEEGIVPGGGAALlraaralrelaakleGDEQLGI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 328 ESYAKALRMLPTIIADNAGYDSADLVAQLRAAhseGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILR 407
Cdd:COG0459 406 EIVARALEAPLRQIAENAGLDGSVVVEKVRAA---KDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILT 482
|
490
....*....|.
gi 119617634 408 VDNIIKAAPRK 418
Cdd:COG0459 483 TEAVIADKPEK 493
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
14-414 |
2.23e-49 |
|
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: 174.33 E-value: 2.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 14 LMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREA 93
Cdd:cd03341 44 LFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGELLEKAEELLRMGLHPSEIIEGYEKALKKALEI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 94 LLSSAVdHGSDEVKFRQDLMNIAGTTLSSKLLtHHKDHFTKLAVEAVLRLK----GSGNLEAIHIIKKLGGSLADSYLDE 169
Cdd:cd03341 124 LEELVV-YKIEDLRNKEEVSKALKTAIASKQY-GNEDFLSPLVAEACISVLpeniGNFNVDNIRVVKILGGSLEDSKVVR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 170 GFLLDKKIgVNQPKRIENAKILIANTGMDtdkikiFGSRVRVdSTAKVAEiehaekekmkekverILKHgincFINRqli 249
Cdd:cd03341 202 GMVFKREP-EGSVKRVKKAKVAVFSCPFD------IGVNVIV-AGGSVGD---------------LALH----YCNK--- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 250 ynypeqlfgaAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHF-------------- 315
Cdd:cd03341 252 ----------YGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEEIGYCDSVYVEEIGDTKVVVFrqnkedskiativl 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 316 ----------------SGVALGKEAV---------------------------------AMESYAKALRMLPTIIADNAG 346
Cdd:cd03341 322 rgatqnilddveraidDGVNVFKSLTkdgrfvpgagateielakklkeygektpgleqyAIKKFAEAFEVVPRTLAENAG 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 347 YDSADLVAQLRAAHSEGNTTAGLDMREGTIG--DMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKA 414
Cdd:cd03341 402 LDATEVLSELYAAHQKGNKSAGVDIESGDEGtkDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQIIMA 471
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
1-412 |
1.33e-48 |
|
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: 172.09 E-value: 1.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 1 MDKILLSSGrdASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:cd03337 41 MLKMLLDPM--GGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVII 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 81 AGWREATKAAREAL--LSSAVDhgsdeVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHI-IKK 157
Cdd:cd03337 119 KAYRKALEDALKILeeISIPVD-----VNDRAQMLKIIKSCIGTKFVSRWSDLMCNLALDAVKTVAVEENGRKKEIdIKR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 158 -------LGGSLADSYLDEGFLLDKKigVNQPK---RIENAKILIANTGMD----TDKikifgsrvRVDSTAkvaeiEHA 223
Cdd:cd03337 194 yakvekiPGGEIEDSRVLDGVMLNKD--VTHPKmrrRIENPRIVLLDCPLEylviTEK--------GVSDLA-----QHY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 224 ekekmkekverILKHGINCF-------INR------QLIYNYPEQL----FGAAGVMaiEHADFAGVERLALVTG----- 281
Cdd:cd03337 259 -----------LVKAGITALrrvrktdNNRiaracgATIVNRPEELtesdVGTGAGL--FEVKKIGDEYFTFITEckdpk 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 282 --------------GEIA-----------STFDHPELVKLGSCKlieEVMIGEdKLIHFSGVALGKEAVAMESYAKALRM 336
Cdd:cd03337 326 actillrgaskdvlNEVErnlqdamavarNIILNPKLVPGGGAT---EMAVSH-ALSEKAKSIEGVEQWPYKAVASALEV 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119617634 337 LPTIIADNAGYDSADLVAQLRAAH-SEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNII 412
Cdd:cd03337 402 IPRTLAQNCGANVIRTLTELRAKHaQGENSTWGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
1-418 |
6.56e-44 |
|
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: 160.67 E-value: 6.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 1 MDKILLSSGrdASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTII 80
Cdd:TIGR02344 41 MLKMLLDPM--GGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVII 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 81 AGWREATKAAREAL--LSSAVDhgsdeVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKKL 158
Cdd:TIGR02344 119 RAYRKALDDALSVLeeISIPVD-----VNDDAAMLKLIQSCIGTKFVSRWSDLMCDLALDAVRTVQRDENGRKEIDIKRY 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 159 -------GGSLADSYLDEGFLLDKKigVNQPK---RIENAKILIANTGMDTDKIKifgSRVRVDST-----AKVAEIEHa 223
Cdd:TIGR02344 194 akvekipGGDIEDSCVLKGVMINKD--VTHPKmrrYIENPRIVLLDCPLEYKKGE---SQTNIEITkeedwNRILQMEE- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 224 ekEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGS-CKLI 302
Cdd:TIGR02344 268 --EYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIARACGATIVNRPEELRESDVGTgCGLF 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 303 EEVMIGED-----------------------------------------------KLIHFSG-------VALGKEAVAME 328
Cdd:TIGR02344 346 EVKKIGDEyftfiteckdpkactillrgaskdilnevernlqdamavarnvlldpKLVPGGGatemavsVALTEKSKKLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 329 --------SYAKALRMLPTIIADNAGYDSADLVAQLRAAHS-EGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAA 399
Cdd:TIGR02344 426 gveqwpyrAVADALEIIPRTLAQNCGANVIRTLTELRAKHAqENNCTWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAI 505
|
490
....*....|....*....
gi 119617634 400 EAAEVILRVDNIIKAAPRK 418
Cdd:TIGR02344 506 ESACLLLRIDDIVSGVKKK 524
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
109-322 |
2.05e-42 |
|
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: 148.38 E-value: 2.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 109 RQDLMNIAGTTLSSKLlTHHKDHFTKLAVEAVLRLKGSG---NLEAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQ-PKR 184
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNrmdDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYmPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 185 IENAKILIANTGMDTdkikifgsrvrvdstakvaeiehaekekmkekverilkhginCFINRQLIYNYPEQLFGAAGVMA 264
Cdd:cd03333 80 LENAKILLLDCPLEY------------------------------------------VVIAEKGIDDLALHYLAKAGIMA 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 119617634 265 IEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGK 322
Cdd:cd03333 118 VRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGK 175
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
14-416 |
2.52e-42 |
|
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: 156.41 E-value: 2.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 14 LMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREA 93
Cdd:TIGR02346 54 LFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 94 LLSSAVDHGSDeVKFRQDLMNIAGTTLSSKLLtHHKDHFTKLAVEAVLRLK----GSGNLEAIHIIKKLGGSLADSYLDE 169
Cdd:TIGR02346 134 LEELVVWEVKD-LRDKDELIKALKASISSKQY-GNEDFLAQLVAQACSTVLpknpQNFNVDNIRVCKILGGSLSNSEVLK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 170 GFLLdKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSrVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLI 249
Cdd:TIGR02346 212 GMVF-NREAEGSVKSVKNAKVAVFSCPLDTATTETKGT-VLIHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSV 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 250 YNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFS------------- 316
Cdd:TIGR02346 290 GDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKqengdskistiil 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 317 -----------------GVALGKEAV---------------------------------AMESYAKALRMLPTIIADNAG 346
Cdd:TIGR02346 370 rgstdnllddieraiddGVNTVKALVkdgrllpgagateielasrltkygeklpgldqyAIKKFAEAFEIIPRTLAENAG 449
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119617634 347 YDSADLVAQLRAAHSEGNTTAGLDMREGTIG--DMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAP 416
Cdd:TIGR02346 450 LNANEVIPKLYAAHKKGNKSKGIDIEAESDGvkDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKP 521
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
3-414 |
3.95e-42 |
|
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: 154.72 E-value: 3.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 3 KILLSSGRDasLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAG 82
Cdd:cd03342 39 KMLVSGAGD--IKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 83 WREATKAAREALLSSAVDhgSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSG---NLEAIHIIKKLG 159
Cdd:cd03342 117 FELAKNKALKFLESFKVP--VEIDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAIYKPDepiDLHMVEIMQMQH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 160 GSLADSYLDEGFLLDKKI-GVNQPKRIENAKILIANTGMDTDKIKIFGSRVrvdstakvaeiehaekekmkekverilkh 238
Cdd:cd03342 195 KSDSDTKLIRGLVLDHGArHPDMPKRVENAYILTCNVSLEYEKTEVNSGFF----------------------------- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 239 gINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDK------- 311
Cdd:cd03342 246 -YSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPECLGYAGLVYERTLGEEKytfiegv 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 312 -------------------------------------------------------LIHFSGVALGKEAVAMESYAKALRM 336
Cdd:cd03342 325 knpksctilikgpndhtitqikdairdglravknaiedkcvvpgagafevalyahLKEFKKSVKGKAKLGVQAFADALLV 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119617634 337 LPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKA 414
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 ... |
3-419 |
3.79e-41 |
|
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: 152.97 E-value: 3.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 3 KILLSSGRDASLmvTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAG 82
Cdd:TIGR02347 43 KMLVSGAGDIKL--TKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 83 WREATKAAREaLLSSAVDHGSDEVKfRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSG---NLEAIHIIKKLG 159
Cdd:TIGR02347 121 FEIARKEALQ-FLDKFKVKKEDEVD-REFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIKKDGediDLFMVEIMEMKH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 160 GSLADSYLDEGFLLDKkiGV---NQPKRIENAKILIANTGMDTDKIKIFGSRV--RVDSTAKVAEIEH----AEKEKMKE 230
Cdd:TIGR02347 199 KSATDTTLIRGLVLDH--GArhpDMPRRVKNAYILTCNVSLEYEKTEVNSGFFysSAEQREKLVKAERkfvdDRVKKIIE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 231 KVERILKHGIN---CFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMI 307
Cdd:TIGR02347 277 LKKKVCGKSPDkgfVVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEALNSVEDLTPECLGWAGLVYETTI 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 308 GEDK--------------------------------------------------------------LIHFSGVALGKEAV 325
Cdd:TIGR02347 357 GEEKytfieecknpksctilikgpndhtiaqikdavrdglravknaiedkcvvpgagafeiaayrhLKEYKKSVKGKAKL 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 326 AMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVI 405
Cdd:TIGR02347 437 GVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEGGEVVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQL 516
|
490
....*....|....
gi 119617634 406 LRVDNIIKAAPRKR 419
Cdd:TIGR02347 517 LLVDEVMRAGRSML 530
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
16-204 |
2.00e-10 |
|
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: 62.47 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 16 VTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAR 91
Cdd:cd03344 46 ITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 92 EALLSSAVdhgsdEVKFRQDLMNIAgtTLSSklltHHKDHFTKLAVEAVLRLKGSGNleaihIIKKLGGSLaDSYLD--E 169
Cdd:cd03344 126 EELKKLSK-----PVKTKEEIAQVA--TISA----NGDEEIGELIAEAMEKVGKDGV-----ITVEEGKTL-ETELEvvE 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 119617634 170 GFLLDKkiG------VNQPKR----IENAKILIantgmdTDKiKI 204
Cdd:cd03344 189 GMQFDR--GylspyfVTDPEKmeveLENPYILL------TDK-KI 224
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
15-106 |
1.42e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 53.66 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 15 MVTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAA 90
Cdd:PRK12849 47 TITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAV 126
|
90
....*....|....*..
gi 119617634 91 REALLSSAVD-HGSDEV 106
Cdd:PRK12849 127 VEELKALARPvSGSEEI 143
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
15-195 |
5.51e-07 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 51.84 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 15 MVTNDGATILKNI----GVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAA 90
Cdd:PTZ00114 59 KITKDGVTVAKAIefsdRFENVGAQLIRQVASKTNDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 91 REALLSSavdhgSDEVKFRQDLMNIAgtTLSS-------KLLThhkDHFTKLAVEAVLRLKGSGNLEaiHIIKKLGG-SL 162
Cdd:PTZ00114 139 LESLKEQ-----SRPVKTKEDILNVA--TISAngdveigSLIA---DAMDKVGKDGTITVEDGKTLE--DELEVVEGmSF 206
|
170 180 190
....*....|....*....|....*....|...
gi 119617634 163 ADSYLDEGFLLDKKigvNQPKRIENAKILIANT 195
Cdd:PTZ00114 207 DRGYISPYFVTNEK---TQKVELENPLILVTDK 236
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
16-105 |
7.80e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 51.26 E-value: 7.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 16 VTNDGATILKNIGVDNPAAKVLVDMSR----VQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAR 91
Cdd:PRK12850 49 ITKDGVTVAKEIELEDKFENMGAQMVKevasKTNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVV 128
|
90
....*....|....
gi 119617634 92 EALLSSAVDHGSDE 105
Cdd:PRK12850 129 DELKKIAKKVTSSK 142
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
16-100 |
1.56e-05 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 47.04 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 16 VTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAR 91
Cdd:PRK00013 48 ITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAV 127
|
....*....
gi 119617634 92 EALLSSAVD 100
Cdd:PRK00013 128 EELKKISKP 136
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
16-150 |
2.12e-05 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 46.56 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 16 VTNDGATILKNIGVD----NPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAR 91
Cdd:PRK14104 49 ITKDGVTVAKEIELEdkfeNMGAQMVREVASKSADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVV 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 119617634 92 EALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLThhkDHFTKLAVEAVLRLKGSGNLE 150
Cdd:PRK14104 129 ADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFLA---DAMKKVGNEGVITVEEAKSLE 184
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
16-147 |
2.90e-05 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 46.27 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617634 16 VTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAR 91
Cdd:PRK12851 49 ITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVV 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 119617634 92 EALLSSAvdhgsDEVKFRQDLMNIAgtTLSSklltHHKDHFTKLAVEAVLRLKGSG 147
Cdd:PRK12851 129 EELKANA-----RPVTTNAEIAQVA--TISA----NGDAEIGRLVAEAMEKVGNEG 173
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
16-89 |
1.25e-04 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 44.07 E-value: 1.25e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119617634 16 VTNDGATILKNIGVD----NPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKA 89
Cdd:PRK12852 49 ITKDGVTVAKEIELEdkfeNMGAQMVREVASKTNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAA 126
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
16-88 |
6.48e-04 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 42.01 E-value: 6.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119617634 16 VTNDGATILKNIGVDNPAAKVLVDMSRV----QDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATK 88
Cdd:CHL00093 48 IVNDGVTIAKEIELEDHIENTGVALIRQaaskTNDVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQ 124
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
16-89 |
1.33e-03 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 41.06 E-value: 1.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119617634 16 VTNDGATILKNIGVDNP----AAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKA 89
Cdd:PLN03167 104 IVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKA 181
|
|
| |
