|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
11-527 |
0e+00 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239452 [Multi-domain] Cd Length: 517 Bit Score: 1026.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 11 IFKAGADEEKAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSGGRDGAVTVTNDGATILKSIGIDNPAAQVLVDMSKV 90
Cdd:cd03336 1 ILKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILQSVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 91 QDDEVGDGTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLKATVDHGNDEEKFRCDLLNISRTTLSSK 170
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEAFREDLLNIARTTLSSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 171 LLTHHKDHFAKLAVEAVLRLKGSGNLEAIHVIKKLGGSLTDSYLDEGFLLDKKIGVNQPKRIENANILIANTGMDTDKIK 250
Cdd:cd03336 161 ILTQDKEHFAELAVDAVLRLKGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQPKRIENAKILIANTPMDTDKIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 251 VFGSRVRVDSTAKVAEIELAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFAAAGVMAIEHADFAGVERLSLVTGGE 330
Cdd:cd03336 241 IFGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTGGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 331 IASTFDHPELVKLGTCKLIEEVMIGEDKLLHFSGVAMGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDTRTVYGG 410
Cdd:cd03336 321 IASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRVVLGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 411 GCSEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAHSEGKSTYGLDMKNGTTGDMAE 490
Cdd:cd03336 401 GCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTVGDMKE 480
|
490 500 510
....*....|....*....|....*....|....*..
gi 148232533 491 LGITESFQVKRQVLLSASEAAEVILRVDDIIKAAPRK 527
Cdd:cd03336 481 LGITESFKVKRQVLLSASEAAEMILRVDDIIKCAPRK 517
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
5-530 |
0e+00 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 946.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 5 SLAPVNIFKAGADEEKAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLS---GGRDGAVTVTNDGATILKSIGIDNPAA 81
Cdd:PTZ00212 4 ANVPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQPmseGPRSGNVTVTNDGATILKSVWLDNPAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 82 QVLVDMSKVQDDEVGDGTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLKATVDHGNDEEKFRCDLLN 161
Cdd:PTZ00212 84 KILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEEKFKEDLLN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 162 ISRTTLSSKLLTHHKDHFAKLAVEAVLRLKGSGNLEAIHVIKKLGGSLTDSYLDEGFLLDKKIGVNQPKRIENANILIAN 241
Cdd:PTZ00212 164 IARTTLSSKLLTVEKDHFAKLAVDAVLRLKGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVGQPKRLENCKILVAN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 242 TGMDTDKIKVFGSRVRVDSTAKVAEIELAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFAAAGVMAIEHADFAGVE 321
Cdd:PTZ00212 244 TPMDTDKIKIYGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGME 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 322 RLSLVTGGEIASTFDHPELVKLGTCKLIEEVMIGEDKLLHFSGVAMGEACTIVLRGATQQILDEAERSLHDALCVLAQTV 401
Cdd:PTZ00212 324 RLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 402 KDTRTVYGGGCSEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAHSEGKSTYGLDMK 481
Cdd:PTZ00212 404 KDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGIDME 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 148232533 482 NGTTGDMAELGITESFQVKRQVLLSASEAAEVILRVDDIIKAAPRKRVP 530
Cdd:PTZ00212 484 KGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRCAPRQREQ 532
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
10-528 |
0e+00 |
|
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT beta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274082 Cd Length: 519 Bit Score: 888.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 10 NIFKAGADEEKAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSGGRDGAVTVTNDGATILKSIGIDNPAAQVLVDMSK 89
Cdd:TIGR02341 1 QIFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 90 VQDDEVGDGTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLKATVDHGNDEEKFRCDLLNISRTTLSS 169
Cdd:TIGR02341 81 VQDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVKFRQDLMNIARTTLSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 170 KLLTHHKDHFAKLAVEAVLRLKGSGNLEAIHVIKKLGGSLTDSYLDEGFLLDKKIGVNQPKRIENANILIANTGMDTDKI 249
Cdd:TIGR02341 161 KILSQHKDHFAQLAVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 250 KVFGSRVRVDSTAKVAEIELAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFAAAGVMAIEHADFAGVERLSLVTGG 329
Cdd:TIGR02341 241 KIFGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVTGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 330 EIASTFDHPELVKLGTCKLIEEVMIGEDKLLHFSGVAMGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDTRTVYG 409
Cdd:TIGR02341 321 EIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTVLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 410 GGCSEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAHSEGKSTYGLDMKNGTTGDMA 489
Cdd:TIGR02341 401 GGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGTIADMR 480
|
490 500 510
....*....|....*....|....*....|....*....
gi 148232533 490 ELGITESFQVKRQVLLSASEAAEVILRVDDIIKAAPRKR 528
Cdd:TIGR02341 481 QLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPRKR 519
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
16-522 |
0e+00 |
|
chaperonin families, type I and type II. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.
Pssm-ID: 238189 Cd Length: 464 Bit Score: 549.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 16 ADEEKAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSGgrDGAVTVTNDGATILKSIGIDNPAAQVLVDMSKVQDDEV 95
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDS--LGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 96 GDGTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLKATVDHgndEEKFRCDLLNISRTTLSSKLLTHH 175
Cdd:cd00309 79 GDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPI---DVEDREELLKVATTSLNSKLVSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 176 KDHFAKLAVEAVLRLKGSG---NLEAIHVIKKLGGSLTDSYLDEGFLLDKKIGVNQ-PKRIENANILIANTGMDTdkikv 251
Cdd:cd00309 156 DDFLGELVVDAVLKVGKENgdvDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYmPKRLENAKILLLDCKLEY----- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 252 fgsrvrvdstakvaeielaekekmkekverilkhginCFINRQLIYNYPEQLFAAAGVMAIEHADFAGVERLSLVTGGEI 331
Cdd:cd00309 231 -------------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 332 ASTFDHPELVKLGTCKLIEEVMIGEDKLLHFSGVAMGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDTRTVYGGG 411
Cdd:cd00309 274 VSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 412 CSEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAHSEGKSTYGLDMKNGTTGDMAEL 491
Cdd:cd00309 354 AAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKEA 433
|
490 500 510
....*....|....*....|....*....|.
gi 148232533 492 GITESFQVKRQVLLSASEAAEVILRVDDIIK 522
Cdd:cd00309 434 GIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
35-523 |
1.86e-174 |
|
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.
Pssm-ID: 395068 [Multi-domain] Cd Length: 489 Bit Score: 500.96 E-value: 1.86e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 35 IGDLVKSTLGPKGMDKILLSGGrdGAVTVTNDGATILKSIGIDNPAAQVLVDMSKVQDDEVGDGTTSVTVLAAELLREAE 114
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSG--GDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 115 ILVAKKIHPQTIISGWRQATQVAREALLKatVDHGNDEEKFRCDLLNISRTTLSSKLLTHHKDHFAKLAVEAVLRLK--- 191
Cdd:pfam00118 79 KLLAAGVHPTTIIEGYEKALEKALEILDS--IISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 192 GSGNLEAIHVIKKLGGSLTDSYLDEGFLLDKKI-GVNQPKRIENANILIANTGMDTDKIKVFGSrVRVDSTAKVAEIELA 270
Cdd:pfam00118 157 GSFDLGNIGVVKILGGSLEDSELVDGVVLDKGPlHPDMPKRLENAKVLLLNCSLEYEKTETKAT-VVLSDAEQLERFLKA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 271 EKEKMKEKVERILKHGINCFINRQLIYNYPEQLFAAAGVMAIEHADFAGVERLSLVTGGEIASTFDHPELVKLGTCKLIE 350
Cdd:pfam00118 236 EEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 351 EVMIGEDKLLHFSGVAMGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDTRTVYGGGCSEMLMAHVVTELANRTPG 430
Cdd:pfam00118 316 EEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 431 KESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAHSEGKSTYGLDMKNGTTGDMAELGITESFQVKRQVLLSASEA 510
Cdd:pfam00118 396 KEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEA 475
|
490
....*....|...
gi 148232533 511 AEVILRVDDIIKA 523
Cdd:pfam00118 476 ASTILRIDDIIKA 488
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
9-524 |
4.65e-132 |
|
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: 393.94 E-value: 4.65e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 9 VNIFKAGADEEKAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSGGRDgaVTVTNDGATILKSIGIDNPAAQVLVDMS 88
Cdd:cd03343 1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGD--VTITNDGATILKEMDIEHPAAKMLVEVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 89 KVQDDEVGDGTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLKATVDHGNDEEKFrcdLLNISRTTLS 168
Cdd:cd03343 79 KTQDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDT---LRKIAKTSLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 169 SKLLTHHKDHFAKLAVEAVLRL--KGSG----NLEAIHVIKKLGGSLTDSYLDEGFLLDK-KIGVNQPKRIENANILIAN 241
Cdd:cd03343 156 GKGAEAAKDKLADLVVDAVLQVaeKRDGkyvvDLDNIKIEKKTGGSVDDTELIRGIVIDKeVVHPGMPKRVENAKIALLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 242 TGMDTDKIKVfGSRVRVDSTAKVAEIELAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFAAAGVMAIEHADFAGVE 321
Cdd:cd03343 236 APLEVKKTEI-DAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDME 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 322 RLSLVTGGEIASTFDHPELVKLGTCKLIEEVMIGEDKLLHFSGVAMGEACTIVLRGATQQILDEAERSLHDALCVLAQTV 401
Cdd:cd03343 315 KLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADAL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 402 KDTRTVYGGGCSEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAHSEGKSTYGLDMK 481
Cdd:cd03343 395 EDGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDVY 474
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 148232533 482 NGTTGDMAELGITESFQVKRQVLLSASEAAEVILRVDDIIKAA 524
Cdd:cd03343 475 TGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
8-524 |
2.37e-129 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 386.93 E-value: 2.37e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 8 PVNIFKAGADEEKAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSGGrdGAVTVTNDGATILKSIGIDNPAAQVLVDM 87
Cdd:NF041082 2 PILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSL--GDVVITNDGVTILKEMDIEHPAAKMIVEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 88 SKVQDDEVGDGTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLKATVDHGNDEEKFrcdLLNISRTTL 167
Cdd:NF041082 80 AKTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKET---LKKIAATAM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 168 SSKLLTHHKDHFAKLAVEAVLRL---KGSGN--LEAIHVIKKLGGSLTDSYLDEGFLLDK-KIGVNQPKRIENANILIAN 241
Cdd:NF041082 157 TGKGAEAAKDKLADLVVDAVKAVaekDGGYNvdLDNIKVEKKVGGSIEDSELVEGVVIDKeRVHPGMPKRVENAKIALLD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 242 TGMDTDKIKVfGSRVRVDSTAKVAEIELAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFAAAGVMAIEHADFAGVE 321
Cdd:NF041082 237 APLEVKKTEI-DAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDME 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 322 RLSLVTGGEIASTFDHPELVKLGTCKLIEEVMIGEDKLLHFSGVAMGEACTIVLRGATQQILDEAERSLHDALCVLAQTV 401
Cdd:NF041082 316 KLAKATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 402 KDTRTVYGGGCSEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAHSEGKSTYGLDMK 481
Cdd:NF041082 396 EDGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLDVY 475
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 148232533 482 NGTTGDMAELGITESFQVKRQVLLSASEAAEVILRVDDIIKAA 524
Cdd:NF041082 476 TGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
7-524 |
2.97e-128 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 384.30 E-value: 2.97e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 7 APVNIFKAGADEEKAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLsggrD--GAVTVTNDGATILKSIGIDNPAAQVL 84
Cdd:NF041083 1 QPVLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLV----DslGDIVITNDGATILKEMDVQHPAAKML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 85 VDMSKVQDDEVGDGTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLKATVDHG-NDEEKfrcdLLNIS 163
Cdd:NF041083 77 VEVAKTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDpDDRET----LKKIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 164 RTTLSSKLLTHHKDHFAKLAVEAVLRL------KGSGNLEAIHVIKKLGGSLTDSYLDEGFLLDK-KIGVNQPKRIENAN 236
Cdd:NF041083 153 ETSLTSKGVEEARDYLAEIAVKAVKQVaekrdgKYYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKeVVHPGMPKRVENAK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 237 ILIANTGMDTDKIKVfGSRVRVDSTAKVAEIELAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFAAAGVMAIEHAD 316
Cdd:NF041083 233 IALLDAPLEVKKTEI-DAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 317 FAGVERLSLVTGGEIASTFDHPELVKLGTCKLIEEVMIGEDKLLHFSGVAMGEACTIVLRGATQQILDEAERSLHDALCV 396
Cdd:NF041083 312 KSDMEKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 397 LAQTVKDTRTVYGGGCSEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAHSEGKSTY 476
Cdd:NF041083 392 VADAVEDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWA 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 148232533 477 GLDMKNGTTGDMAELGITESFQVKRQVLLSASEAAEVILRVDDIIKAA 524
Cdd:NF041083 472 GINVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
8-523 |
2.33e-126 |
|
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: 379.71 E-value: 2.33e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 8 PVNIFKAGADEEKAeTARLSSFIGA-IAIGDLVKSTLGPKGMDKILLSGgrDGAVTVTNDGATILKSIGIDNPAAQVLVD 86
Cdd:cd03340 1 PIILLKEGTDTSQG-KGQLISNINAcQAIADAVRTTLGPRGMDKLIVDG--RGKVTISNDGATILKLLDIVHPAAKTLVD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 87 MSKVQDDEVGDGTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLKATVD-HGNDEEKFRCDLLNISRT 165
Cdd:cd03340 78 IAKSQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNiDKEDKEEQRELLEKCAAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 166 TLSSKLLTHHKDHFAKLAVEAVLRLKGSGNLEAIHVIKKLGGSLTDSYLDEGFLLDKKIGV----NQPKRIENANILIAN 241
Cdd:cd03340 158 ALNSKLIASEKEFFAKMVVDAVLSLDDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYagfeQQPKKFKNPKILLLN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 242 TGMDTDKIKVfGSRVRVDSTAKVAEIELAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFAAAGVMA---IEHADFa 318
Cdd:cd03340 238 VELELKAEKD-NAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCagrVPEEDL- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 319 gvERLSLVTGGEIASTFDHPELVKLGTCKLIEEVMIGEDKLLHFSGVAMGEACTIVLRGATQQILDEAERSLHDALCVLA 398
Cdd:cd03340 316 --KRVAQATGGSIQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 399 QTVKDTRTVYGGGCSEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAHSEGKST-YG 477
Cdd:cd03340 394 RAIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKwYG 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 148232533 478 LDMKNGTTGDMAELGITESFQVKRQVLLSASEAAEVILRVDDIIKA 523
Cdd:cd03340 474 VDINNEGIADNFEAFVWEPSLVKINALTAATEAACLILSVDETIKN 519
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
8-523 |
2.49e-125 |
|
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: 376.72 E-value: 2.49e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 8 PVNIFKAGADEEKAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSGGRDgaVTVTNDGATILKSIGIDNPAAQVLVDM 87
Cdd:TIGR02339 1 PVFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGD--VTITNDGATILKEMDIEHPAAKMLVEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 88 SKVQDDEVGDGTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLKATVDHGNDEEKFrcdLLNISRTTL 167
Cdd:TIGR02339 79 AKTQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDL---LKKIAYTSL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 168 SSKLLT-HHKDHFAKLAVEAVLRL-------KGSGNLEAIHVIKKLGGSLTDSYLDEGFLLDK-KIGVNQPKRIENANIL 238
Cdd:TIGR02339 156 TSKASAeVAKDKLADLVVEAVKQVaelrgdgKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKeVVHPGMPKRVENAKIA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 239 IANTGMDTDKIKVfGSRVRVDSTAKVAEIELAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFAAAGVMAIEHADFA 318
Cdd:TIGR02339 236 LLDAPLEVEKTEI-DAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 319 GVERLSLVTGGEIASTFDHPELVKLGTCKLIEEVMIGEDKLLHFSGVAMGEACTIVLRGATQQILDEAERSLHDALCVLA 398
Cdd:TIGR02339 315 DIEKLARATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 399 QTVKDTRTVYGGGCSEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAHSEGKSTYGL 478
Cdd:TIGR02339 395 NALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAGI 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 148232533 479 DMKNGTTGDMAELGITESFQVKRQVLLSASEAAEVILRVDDIIKA 523
Cdd:TIGR02339 475 NVFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
8-523 |
1.40e-116 |
|
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: 354.45 E-value: 1.40e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 8 PVNIFKAGADEEKAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSGGrdGAVTVTNDGATILKSIGIDNPAAQVLVDM 87
Cdd:TIGR02345 3 TIVLLKEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSN--GKATISNDGATILKLLDIVHPAAKTLVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 88 SKVQDDEVGDGTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLKATVDHGNDEEKFRCDLLNISRTTL 167
Cdd:TIGR02345 81 AKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKGEQRELLEKCAATAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 168 SSKLLTHHKDHFAKLAVEAVLRLKGSG-NLEAIHVIKKLGGSLTDSYLDEGFLLDKKIGV----NQPKRIENANILIANT 242
Cdd:TIGR02345 161 SSKLISHNKEFFSKMIVDAVLSLDRDDlDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYagfeQQPKKFANPKILLLNV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 243 GMDTdKIKVFGSRVRVDSTAKVAEIELAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFAAAGVMAIEHADFAGVER 322
Cdd:TIGR02345 241 ELEL-KAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 323 LSLVTGGEIASTFDHPELVKLGTCKLIEEVMIGEDKLLHFSGVAMGEACTIVLRGATQQILDEAERSLHDALCVLAQTVK 402
Cdd:TIGR02345 320 VIKACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 403 DTRTVYGGGCSEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAHSEGKSTYGLDMKN 482
Cdd:TIGR02345 400 NKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYGVDINT 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 148232533 483 GTTGDMAELGITESFQVKRQVLLSASEAAEVILRVDDIIKA 523
Cdd:TIGR02345 480 EDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITN 520
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
22-525 |
4.39e-116 |
|
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: 353.13 E-value: 4.39e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 22 ETARLSSFIGAIAIGDLVKSTLGPKGMDKILLsggrD--GAVTVTNDGATILKSIGIDNPAAQVLVDMSKVQDDEVGDGT 99
Cdd:cd03335 7 QDVRTQNVTAAMAIANIVKSSLGPVGLDKMLV----DdiGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 100 TSVTVLAAELLREAEILVAKKIHPQTIISGWRQAtqvAREAL--LKATVDHGNDEEKFRCdLLNISRTTLSSKLLTHHKD 177
Cdd:cd03335 83 TSVVIIAAELLKRANELVKQKIHPTTIISGYRLA---CKEAVkyIKEHLSISVDNLGKES-LINVAKTSMSSKIIGADSD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 178 HFAKLAVEAVLRLKGSGNL-------EAIHVIKKLGGSLTDSYLDEGFLLDKKIGVNQ-PKRIENANILIANTGMDTDKI 249
Cdd:cd03335 159 FFANMVVDAILAVKTTNEKgktkypiKAVNILKAHGKSAKESYLVNGYALNCTRASQGmPTRVKNAKIACLDFNLQKTKM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 250 KVfGSRVRVDSTAKVAEIELAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFAAAGVMAIEHADFAGVERLSLVTGG 329
Cdd:cd03335 239 KL-GVQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 330 EIASTFDHPE------LVKLGTCKLIEEVMIGEDKLLHFSGVAMGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKD 403
Cdd:cd03335 318 TLVSTLANLEgeetfdPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLES 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 404 TRTVYGGGCSEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAHSEGKST-------- 475
Cdd:cd03335 398 NSVVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAQVKpdkkhlkw 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 148232533 476 YGLDMKNGTTGDMAELGITESFQVKRQVLLSASEAAEVILRVDDIIKAAP 525
Cdd:cd03335 478 YGLDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIKLNP 527
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
15-527 |
2.06e-113 |
|
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274081 [Multi-domain] Cd Length: 536 Bit Score: 346.71 E-value: 2.06e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 15 GADEEKAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSGGrdGAVTVTNDGATILKSIGIDNPAAQVLVDMSKVQDDE 94
Cdd:TIGR02340 4 GGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDI--GDVTITNDGATILKLLEVEHPAAKILVELAQLQDRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 95 VGDGTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQAtqvAREAL------LKATVDhgndeEKFRCDLLNISRTTLS 168
Cdd:TIGR02340 82 VGDGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLA---CKEAVkyikenLSVSVD-----ELGREALINVAKTSMS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 169 SKLLTHHKDHFAKLAVEAVLRLKGSGN-------LEAIHVIKKLGGSLTDSYLDEGFLLDKKIGVNQ-PKRIENANILIA 240
Cdd:TIGR02340 154 SKIIGLDSDFFSNIVVDAVLAVKTTNEngetkypIKAINILKAHGKSARESMLVKGYALNCTVASQQmPKRIKNAKIACL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 241 NTGMDTDKIKVfGSRVRVDSTAKVAEIELAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFAAAGVMAIEHADFAGV 320
Cdd:TIGR02340 234 DFNLQKAKMAL-GVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 321 ERLSLVTGGEIASTFDHPE------LVKLGTCKLIEEVMIGEDKLLHFSGVAMGEACTIVLRGATQQILDEAERSLHDAL 394
Cdd:TIGR02340 313 KRIAKATGATLVSTLADLEgeetfeASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDAL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 395 CVLAQTVKDTRTVYGGGCSEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAHSEGKS 474
Cdd:TIGR02340 393 CVVKRTLESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAQL 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148232533 475 T--------YGLDMKNGTTGDMAELGITESFQVKRQVLLSASEAAEVILRVDDIIKAAPRK 527
Cdd:TIGR02340 473 KpekkhlkwYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIKLNPEQ 533
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
24-522 |
4.96e-110 |
|
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: 337.73 E-value: 4.96e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 24 ARLSSFIGAIAIGDLVKSTLGPKGMDKILLSGgrDGAVTVTNDGATILKSIGIDNPAAQVLVDMSKVQDDEVGDGTTSVT 103
Cdd:cd03339 24 AHKSHILAAKSVANILRTSLGPRGMDKILVSP--DGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 104 VLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALlKATVDHGNDEEKFRCDLLNISRTTLSSKLLTHHKDHFAKLA 183
Cdd:cd03339 102 VLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHL-EEIADKIEFSPDNKEPLIQTAMTSLGSKIVSRCHRQFAEIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 184 VEAVLRL----KGSGNLEAIHVIKKLGGSLTDSYLDEGFLLDKKIGVNQ-PKRIENANILIANTGMDTDKIKVfGSRVRV 258
Cdd:cd03339 181 VDAVLSVadleRKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHPQmPKEVKDAKIAILTCPFEPPKPKT-KHKLDI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 259 DSTAKVAEIELAEKEKMKEKVERILKHGINCFI---------NRQLIYNypeQLFAAAGVMAIEhadfagVERLSLVTGG 329
Cdd:cd03339 260 TSVEDYKKLQEYEQKYFREMVEQVKDAGANLVIcqwgfddeaNHLLLQN---GLPAVRWVGGVE------IELIAIATGG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 330 EIASTFDHPELVKLGTCKLIEEVMIG--EDKLLHFSGVAMGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDTRTV 407
Cdd:cd03339 331 RIVPRFEDLSPEKLGKAGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIV 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 408 YGGGCSEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAH-SEGKSTYGLDMKNGTTG 486
Cdd:cd03339 411 YGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQvKEKNPHLGIDCLGRGTN 490
|
490 500 510
....*....|....*....|....*....|....*.
gi 148232533 487 DMAELGITESFQVKRQVLLSASEAAEVILRVDDIIK 522
Cdd:cd03339 491 DMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
17-521 |
4.15e-105 |
|
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: 324.62 E-value: 4.15e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 17 DEEKAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSGgrDGAVTVTNDGATILKSIGIDNPAAQVLVDMSKVQDDEVG 96
Cdd:cd03338 2 DKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTG--KGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 97 DGTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREAL--LKATVDHGNDEekfrcDLLNISRTTLSSKLLTH 174
Cdd:cd03338 80 DGTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILdsMSIPVDLNDRE-----SLIKSATTSLNSKVVSQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 175 HKDHFAKLAVEAVLRL-----KGSGNLEAIHVIKKLGGSLTDSYLDEGFLLDKKI--GVNQPKRIENANILIAN------ 241
Cdd:cd03338 155 YSSLLAPIAVDAVLKVidpatATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKAskKAGGPTRIEKAKIGLIQfclspp 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 242 -TGMDtdkikvfgSRVRVDSTAKVAEIELAEKEKMKEKVERILKHGINCF-----INRQLIYNYPEQLFAAAGVMAIEHA 315
Cdd:cd03338 235 kTDMD--------NNIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLliqksILRDAVSDLALHFLAKLKIMVVKDI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 316 DFAGVERLSLVTGGEIASTFDHPELVKLGTCKLIEEVMIGEDKLLHFSGVA-MGEACTIVLRGATQQILDEAERSLHDAL 394
Cdd:cd03338 307 EREEIEFICKTIGCKPVASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKnPGKTVTILVRGSNKLVLDEAERSLHDAL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 395 CVLAQTVKDTRTVYGGGCSEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAHSEGKS 474
Cdd:cd03338 387 CVIRCLVKKRALIPGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEK 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 148232533 475 TYGLDMKNGTTGDMAELGITESFQVKRQVLLSASEAAEVILRVDDII 521
Cdd:cd03338 467 NAGINVRKGAITNILEENVVQPLLVSTSAITLATETVRMILKIDDIV 513
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
20-522 |
3.57e-101 |
|
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: 315.20 E-value: 3.57e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 20 KAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSggRDGAVTVTNDGATILKSIGIDNPAAQVLVDMSKVQDDEVGDGT 99
Cdd:TIGR02343 24 KGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLIS--PDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 100 TSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLKaTVDHGNDEEKFRCDLLNISRTTLSSKLLTHHKDHF 179
Cdd:TIGR02343 102 TGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEE-ISDEISADNNNREPLIQAAKTSLGSKIVSKCHRRF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 180 AKLAVEAVLRL----KGSGNLEAIHVIKKLGGSLTDSYLDEGFLLDKKIGVNQ-PKRIENANILIANTGMDTDKIKVfGS 254
Cdd:TIGR02343 181 AEIAVDAVLNVadmeRRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQmPKEVEDAKIAILTCPFEPPKPKT-KH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 255 RVRVDSTAKVAEIELAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFAAAGVMAIEHADFAGVERLSLVTGGEIAST 334
Cdd:TIGR02343 260 KLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVPR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 335 FDHPELVKLGTCKLIEEVMIG--EDKLLHFSGVAMGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDTRTVYGGGC 412
Cdd:TIGR02343 340 FQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGGGA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 413 SEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAH-SEGKSTYGLDMKNGTTGDMAEL 491
Cdd:TIGR02343 420 AEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQlKEKNPNLGVDCLGYGTNDMKEQ 499
|
490 500 510
....*....|....*....|....*....|.
gi 148232533 492 GITESFQVKRQVLLSASEAAEVILRVDDIIK 522
Cdd:TIGR02343 500 FVFETLIGKKQQILLATQLVRMILKIDDVIS 530
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
17-524 |
2.96e-98 |
|
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: 307.10 E-value: 2.96e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 17 DEEKAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSGgrDGAVTVTNDGATILKSIGIDNPAAQVLVDMSKVQDDEVG 96
Cdd:TIGR02342 3 DKDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDG--KGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 97 DGTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREAL--LKATVDHGNDEEkfrcdLLNISRTTLSSKLLTH 174
Cdd:TIGR02342 81 DGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILdeMSIPVDLSDREQ-----LLKSATTSLSSKVVSQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 175 HKDHFAKLAVEAVLRLKGSG-----NLEAIHVIKKLGGSLTDSYLDEGFLLDKKIGVNQ--PKRIENANILIANTGMDTD 247
Cdd:TIGR02342 156 YSSLLAPLAVDAVLKVIDPEnaknvDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAggPTRIEKAKIGLIQFQISPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 248 KIKVfGSRVRVDSTAKVAEIELAEKEKMKEKVERILKHGINCF-----INRQLIYNYPEQLFAAAGVMAIEHADFAGVER 322
Cdd:TIGR02342 236 KTDM-ENQIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLliqksILRDAVNDLALHFLAKMKIMVVKDIEREEIEF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 323 LSLVTGGEIASTFDHPELVKLGTCKLIEEVMIGEDKLLHFSGVA-MGEACTIVLRGATQQILDEAERSLHDALCVLAQTV 401
Cdd:TIGR02342 315 ICKTIGCKPIASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQnAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 402 KDTRTVYGGGCSEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAHSEGKSTYGLDMK 481
Cdd:TIGR02342 395 KKRGLIAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISVR 474
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 148232533 482 NGTTGDMAELGITESFQVKRQVLLSASEAAEVILRVDDIIKAA 524
Cdd:TIGR02342 475 KGGITNMLEEHVLQPLLVTTSAITLASETVRSILKIDDIVFTR 517
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
8-521 |
4.89e-94 |
|
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: 294.97 E-value: 4.89e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 8 PVNIFKAGADEEKAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSGGrdGAVTVTNDGATILKSIGIDNPAAQVLVDM 87
Cdd:cd03337 1 PVLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPM--GGIVLTNDGNAILREIDVAHPAAKSMIEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 88 SKVQDDEVGDGTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLKA--TVDHGNDEekfrcDLLNISRT 165
Cdd:cd03337 79 SRTQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEIsiPVDVNDRA-----QMLKIIKS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 166 TLSSKLLTHHKDHFAKLAVEAVLRLKGSGNLEAIHV-IKK-------LGGSLTDSYLDEGFLLDKKigVNQPK---RIEN 234
Cdd:cd03337 154 CIGTKFVSRWSDLMCNLALDAVKTVAVEENGRKKEIdIKRyakvekiPGGEIEDSRVLDGVMLNKD--VTHPKmrrRIEN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 235 ANILIantgmdtdkikvfgsrvrVDSTAKVAEI------ELAEKEkmkekverILKHGINCfINRqliynypeqlfaaag 308
Cdd:cd03337 232 PRIVL------------------LDCPLEYLVItekgvsDLAQHY--------LVKAGITA-LRR--------------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 309 vmaIEHADfagVERLSLVTGGEIASTFDHPELVKLGT-CKLIEEVMIGEDKLLHFSGVAMGEACTIVLRGATQQILDEAE 387
Cdd:cd03337 270 ---VRKTD---NNRIARACGATIVNRPEELTESDVGTgAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 388 RSLHDALCVLAQTVKDTRTVYGGGCSEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRA 467
Cdd:cd03337 344 RNLQDAMAVARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRA 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 148232533 468 AH-SEGKSTYGLDMKNGTTGDMAELGITESFQVKRQVLLSASEAAEVILRVDDII 521
Cdd:cd03337 424 KHaQGENSTWGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
22-527 |
2.05e-89 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 283.51 E-value: 2.05e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 22 ETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSggRDGAVTVTNDGATILKSIGIDNP----AAQVLVDMSKVQDDEVGD 97
Cdd:COG0459 9 EDARRANIRGVKALADAVKVTLGPKGRNVMLVK--SFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 98 GTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLKATVDHGNDEEkfrcdLLNISRTTLSSkllthhKD 177
Cdd:COG0459 87 GTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEE-----LAQVATISANG------DE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 178 HFAKLAVEAVLRLKGSGNLeaihVIKKLGGSLTDSYLDEGFLLDKKI--------GVNQPKRIENANILIANtgmdtDKI 249
Cdd:COG0459 156 EIGELIAEAMEKVGKDGVI----TVEEGKGLETELEVVEGMQFDKGYlspyfvtdPEKMPAELENAYILLTD-----KKI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 250 KVFGSRVrvdstaKVAEielaekekmkekveRILKHGINCFINRQLIYNYPEQLFAAAGVMAIEHAdfAGV--------- 320
Cdd:COG0459 227 SSIQDLL------PLLE--------------KVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRV--VAVkapgfgdrr 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 321 ----ERLSLVTGGEIAS-----TFDHPELVKLGTCKLIEevmIGEDKLLHFSGVAMGEACTIVLRGATQQILDEAERSLH 391
Cdd:COG0459 285 kamlEDIAILTGGRVISedlglKLEDVTLDDLGRAKRVE---VDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 392 DALCVLAQTVKDtRTVYGGGCSEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAhse 471
Cdd:COG0459 362 DALHATRAAVEE-GIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA--- 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 148232533 472 GKSTYGLDMKNGTTGDMAELGITESFQVKRQVLLSASEAAEVILRVDDIIKAAPRK 527
Cdd:COG0459 438 KDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEK 493
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
35-523 |
8.93e-86 |
|
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: 273.33 E-value: 8.93e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 35 IGDLVKSTLGPKGMDKILLSggRDGAVTVTNDGATILKSIGIDNPAAQVLVDMSKVQDDEVGDGTTSVTVLAAELLREAE 114
Cdd:cd03341 20 LSQITRTSYGPNGMNKMVIN--HLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGELLEKAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 115 ILVAKKIHPQTIISGWRQATQVAREALLKATVDHGNDEEKFRcDLLNISRTTLSSKLLtHHKDHFAKLAVEAVLRLK--- 191
Cdd:cd03341 98 ELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLRNKE-EVSKALKTAIASKQY-GNEDFLSPLVAEACISVLpen 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 192 -GSGNLEAIHVIKKLGGSLTDSYLDEGFLLDKKIgVNQPKRIENANILIANTGMDTdKIKVfgsrvrVDSTAKVAEIELa 270
Cdd:cd03341 176 iGNFNVDNIRVVKILGGSLEDSKVVRGMVFKREP-EGSVKRVKKAKVAVFSCPFDI-GVNV------IVAGGSVGDLAL- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 271 ekekmkekverilkHgincFINRqliynypeqlfaaAGVMAIEHADFAGVERLSLVTGGEIASTFDHPELVKLGTCKLIE 350
Cdd:cd03341 247 --------------H----YCNK-------------YGIMVIKINSKFELRRLCRTVGATPLPRLGAPTPEEIGYCDSVY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 351 EVMIGEDKLLHFSGV-AMGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDTRTVYGGGCSEMLMAHVVTELANRTP 429
Cdd:cd03341 296 VEEIGDTKVVVFRQNkEDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAKKLKEYGEKTP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 430 GKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAHSEGKSTYGLDMKNGTTG--DMAELGITESFQVKRQVLLSA 507
Cdd:cd03341 376 GLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDEGtkDAKEAGIFDHLATKKWAIKLA 455
|
490
....*....|....*.
gi 148232533 508 SEAAEVILRVDDIIKA 523
Cdd:cd03341 456 TEAAVTVLRVDQIIMA 471
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
8-527 |
3.47e-84 |
|
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT gamma chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274085 [Multi-domain] Cd Length: 524 Bit Score: 270.46 E-value: 3.47e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 8 PVNIFKAGADEEKAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSGGrdGAVTVTNDGATILKSIGIDNPAAQVLVDM 87
Cdd:TIGR02344 1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPM--GGIVMTNDGNAILREIDVAHPAAKSMIEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 88 SKVQDDEVGDGTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLKAT--VDHGNDEekfrcDLLNISRT 165
Cdd:TIGR02344 79 SRTQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISipVDVNDDA-----AMLKLIQS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 166 TLSSKLLTHHKDHFAKLAVEAVLRLKGSGNLEAIHVIKKL-------GGSLTDSYLDEGFLLDKKigVNQPK---RIENA 235
Cdd:TIGR02344 154 CIGTKFVSRWSDLMCDLALDAVRTVQRDENGRKEIDIKRYakvekipGGDIEDSCVLKGVMINKD--VTHPKmrrYIENP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 236 NILIANTGMDTDKIKvfgSRVRVDSTA--------KVAEIELAEKEKMkekverILKHGINCFINRQLIYNYPEQLFAAA 307
Cdd:TIGR02344 232 RIVLLDCPLEYKKGE---SQTNIEITKeedwnrilQMEEEYVQLMCED------IIAVKPDLVITEKGVSDLAQHYLLKA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 308 GVMAIEHADFAGVERLSLVTGGEIASTFDHPELVKLGT-CKLIEEVMIGEDKLLHFSGVAMGEACTIVLRGATQQILDEA 386
Cdd:TIGR02344 303 NITAIRRVRKTDNNRIARACGATIVNRPEELRESDVGTgCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 387 ERSLHDALCVLAQTVKDTRTVYGGGCSEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLR 466
Cdd:TIGR02344 383 ERNLQDAMAVARNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELR 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148232533 467 AAHS-EGKSTYGLDMKNGTTGDMAELGITESFQVKRQVLLSASEAAEVILRVDDIIKAAPRK 527
Cdd:TIGR02344 463 AKHAqENNCTWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVSGVKKK 524
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
35-525 |
3.21e-76 |
|
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: 250.02 E-value: 3.21e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 35 IGDLVKSTLGPKGMDKILLSggRDGAVTVTNDGATILKSIGIDNPAAQVLVDMSKVQDDEVGDGTTSVTVLAAELLREAE 114
Cdd:TIGR02346 30 LSQITRTSLGPNGMNKMVIN--HLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGELLNKAE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 115 ILVAKKIHPQTIISGWRQATQVAREALLKATVDHGNDEEKFRcDLLNISRTTLSSKLLtHHKDHFAKLAVEAVLRLK--- 191
Cdd:TIGR02346 108 ELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDLRDKD-ELIKALKASISSKQY-GNEDFLAQLVAQACSTVLpkn 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 192 -GSGNLEAIHVIKKLGGSLTDSYLDEGFLLdKKIGVNQPKRIENANILIANTGMDTDKIKVFGSrVRVDSTAKVAEIELA 270
Cdd:TIGR02346 186 pQNFNVDNIRVCKILGGSLSNSEVLKGMVF-NREAEGSVKSVKNAKVAVFSCPLDTATTETKGT-VLIHNAEELLNYSKG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 271 EKEKMKEKVERILKHGINCFINRQLIYNYPEQLFAAAGVMAIEHADFAGVERLSLVTGGEIASTFDHPELVKLGTCKLIE 350
Cdd:TIGR02346 264 EENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRLGAPTPEEIGYVDSVY 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 351 EVMIGEDKLLHFSGVAMGEAC-TIVLRGATQQILDEAERSLHDALCVLAQTVKDTRTVYGGGCSEMLMAHVVTELANRTP 429
Cdd:TIGR02346 344 VSEIGGDKVTVFKQENGDSKIsTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIELASRLTKYGEKLP 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 430 GKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAHSEGKSTYGLDMKNGTTG--DMAELGITESFQVKRQVLLSA 507
Cdd:TIGR02346 424 GLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDIEAESDGvkDASEAGIYDMLATKKWAIKLA 503
|
490
....*....|....*...
gi 148232533 508 SEAAEVILRVDDIIKAAP 525
Cdd:TIGR02346 504 TEAAVTVLRVDQIIMAKP 521
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
20-523 |
4.33e-69 |
|
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: 229.84 E-value: 4.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 20 KAETARLSSFI-----GAIAIGDLVKSTLGPKGMDKILLSGGrdGAVTVTNDGATILKSIGIDNPAAQVLVDMSKVQDDE 94
Cdd:cd03342 4 KAEVLRRGQALavnisAAKGLQDVLKTNLGPKGTLKMLVSGA--GDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 95 VGDGTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREAL--LKATVDHGNDEEKfrcdLLNISRTTLSSKLL 172
Cdd:cd03342 82 TGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLesFKVPVEIDTDREL----LLSVARTSLRTKLH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 173 THHKDHFAKLAVEAVLRLKGSG---NLEAIHVIKKLGGSLTDSYLDEGFLLDKKI-GVNQPKRIENANILIANTGMDTDK 248
Cdd:cd03342 158 ADLADQLTEIVVDAVLAIYKPDepiDLHMVEIMQMQHKSDSDTKLIRGLVLDHGArHPDMPKRVENAYILTCNVSLEYEK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 249 IKVFGSRVrvdstakvaeielaekekmkekverilkhgINCFINRQLIYNYPEQLFAAAGVMAIEHADFAGVERLSLVTG 328
Cdd:cd03342 238 TEVNSGFF------------------------------YSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 329 GEIASTFDHPELVKLGTCKLIEEVMIGEDKLLHFSGVAMGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDTRTVY 408
Cdd:cd03342 288 GVAMNSVDDLSPECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 409 GGGCSEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAHSEGKSTYGLDMKNGTTGDM 488
Cdd:cd03342 368 GAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDP 447
|
490 500 510
....*....|....*....|....*....|....*
gi 148232533 489 AELGITESFQVKRQVLLSASEAAEVILRVDDIIKA 523
Cdd:cd03342 448 ESEGIWDNYSVKRQILHSATVIASQLLLVDEIIRA 482
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
20-528 |
1.09e-67 |
|
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: 227.31 E-value: 1.09e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 20 KAETARLSSFI-----GAIAIGDLVKSTLGPKGMDKILLSGGrdGAVTVTNDGATILKSIGIDNPAAQVLVDMSKVQDDE 94
Cdd:TIGR02347 8 KAESLRRDAALmmninAARGLQDVLKTNLGPKGTLKMLVSGA--GDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 95 VGDGTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREAL--LKATVDHGNDEEKfrcdLLNISRTTLSSKLL 172
Cdd:TIGR02347 86 TGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLdkFKVKKEDEVDREF----LLNVARTSLRTKLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 173 THHKDHFAKLAVEAVLRLKGSGNLEAIHVIKKLG---GSLTDSYLDEGFLLDKkiGV---NQPKRIENANILIANTGMDT 246
Cdd:TIGR02347 162 ADLADQLTEIVVDAVLAIKKDGEDIDLFMVEIMEmkhKSATDTTLIRGLVLDH--GArhpDMPRRVKNAYILTCNVSLEY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 247 DKIKVFGSRV--------------RVDSTAKVAEI-ELAEKEKMKEKVERILkhgincFINRQLIYNYPEQLFAAAGVMA 311
Cdd:TIGR02347 240 EKTEVNSGFFyssaeqreklvkaeRKFVDDRVKKIiELKKKVCGKSPDKGFV------VINQKGIDPPSLDLLAKEGIMA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 312 IEHADFAGVERLSLVTGGEIASTFDHPELVKLGTCKLIEEVMIGEDKLLHFSGVAMGEACTIVLRGATQQILDEAERSLH 391
Cdd:TIGR02347 314 LRRAKRRNMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 392 DALCVLAQTVKDTRTVYGGGCSEMLMAHVVTELANRTPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRAAHSE 471
Cdd:TIGR02347 394 DGLRAVKNAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDE 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 148232533 472 GKSTYGLDMKNGTTGDMAELGITESFQVKRQVLLSASEAAEVILRVDDIIKAAPRKR 528
Cdd:TIGR02347 474 GGEVVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRAGRSML 530
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
158-403 |
5.34e-63 |
|
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. This superfamily also contains related domains from Fab1-like phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinases that only contain the intermediate and apical domains.
Pssm-ID: 239449 [Multi-domain] Cd Length: 209 Bit Score: 205.01 E-value: 5.34e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 158 DLLNISRTTLSSKLlTHHKDHFAKLAVEAVLRLKGSG---NLEAIHVIKKLGGSLTDSYLDEGFLLDKKIGVNQ-PKRIE 233
Cdd:cd03333 3 LLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNrmdDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYmPKRLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 234 NANILIANTGMDTdkikvfgsrvrvdstakvaeielaekekmkekverilkhginCFINRQLIYNYPEQLFAAAGVMAIE 313
Cdd:cd03333 82 NAKILLLDCPLEY------------------------------------------VVIAEKGIDDLALHYLAKAGIMAVR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 314 HADFAGVERLSLVTGGEIASTFDHPELVKLGTCKLIEEVMIGEDKLLHFSGVAMGEACTIVLRGATQQILDEAERSLHDA 393
Cdd:cd03333 120 RVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRSLHDA 199
|
250
....*....|
gi 148232533 394 LCVLAQTVKD 403
Cdd:cd03333 200 LCAVRAAVEE 209
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
22-515 |
8.96e-16 |
|
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). With the aid of cochaperonin GroES, GroEL encapsulates non-native substrate proteins inside the cavity of the GroEL-ES complex and promotes folding by using energy derived from ATP hydrolysis.
Pssm-ID: 239460 Cd Length: 520 Bit Score: 79.81 E-value: 8.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 22 ETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSGGrdGAVTVTNDGATILKSIGIDNP----AAQVLVDMSKVQDDEVGD 97
Cdd:cd03344 7 EEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSF--GSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 98 GTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLKATVDhGNDEEkfrcDLLNISrtTLSSklltHHKD 177
Cdd:cd03344 85 GTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKP-VKTKE----EIAQVA--TISA----NGDE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 178 HFAKLAVEAVLRLKGSGnleAIHVikKLGGSLTDsYLD--EGFLLDKkiG------VNQPKR----IENANILIantgmd 245
Cdd:cd03344 154 EIGELIAEAMEKVGKDG---VITV--EEGKTLET-ELEvvEGMQFDR--GylspyfVTDPEKmeveLENPYILL------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 246 TD-KIKVFGSRVRV-DSTAK-------VAE-IE---LAekekmkekverilkhgincfinrQLIYNYPEQLFAAAGVMAI 312
Cdd:cd03344 220 TDkKISSIQELLPIlELVAKagrplliIAEdVEgeaLA-----------------------TLVVNKLRGGLKVCAVKAP 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 313 EHADF--AGVERLSLVTGG-----EIASTFDHPELVKLGTCKlieEVMIGEDKllhfsgvamgeacTIVLRGA------- 378
Cdd:cd03344 277 GFGDRrkAMLEDIAILTGGtviseELGLKLEDVTLEDLGRAK---KVVVTKDD-------------TTIIGGAgdkaaik 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 379 --TQQILDEAERSLHD---------------ALCVL---AQT---VKD-----------TR------TVYGGGCSEMLMA 418
Cdd:cd03344 341 arIAQIRKQIEETTSDydkeklqerlaklsgGVAVIkvgGATeveLKEkkdrvedalnaTRaaveegIVPGGGVALLRAS 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 419 HVVTELANRTPGkESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRaahsEGKSTYGLDMKNGTTGDMAELGITESFQ 498
Cdd:cd03344 421 PALDKLKALNGD-EKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVL----ESPDGFGYDAATGEYVDMIEAGIIDPTK 495
|
570
....*....|....*..
gi 148232533 499 VKRQVLLSASEAAEVIL 515
Cdd:cd03344 496 VVRSALQNAASVASLLL 512
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
31-531 |
3.13e-15 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 78.24 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 31 GAIAIGDLVKSTLGPKGMDKILLSGGrdGAVTVTNDGATILKSIGIDNP----AAQVLVDMSKVQDDEVGDGTTSVTVLA 106
Cdd:PRK12851 19 GVNILADAVKVTLGPKGRNVVIDKSF--GAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 107 AELLREAEILVAKKIHPQTIISGWRQATQVAREALLKATVDHGNDEEKFRCdllnisrTTLSSklltHHKDHFAKLAVEA 186
Cdd:PRK12851 97 QAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQV-------ATISA----NGDAEIGRLVAEA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 187 VLRLKGSGnleaihVIKKLGGSLTDSYLD--EGFLLDK----KIGVNQPKR----IENANILIANtgmdtDKIKVFGSRV 256
Cdd:PRK12851 166 MEKVGNEG------VITVEESKTAETELEvvEGMQFDRgylsPYFVTDADKmeaeLEDPYILIHE-----KKISNLQDLL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 257 RV-DSTAKVAEIELaekekmkekverILKHGINCFINRQLIYNYPEQLFAAAGVMAIEHAD--FAGVERLSLVTGGEIAS 333
Cdd:PRK12851 235 PVlEAVVQSGKPLL------------IIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDrrKAMLEDIAILTGGTVIS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 334 -----TFDHPELVKLGTCKLI-----EEVMIG---------------------------EDKLLHFSGVAMGEACTIVLR 376
Cdd:PRK12851 303 edlgiKLENVTLEQLGRAKKVvvekeNTTIIDgagskteiegrvaqiraqieettsdydREKLQERLAKLAGGVAVIRVG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 377 GATQQILDEAERSLHDALCVLAQTVKDTrTVYGGGCSEMLMAHVVTELANRTpGKESVAMESFAKALRMLPTIIADNAGY 456
Cdd:PRK12851 383 ASTEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVALLRAVKALDKLETAN-GDQRTGVEIVRRALEAPVRQIAENAGA 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148232533 457 DSADLVSQLRaahsEGKSTYGLDMKNGTTGDMAELGITESFQVKRQVLLSASEAAEVILRVDDIIKAAPRKRVPD 531
Cdd:PRK12851 461 EGSVVVGKLR----EKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAP 531
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
24-530 |
4.29e-15 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 77.84 E-value: 4.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 24 ARLSSFIGAIAIGDLVKSTLGPKGMDKILLSggRDGAVTVTNDGATILKSIGIDNP----AAQVLVDMSKVQDDEVGDGT 99
Cdd:PRK12850 12 ARDRLLRGVNILANAVKVTLGPKGRNVVLEK--SFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 100 TSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLKATVDHGNDEEKFRCDLLNISRTTLSSKLLTHHKDHF 179
Cdd:PRK12850 90 TTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGEMIAEAMDKV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 180 AKLAVEAVLRLKGSG-NLEAIHVIKklggsltdsyLDEGFLldKKIGVNQPKR----IENANILIANTgmdtdKIKVFGS 254
Cdd:PRK12850 170 GKEGVITVEEAKTLGtELDVVEGMQ----------FDRGYL--SPYFVTNPEKmraeLEDPYILLHEK-----KISNLQD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 255 RVRVDSTAKVAEIELAekekmkekverILKHGINCFINRQLIYNYPEQLFAAAGVMAIEHAD--FAGVERLSLVTGGEIA 332
Cdd:PRK12850 233 LLPILEAVVQSGRPLL-----------IIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDrrKAMLEDIAVLTGGQVI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 333 S-----TFDHPELVKLGTCKlieEVMIGEDKLLHFSGVamGEACTIVLRgaTQQILDEAERSLHDA--------LCVLAQ 399
Cdd:PRK12850 302 SedlgiKLENVTLDMLGRAK---RVLITKENTTIIDGA--GDKKNIEAR--VKQIRAQIEETTSDYdreklqerLAKLAG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 400 TV----------------KD--------TRT------VYGGGCSeMLMAHVVTELANRTPGKESVAMESFAKALRMLPTI 449
Cdd:PRK12850 375 GVavirvggatevevkekKDrvddalhaTRAaveegiVPGGGVA-LLRARSALRGLKGANADETAGIDIVRRALEEPLRQ 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 450 IADNAGYDSADLVSQLRaahsEGKSTYGLDMKNGTTGDMAELGITESFQVKRQVLLSASEAAEVILRVDDIIKAAPRKRV 529
Cdd:PRK12850 454 IATNAGFEGSVVVGKVA----ELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAA 529
|
.
gi 148232533 530 P 530
Cdd:PRK12850 530 A 530
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
22-153 |
2.37e-13 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 72.53 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 22 ETARLSSFIGAIAIGDLVKSTLGPKGMDKILlsgGRD-GAVTVTNDGATILKSIGIDNP----AAQVLVDMSKVQDDEVG 96
Cdd:PRK12849 9 EEARRALERGVNKLADAVKVTLGPKGRNVVI---DKSfGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAG 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148232533 97 DGTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLK--------------ATVDHGNDEE 153
Cdd:PRK12849 86 DGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKAlarpvsgseeiaqvATISANGDEE 156
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
24-527 |
3.39e-13 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 71.99 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 24 ARLSSFIGAIAIGDLVKSTLGPKGMDKILlsGGRDGAVTVTNDGATILKSIGID----NPAAQVLVDMSKVQDDEVGDGT 99
Cdd:PRK14104 12 ARDRMLRGVDILANAVKVTLGPKGRNVVL--DKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKSADAAGDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 100 TSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLKATVDHGNDEEKFRCDLLNISRTTLSSKLLThhkDHF 179
Cdd:PRK14104 90 TTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFLA---DAM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 180 AKLAVEAVLRLKGSGNLEaihvikklggslTDSYLDEGFLLDKkiGVNQPKRIENAniliantgmdtDKIKVFGSrvrvD 259
Cdd:PRK14104 167 KKVGNEGVITVEEAKSLE------------TELDVVEGMQFDR--GYISPYFVTNA-----------DKMRVEMD----D 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 260 STAKVAEIELAEKEKMKEKVERILKHGINCFINRQ---------LIYNYPEQLFAAAGVMAIEHADF--AGVERLSLVTG 328
Cdd:PRK14104 218 AYILINEKKLSSLNELLPLLEAVVQTGKPLVIVAEdvegealatLVVNRLRGGLKVAAVKAPGFGDRrkAMLQDIAILTG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 329 GEIAS-----TFDHPELVKLGTCKlieEVMIGEDKLLHFSGVA-----------------------------------MG 368
Cdd:PRK14104 298 GQAISedlgiKLENVTLQMLGRAK---KVMIDKENTTIVNGAGkkadiearvaqikaqieettsdydreklqerlaklAG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 369 EACTIVLRGATQQILDEAERSLHDALCVLAQTVKDTrTVYGGGCSEMLMAHVVTELANRTPGKESvAMESFAKALRMLPT 448
Cdd:PRK14104 375 GVAVIRVGGATEVEVKERKDRVDDAMHATRAAVEEG-IVPGGGVALLRASEQLKGIKTKNDDQKT-GVEIVRKALSAPAR 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148232533 449 IIADNAGYDSADLVSQLRaahSEGKSTYGLDMKNGTTGDMAELGITESFQVKRQVLLSASEAAEVILRVDDIIKAAPRK 527
Cdd:PRK14104 453 QIAINAGEDGSVIVGKIL---EKEQYSYGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKK 528
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
24-515 |
2.06e-12 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 69.56 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 24 ARLSSFIGAIAIGDLVKSTLGPKGMDKILLSGgrDGAVTVTNDGATILKSI----GIDNPAAQVLVDMSKVQDDEVGDGT 99
Cdd:PTZ00114 23 ARQSLLKGIERLADAVAVTLGPKGRNVIIEQE--YGSPKITKDGVTVAKAIefsdRFENVGAQLIRQVASKTNDKAGDGT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 100 TSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLKATVDHGNDEekfrcDLLNISrtTLSS-------KLL 172
Cdd:PTZ00114 101 TTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKE-----DILNVA--TISAngdveigSLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 173 ThhkDHFAKLAVEAVLRLKGSGNLEaiHVIKKLGGSLTD-SYLDEGFLLDKKigvNQPKRIENANILIANTgmdtdKIkv 251
Cdd:PTZ00114 174 A---DAMDKVGKDGTITVEDGKTLE--DELEVVEGMSFDrGYISPYFVTNEK---TQKVELENPLILVTDK-----KI-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 252 fgsrvrvdstAKVAEIelaekekmkekvERILKHGIN-----CFINR--------QLIYNypeQLFAAAGVMAIEHADF- 317
Cdd:PTZ00114 239 ----------SSIQSI------------LPILEHAVKnkrplLIIAEdvegealqTLIIN---KLRGGLKVCAVKAPGFg 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 318 ----AGVERLSLVTGGEIAS------TFDHPELVKLGTCK------------------------------LIEEVMIGED 357
Cdd:PTZ00114 294 dnrkDILQDIAVLTGATVVSednvglKLDDFDPSMLGSAKkvtvtkdetviltgggdkaeikervellrsQIERTTSEYD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 358 K------LLHFSG-VAmgeacTIVLRGATQQILDEAERSLHDALCVLAQTVKdTRTVYGGGCSeMLMAHVV---TELANR 427
Cdd:PTZ00114 374 KeklkerLAKLSGgVA-----VIKVGGASEVEVNEKKDRIEDALNATRAAVE-EGIVPGGGVA-LLRASKLldkLEEDNE 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 428 TPGKESVAMESFAKALRMLPTIIADNAGYDSADLVSQLRaahSEGKSTYGLDMKNGTTGDMAELGITESFQVKRQVLLSA 507
Cdd:PTZ00114 447 LTPDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKIL---EKKDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDA 523
|
....*...
gi 148232533 508 SEAAEVIL 515
Cdd:PTZ00114 524 ASVASLML 531
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
14-534 |
2.13e-12 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 69.49 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 14 AGADEEKAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSGGrdGAVTVTNDGATILKSIGID----NPAAQVLVDMSK 89
Cdd:PRK12852 2 AAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSF--GAPRITKDGVTVAKEIELEdkfeNMGAQMVREVAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 90 VQDDEVGDGTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLKATVDHGNDEEKFRCDLLNISRTTLSS 169
Cdd:PRK12852 80 KTNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 170 KLLTHHKDhfaKLAVEAVLRLKGSGNLEaihvikklggslTDSYLDEGFLLDKkiGVNQPKRIENANILIANtgMDTDKI 249
Cdd:PRK12852 160 KMIAQAMQ---KVGNEGVITVEENKSLE------------TEVDIVEGMKFDR--GYLSPYFVTNAEKMTVE--LDDAYI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 250 KVFGSRVrvdsTAKVAEIELAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFAAAGVMAIEHADF--AGVERLSLVT 327
Cdd:PRK12852 221 LLHEKKL----SGLQAMLPVLEAVVQSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRrkAMLEDIAILT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 328 GGEIAS-----TFDHPELVKLGTCK------------------------------LIEEVMIGED--KLLHFSGVAMGEA 370
Cdd:PRK12852 297 GGQLISedlgiKLENVTLKMLGRAKkvvidkenttivngagkkadiearvgqikaQIEETTSDYDreKLQERLAKLAGGV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 371 CTIVLRGATQQILDEAERSLHDALCVLAQTVKDTrTVYGGGCSEMLMAHVVTELANRTPGKEsVAMESFAKALRMLPTII 450
Cdd:PRK12852 377 AVIRVGGATEVEVKEKKDRVEDALNATRAAVQEG-IVPGGGVALLRAKKAVGRINNDNADVQ-AGINIVLKALEAPIRQI 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 451 ADNAGYDSADLVSQLRAAHSEgksTYGLDMKNGTTGDMAELGITESFQVKRQVLLSASEAAEVILRVDDIIKAAPRKRVP 530
Cdd:PRK12852 455 AENAGVEGSIVVGKILENKSE---TFGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDAA 531
|
....
gi 148232533 531 DHHP 534
Cdd:PRK12852 532 PAMP 535
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
22-153 |
1.27e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 67.07 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 22 ETARLSSFIGAIAIGDLVKSTLGPKGMDKILlsggrD---GAVTVTNDGATILKSIGIDNP----AAQVLVDMSKVQDDE 94
Cdd:PRK00013 9 EDARRKLLRGVNKLADAVKVTLGPKGRNVVL-----EksfGAPTITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDV 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148232533 95 VGDGTTSVTVLAAELLREAEILVAKKIHPQTIISGWRQATQVAREALLK--------------ATVDHGNDEE 153
Cdd:PRK00013 84 AGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKiskpvedkeeiaqvATISANGDEE 156
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
39-153 |
3.48e-08 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 55.88 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 39 VKSTLGPKGMDKILLSggRDGAVTVTNDGATILKSIGIDNPAAQVLVDM-----SKVqDDEVGDGTTSVTVLAAELLREA 113
Cdd:CHL00093 26 VSVTLGPKGRNVVLEK--KYGSPQIVNDGVTIAKEIELEDHIENTGVALirqaaSKT-NDVAGDGTTTATVLAYAIVKQG 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 148232533 114 EILVAKKIHPQTIISGWRQATQVAREALLK--------------ATVDHGNDEE 153
Cdd:CHL00093 103 MKNVAAGANPISLKRGIEKATQYVVSQIAEyarpvediqaitqvASISAGNDEE 156
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
31-153 |
9.73e-08 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 54.55 E-value: 9.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 31 GAIAIGDLVKSTLGPKGMDKILLSggRDGAVTVTNDGATILKSIGIDNP----AAQVLVDMSKVQDDEVGDGTTSVTVLA 106
Cdd:PLN03167 74 GVNKLADLVGVTLGPKGRNVVLES--KYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVVLA 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 107 AELLREAEILVAKKIHPQTIISGWRQATQVAREALLK-------------ATVDHGNDEE 153
Cdd:PLN03167 152 QGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKmskevedseladvAAVSAGNNYE 211
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
299-398 |
2.33e-05 |
|
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: 46.06 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148232533 299 YPEQLFAAAGVMAIEHADFAGVERLSLVTGGEIASTFDHpeLV---KLGTCKLIE-EVMIGEDK----LLHFSGVAMGEA 370
Cdd:cd03334 143 IAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDD--LLtspKLGTCESFRvRTYVEEHGrsktLMFFEGCPKELG 220
|
90 100
....*....|....*....|....*...
gi 148232533 371 CTIVLRGATQQILDEAERSLHdaLCVLA 398
Cdd:cd03334 221 CTILLRGGDLEELKKVKRVVE--FMVFA 246
|
|
| |
