|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
6-520 |
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: 938.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 6 ILKDNAQEERGESARLSSFVGAIAIGDLVKSTLGPKGMDKILISGNpeSAGGIKVTNDGATILKSIGVDNPAAKVLVDMS 85
Cdd:cd03336 1 ILKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILQSVG--RSGGVTVTNDGATILKSIGVDNPAAKVLVDIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 86 MTQDHEVGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDN---IRDDLLKIARTTLG 162
Cdd:cd03336 79 KVQDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDeeaFREDLLNIARTTLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 163 SKILSQHKEHFAQLAVDAVLRLKGSGNLDAIQIIKKLGGSMNESYLDEGFLLEKLPGMFQPRRVEKAKILIANTPMDTDK 242
Cdd:cd03336 159 SKILTQDKEHFAELAVDAVLRLKGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQPKRIENAKILIANTPMDTDK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 243 VKVFGSRVRVDGVAKVAELEAAEKLKMKEKVDKILAHNCNVFINRQLIYNYPEQLFADAKVMAIEHADFEGIERLALVLG 322
Cdd:cd03336 239 IKIFGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLALVTG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 323 GEIVSTFDSPQTAQFGSCDLIEEIMIGEDRLLRFSGVKLGEACSVVLRGATQQILDESERSLHDALCVLVTHVKESKTVA 402
Cdd:cd03336 319 GEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTRVVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 403 GAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHANGRHNMGIDIEKGEVADV 482
Cdd:cd03336 399 GGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNTTAGLDMRKGTVGDM 478
|
490 500 510
....*....|....*....|....*....|....*...
gi 25147750 483 TKLGVIESYNVKLCMVSSAAEATEQILRVDDIIKAAPR 520
Cdd:cd03336 479 KELGITESFKVKRQVLLSASEAAEMILRVDDIIKCAPR 516
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
5-522 |
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: 904.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 5 QILKDNAQEERGESARLSSFVGAIAIGDLVKSTLGPKGMDKILISGNPEsaGGIKVTNDGATILKSIGVDNPAAKVLVDM 84
Cdd:TIGR02341 1 QIFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSSSD--ASIMVTNDGATILKSIGVDNPAAKVLVDM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 85 SMTQDHEVGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDN---IRDDLLKIARTTL 161
Cdd:TIGR02341 79 SKVQDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDevkFRQDLMNIARTTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 162 GSKILSQHKEHFAQLAVDAVLRLKGSGNLDAIQIIKKLGGSMNESYLDEGFLLEKLPGMFQPRRVEKAKILIANTPMDTD 241
Cdd:TIGR02341 159 SSKILSQHKDHFAQLAVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 242 KVKVFGSRVRVDGVAKVAELEAAEKLKMKEKVDKILAHNCNVFINRQLIYNYPEQLFADAKVMAIEHADFEGIERLALVL 321
Cdd:TIGR02341 239 KVKIFGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLALVT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 322 GGEIVSTFDSPQTAQFGSCDLIEEIMIGEDRLLRFSGVKLGEACSVVLRGATQQILDESERSLHDALCVLVTHVKESKTV 401
Cdd:TIGR02341 319 GGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESRTV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 402 AGAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHANGRHNMGIDIEKGEVAD 481
Cdd:TIGR02341 399 LGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTMGLDMNEGTIAD 478
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 25147750 482 VTKLGVIESYNVKLCMVSSAAEATEQILRVDDIIKAAPRAR 522
Cdd:TIGR02341 479 MRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPRKR 519
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
3-524 |
0e+00 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 891.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 3 PVQILKDNAQEERGESARLSSFVGAIAIGDLVKSTLGPKGMDKILISGNPES-AGGIKVTNDGATILKSIGVDNPAAKVL 81
Cdd:PTZ00212 7 PPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMSEGPrSGNVTVTNDGATILKSVWLDNPAAKIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 82 VDMSMTQDHEVGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDN---IRDDLLKIAR 158
Cdd:PTZ00212 87 VDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDeekFKEDLLNIAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 159 TTLGSKILSQHKEHFAQLAVDAVLRLKGSGNLDAIQIIKKLGGSMNESYLDEGFLLEKLPGMFQPRRVEKAKILIANTPM 238
Cdd:PTZ00212 167 TTLSSKLLTVEKDHFAKLAVDAVLRLKGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVGQPKRLENCKILVANTPM 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 239 DTDKVKVFGSRVRVDGVAKVAELEAAEKLKMKEKVDKILAHNCNVFINRQLIYNYPEQLFADAKVMAIEHADFEGIERLA 318
Cdd:PTZ00212 247 DTDKIKIYGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHADFDGMERLA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 319 LVLGGEIVSTFDSPQTAQFGSCDLIEEIMIGEDRLLRFSGVKLGEACSVVLRGATQQILDESERSLHDALCVLVTHVKES 398
Cdd:PTZ00212 327 AALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTVKDT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 399 KTVAGAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHANGRHNMGIDIEKGE 478
Cdd:PTZ00212 407 RVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGNKTAGIDMEKGT 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 25147750 479 VADVTKLGVIESYNVKLCMVSSAAEATEQILRVDDIIKAAPRARAQ 524
Cdd:PTZ00212 487 VGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRCAPRQREQ 532
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
11-516 |
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: 537.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 11 AQEERGESARLSSFVGAIAIGDLVKSTLGPKGMDKILISGNpesaGGIKVTNDGATILKSIGVDNPAAKVLVDMSMTQDH 90
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSL----GDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 91 EVGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDNIRDDLLKIARTTLGSKILSQHK 170
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 171 EHFAQLAVDAVLRLKGSG---NLDAIQIIKKLGGSMNESYLDEGFLLEK---LPGMfqPRRVEKAKILIANTPMDTdkvk 244
Cdd:cd00309 157 DFLGELVVDAVLKVGKENgdvDLGVIRVEKKKGGSLEDSELVVGMVFDKgylSPYM--PKRLENAKILLLDCKLEY---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 245 vfgsrvrvdgvakvaeleaaeklkmkekvdkilahncnVFINRQLIYNYPEQLFADAKVMAIEHADFEGIERLALVLGGE 324
Cdd:cd00309 231 --------------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGAT 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 325 IVSTFDSPQTAQFGSCDLIEEIMIGEDRLLRFSGVKLGEACSVVLRGATQQILDESERSLHDALCVLVTHVKESKTVAGA 404
Cdd:cd00309 273 IVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 405 GASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHANGRHNMGIDIEKGEVADVTK 484
Cdd:cd00309 353 GAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGGNAGGDVETGEIVDMKE 432
|
490 500 510
....*....|....*....|....*....|..
gi 25147750 485 LGVIESYNVKLCMVSSAAEATEQILRVDDIIK 516
Cdd:cd00309 433 AGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
30-517 |
3.17e-176 |
|
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: 505.58 E-value: 3.17e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 30 IGDLVKSTLGPKGMDKILISgnpeSAGGIKVTNDGATILKSIGVDNPAAKVLVDMSMTQDHEVGDGTTSVTVLAAELLKE 109
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVN----SGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 110 AEKLVNQRIHPQTIISGYRRALGIAQESLKKS-SIESGDNIRDDLLKIARTTLGSKILSQHKEHFAQLAVDAVLRLK--- 185
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIPknd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 186 GSGNLDAIQIIKKLGGSMNESYLDEGFLLEKLPGMFQ-PRRVEKAKILIANTPMDTDKVKVFGSrVRVDGVAKVAELEAA 264
Cdd:pfam00118 157 GSFDLGNIGVVKILGGSLEDSELVDGVVLDKGPLHPDmPKRLENAKVLLLNCSLEYEKTETKAT-VVLSDAEQLERFLKA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 265 EKLKMKEKVDKILAHNCNVFINRQLIYNYPEQLFADAKVMAIEHADFEGIERLALVLGGEIVSTFDSPQTAQFGSCDLIE 344
Cdd:pfam00118 236 EEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 345 EIMIGEDRLLRFSGVKLGEACSVVLRGATQQILDESERSLHDALCVLVTHVKESKTVAGAGASEILMSSAIAVEAQKVAG 424
Cdd:pfam00118 316 EEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 425 KEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHANGRHNMGIDIEKGEVADVTKLGVIESYNVKLCMVSSAAEA 504
Cdd:pfam00118 396 KEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEA 475
|
490
....*....|...
gi 25147750 505 TEQILRVDDIIKA 517
Cdd:pfam00118 476 ASTILRIDDIIKA 488
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
4-518 |
1.72e-144 |
|
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: 425.52 E-value: 1.72e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 4 VQILKDNAQEERGESARLSSFVGAIAIGDLVKSTLGPKGMDKILIsgnpESAGGIKVTNDGATILKSIGVDNPAAKVLVD 83
Cdd:cd03343 1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLV----DSLGDVTITNDGATILKEMDIEHPAAKMLVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 84 MSMTQDHEVGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDNIRDDLLKIARTTLGS 163
Cdd:cd03343 77 VAKTQDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 164 KILSQHKEHFAQLAVDAVLRL--KGSG----NLDAIQIIKKLGGSMNESYLDEGFLLEKL---PGMfqPRRVEKAKILIA 234
Cdd:cd03343 157 KGAEAAKDKLADLVVDAVLQVaeKRDGkyvvDLDNIKIEKKTGGSVDDTELIRGIVIDKEvvhPGM--PKRVENAKIALL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 235 NTPMDTDKVKVfGSRVRVDGVAKVAELEAAEKLKMKEKVDKILAHNCNVFINRQLIYNYPEQLFADAKVMAIEHADFEGI 314
Cdd:cd03343 235 DAPLEVKKTEI-DAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 315 ERLALVLGGEIVSTFDSPQTAQFGSCDLIEEIMIGEDRLLRFSGVKLGEACSVVLRGATQQILDESERSLHDALCVLVTH 394
Cdd:cd03343 314 EKLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 395 VKESKTVAGAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHANGRHNMGIDI 474
Cdd:cd03343 394 LEDGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGNKNAGLDV 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 25147750 475 EKGEVADVTKLGVIESYNVKLCMVSSAAEATEQILRVDDIIKAA 518
Cdd:cd03343 474 YTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIAAK 517
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
3-518 |
4.56e-140 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 414.28 E-value: 4.56e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 3 PVQILKDNAQEERGESARLSSFVGAIAIGDLVKSTLGPKGMDKILISgnpeSAGGIKVTNDGATILKSIGVDNPAAKVLV 82
Cdd:NF041082 2 PILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVD----SLGDVVITNDGVTILKEMDIEHPAAKMIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 83 DMSMTQDHEVGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDNIRDDLLKIARTTLG 162
Cdd:NF041082 78 EVAKTQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 163 SKILSQHKEHFAQLAVDAVLRL---KGSGN--LDAIQIIKKLGGSMNESYLDEGFLLEKL---PGMfqPRRVEKAKILIA 234
Cdd:NF041082 158 GKGAEAAKDKLADLVVDAVKAVaekDGGYNvdLDNIKVEKKVGGSIEDSELVEGVVIDKErvhPGM--PKRVENAKIALL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 235 NTPMDTDKVKVfGSRVRVDGVAKVAE-LEAAEKLkMKEKVDKILAHNCNVFINRQLIYNYPEQLFADAKVMAIEHADFEG 313
Cdd:NF041082 236 DAPLEVKKTEI-DAKISITDPDQLQAfLDQEEKM-LKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 314 IERLALVLGGEIVSTFDSPQTAQFGSCDLIEEIMIGEDRLLRFSGVKLGEACSVVLRGATQQILDESERSLHDALCVLVT 393
Cdd:NF041082 314 MEKLAKATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 394 HVKESKTVAGAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHANGRHNMGID 473
Cdd:NF041082 394 VLEDGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHEKGNKTAGLD 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 25147750 474 IEKGEVADVTKLGVIESYNVKLCMVSSAAEATEQILRVDDIIKAA 518
Cdd:NF041082 474 VYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIAAA 518
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
3-518 |
1.42e-139 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 413.19 E-value: 1.42e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 3 PVQILKDNAQEERGESARLSSFVGAIAIGDLVKSTLGPKGMDKILIsgnpESAGGIKVTNDGATILKSIGVDNPAAKVLV 82
Cdd:NF041083 2 PVLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLV----DSLGDIVITNDGATILKEMDVQHPAAKMLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 83 DMSMTQDHEVGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDNIRDDLLKIARTTLG 162
Cdd:NF041083 78 EVAKTQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 163 SKILSQHKEHFAQLAVDAVLRL------KGSGNLDAIQIIKKLGGSMNESYLDEGFLLEK---LPGMfqPRRVEKAKILI 233
Cdd:NF041083 158 SKGVEEARDYLAEIAVKAVKQVaekrdgKYYVDLDNIQIEKKHGGSIEDTQLIYGIVIDKevvHPGM--PKRVENAKIAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 234 ANTPMDTDKVKVfGSRVRVDGVAKVAELEAAEKLKMKEKVDKILAHNCNVFINRQLIYNYPEQLFADAKVMAIEHADFEG 313
Cdd:NF041083 236 LDAPLEVKKTEI-DAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 314 IERLALVLGGEIVSTFDSPQTAQFGSCDLIEEIMIGEDRLLRFSGVKLGEACSVVLRGATQQILDESERSLHDALCVLVT 393
Cdd:NF041083 315 MEKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVAD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 394 HVKESKTVAGAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHANGRHNMGID 473
Cdd:NF041083 395 AVEDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKWAGIN 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 25147750 474 IEKGEVADVTKLGVIESYNVKLCMVSSAAEATEQILRVDDIIKAA 518
Cdd:NF041083 475 VFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIAAK 519
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
3-517 |
1.13e-136 |
|
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: 405.61 E-value: 1.13e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 3 PVQILKDNAQEERGESARLSSFVGAIAIGDLVKSTLGPKGMDKILIsgnpESAGGIKVTNDGATILKSIGVDNPAAKVLV 82
Cdd:TIGR02339 1 PVFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLV----DSLGDVTITNDGATILKEMDIEHPAAKMLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 83 DMSMTQDHEVGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDNIRDDLLKIARTTLG 162
Cdd:TIGR02339 77 EVAKTQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 163 SKILSQH-KEHFAQLAVDAVLRL-------KGSGNLDAIQIIKKLGGSMNESYLDEGFLLEKL---PGMfqPRRVEKAKI 231
Cdd:TIGR02339 157 SKASAEVaKDKLADLVVEAVKQVaelrgdgKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEvvhPGM--PKRVENAKI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 232 LIANTPMDTDKVKVfGSRVRVDGVAKVAELEAAEKLKMKEKVDKILAHNCNVFINRQLIYNYPEQLFADAKVMAIEHADF 311
Cdd:TIGR02339 235 ALLDAPLEVEKTEI-DAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 312 EGIERLALVLGGEIVSTFDSPQTAQFGSCDLIEEIMIGEDRLLRFSGVKLGEACSVVLRGATQQILDESERSLHDALCVL 391
Cdd:TIGR02339 314 SDIEKLARATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 392 VTHVKESKTVAGAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHANGRHNMG 471
Cdd:TIGR02339 394 ANALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGNKNAG 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 25147750 472 IDIEKGEVADVTKLGVIESYNVKLCMVSSAAEATEQILRVDDIIKA 517
Cdd:TIGR02339 474 INVFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVIAA 519
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
3-517 |
2.43e-129 |
|
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: 387.03 E-value: 2.43e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 3 PVQILKDNAQEERGESARLSSFVGAIAIGDLVKSTLGPKGMDKILISGNpesaGGIKVTNDGATILKSIGVDNPAAKVLV 82
Cdd:cd03340 1 PIILLKEGTDTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGR----GKVTISNDGATILKLLDIVHPAAKTLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 83 DMSMTQDHEVGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSI----ESGDNIRDDLLKIAR 158
Cdd:cd03340 77 DIAKSQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVnidkEDKEEQRELLEKCAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 159 TTLGSKILSQHKEHFAQLAVDAVLRLKGSGNLDAIQIIKKLGGSMNESYLDEGFLLEKlpgMF-------QPRRVEKAKI 231
Cdd:cd03340 157 TALNSKLIASEKEFFAKMVVDAVLSLDDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKK---TFsyagfeqQPKKFKNPKI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 232 LIANTPMDTDKVKVfGSRVRVDGVAKVAELEAAEKLKMKEKVDKILAHNCNVFINRQLIYNYPEQLFADAKVMAIEHADF 311
Cdd:cd03340 234 LLLNVELELKAEKD-NAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 312 EGIERLALVLGGEIVSTFDSPQTAQFGSCDLIEEIMIGEDRLLRFSGVKLGEACSVVLRGATQQILDESERSLHDALCVL 391
Cdd:cd03340 313 EDLKRVAQATGGSIQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 392 VTHVKESKTVAGAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHANGRH-NM 470
Cdd:cd03340 393 RRAIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGkWY 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 25147750 471 GIDIEKGEVADVTKLGVIESYNVKLCMVSSAAEATEQILRVDDIIKA 517
Cdd:cd03340 473 GVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLILSVDETIKN 519
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
16-519 |
1.97e-128 |
|
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: 384.71 E-value: 1.97e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 16 GESARLSSFVGAIAIGDLVKSTLGPKGMDKILIsgnpESAGGIKVTNDGATILKSIGVDNPAAKVLVDMSMTQDHEVGDG 95
Cdd:cd03335 6 GQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLV----DDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 96 TTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDNI-RDDLLKIARTTLGSKILSQHKEHFA 174
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEHLSISVDNLgKESLINVAKTSMSSKIIGADSDFFA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 175 QLAVDAVLRLKGSGNL-------DAIQIIKKLGGSMNESYLDEGFLLE-KLPGMFQPRRVEKAKILIANTPMDTDKVKVf 246
Cdd:cd03335 162 NMVVDAILAVKTTNEKgktkypiKAVNILKAHGKSAKESYLVNGYALNcTRASQGMPTRVKNAKIACLDFNLQKTKMKL- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 247 GSRVRVDGVAKVAELEAAEKLKMKEKVDKILAHNCNVFINRQLIYNYPEQLFADAKVMAIEHADFEGIERLALVLGGEIV 326
Cdd:cd03335 241 GVQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 327 STFDSPQ------TAQFGSCDLIEEIMIGEDRLLRFSGVKLGEACSVVLRGATQQILDESERSLHDALCVlVTHVKESKT 400
Cdd:cd03335 321 STLANLEgeetfdPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCV-VKRTLESNS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 401 -VAGAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHA--------NGRHNMG 471
Cdd:cd03335 400 vVPGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAaaqvkpdkKHLKWYG 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 25147750 472 IDIEKGEVADVTKLGVIESYNVKLCMVSSAAEATEQILRVDDIIKAAP 519
Cdd:cd03335 480 LDLINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIKLNP 527
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
16-519 |
1.35e-125 |
|
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: 377.91 E-value: 1.35e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 16 GESARLSSFVGAIAIGDLVKSTLGPKGMDKILIsgnpESAGGIKVTNDGATILKSIGVDNPAAKVLVDMSMTQDHEVGDG 95
Cdd:TIGR02340 10 GQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLV----DDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 96 TTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDNI-RDDLLKIARTTLGSKILSQHKEHFA 174
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKENLSVSVDELgREALINVAKTSMSSKIIGLDSDFFS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 175 QLAVDAVLRLKGSGN-------LDAIQIIKKLGGSMNESYLDEGFLLE-KLPGMFQPRRVEKAKILIANTPMDTDKVKVf 246
Cdd:TIGR02340 166 NIVVDAVLAVKTTNEngetkypIKAINILKAHGKSARESMLVKGYALNcTVASQQMPKRIKNAKIACLDFNLQKAKMAL- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 247 GSRVRVDGVAKVAELEAAEKLKMKEKVDKILAHNCNVFINRQLIYNYPEQLFADAKVMAIEHADFEGIERLALVLGGEIV 326
Cdd:TIGR02340 245 GVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 327 STF------DSPQTAQFGSCDLIEEIMIGEDRLLRFSGVKLGEACSVVLRGATQQILDESERSLHDALCVlVTHVKESKT 400
Cdd:TIGR02340 325 STLadlegeETFEASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCV-VKRTLESNS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 401 -VAGAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHA--------NGRHNMG 471
Cdd:TIGR02340 404 vVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAaaqlkpekKHLKWYG 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 25147750 472 IDIEKGEVADVTKLGVIESYNVKLCMVSSAAEATEQILRVDDIIKAAP 519
Cdd:TIGR02340 484 LDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIKLNP 531
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
14-515 |
8.45e-120 |
|
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: 362.37 E-value: 8.45e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 14 ERGESARLSSFVGAIAIGDLVKSTLGPKGMDKILISGNpesaGGIKVTNDGATILKSIGVDNPAAKVLVDMSMTQDHEVG 93
Cdd:cd03338 4 EKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGK----GEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 94 DGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDNIRDDLLKIARTTLGSKILSQHKEHF 173
Cdd:cd03338 80 DGTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 174 AQLAVDAVLRL---KGSGNLDA--IQIIKKLGGSMNESYLDEG--FLLEKLPGMFQPRRVEKAKILIAN-------TPMD 239
Cdd:cd03338 160 APIAVDAVLKVidpATATNVDLkdIRIVKKLGGTIEDTELVDGlvFTQKASKKAGGPTRIEKAKIGLIQfclsppkTDMD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 240 tdkvkvfgSRVRVDGVAKVAELEAAEKLKMKEKVDKILAHNCNVF-----INRQLIYNYPEQLFADAKVMAIEHADFEGI 314
Cdd:cd03338 240 --------NNIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLliqksILRDAVSDLALHFLAKLKIMVVKDIEREEI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 315 ERLALVLGGEIVSTFDSPQTAQFGSCDLIEEIMIGEDRLLRFSGVK-LGEACSVVLRGATQQILDESERSLHDALCVLVT 393
Cdd:cd03338 312 EFICKTIGCKPVASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKnPGKTVTILVRGSNKLVLDEAERSLHDALCVIRC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 394 HVKESKTVAGAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHANGRHNMGID 473
Cdd:cd03338 392 LVKKRALIPGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEKNAGIN 471
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 25147750 474 IEKGEVADVTKLGVIESYNVKLCMVSSAAEATEQILRVDDII 515
Cdd:cd03338 472 VRKGAITNILEENVVQPLLVSTSAITLATETVRMILKIDDIV 513
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
3-517 |
2.14e-119 |
|
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: 361.38 E-value: 2.14e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 3 PVQILKDNAQEERGESARLSSFVGAIAIGDLVKSTLGPKGMDKILISGNpesaGGIKVTNDGATILKSIGVDNPAAKVLV 82
Cdd:TIGR02345 3 TIVLLKEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSN----GKATISNDGATILKLLDIVHPAAKTLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 83 DMSMTQDHEVGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSI---ESGDNIRDDLLKIART 159
Cdd:TIGR02345 79 DIAKSQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVtidEEKGEQRELLEKCAAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 160 TLGSKILSQHKEHFAQLAVDAVLRLKGSG-NLDAIQIIKKLGGSMNESYLDEGFLLEKlpgMF-------QPRRVEKAKI 231
Cdd:TIGR02345 159 ALSSKLISHNKEFFSKMIVDAVLSLDRDDlDLKLIGIKKVQGGALEDSQLVNGVAFKK---TFsyagfeqQPKKFANPKI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 232 LIANTPMDTdKVKVFGSRVRVDGVAKVAELEAAEKLKMKEKVDKILAHNCNVFINRQLIYNYPEQLFADAKVMAIEHADF 311
Cdd:TIGR02345 236 LLLNVELEL-KAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 312 EGIERLALVLGGEIVSTFDSPQTAQFGSCDLIEEIMIGEDRLLRFSGVKLGEACSVVLRGATQQILDESERSLHDALCVL 391
Cdd:TIGR02345 315 EDLKRVIKACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 392 VTHVKESKTVAGAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHANGRHNMG 471
Cdd:TIGR02345 395 RRALKNKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGKWYG 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 25147750 472 IDIEKGEVADVTKLGVIESYNVKLCMVSSAAEATEQILRVDDIIKA 517
Cdd:TIGR02345 475 VDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITN 520
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
3-516 |
1.97e-116 |
|
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: 353.91 E-value: 1.97e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 3 PVQILKDNAQEER--GESARLSSFVGAIAIGDLVKSTLGPKGMDKILISGNpesaGGIKVTNDGATILKSIGVDNPAAKV 80
Cdd:cd03339 6 PFIIVREQEKKKRlkGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPD----GEVTVTNDGATILEKMDVDHQIAKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 81 LVDMSMTQDHEVGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSS--IESGDNIRDDLLKIAR 158
Cdd:cd03339 82 LVELSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIAdkIEFSPDNKEPLIQTAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 159 TTLGSKILSQHKEHFAQLAVDAVLRL----KGSGNLDAIQIIKKLGGSMNESYLDEGFLLEK---LPGMfqPRRVEKAKI 231
Cdd:cd03339 162 TSLGSKIVSRCHRQFAEIAVDAVLSVadleRKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKdfsHPQM--PKEVKDAKI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 232 LIANTPMDTDKVKVfGSRVRVDGVAKVAELEAAEKLKMKEKVDKILAHNCNVFI---------NRQLIYNypeQLFADAK 302
Cdd:cd03339 240 AILTCPFEPPKPKT-KHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVIcqwgfddeaNHLLLQN---GLPAVRW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 303 VMAIEhadfegIERLALVLGGEIVSTFDSPQTAQFGSCDLIEEIMIG--EDRLLRFSGVKLGEACSVVLRGATQQILDES 380
Cdd:cd03339 316 VGGVE------IELIAIATGGRIVPRFEDLSPEKLGKAGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 381 ERSLHDALCVLVTHVKESKTVAGAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLR 460
Cdd:cd03339 390 KRSLHDALCVVRNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVK 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 25147750 461 AEH-ANGRHNMGIDIEKGEVADVTKLGVIESYNVKLCMVSSAAEATEQILRVDDIIK 516
Cdd:cd03339 470 ARQvKEKNPHLGIDCLGRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
3-516 |
5.86e-105 |
|
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: 324.45 E-value: 5.86e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 3 PVQILKDNAQEER--GESARLSSFVGAIAIGDLVKSTLGPKGMDKILISGNpesaGGIKVTNDGATILKSIGVDNPAAKV 80
Cdd:TIGR02343 10 PFIIIKDQDNKKRlkGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPD----GDITVTNDGATILSQMDVDNQIAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 81 LVDMSMTQDHEVGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSS--IESGDNIRDDLLKIAR 158
Cdd:TIGR02343 86 MVELSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISdeISADNNNREPLIQAAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 159 TTLGSKILSQHKEHFAQLAVDAVLRL----KGSGNLDAIQIIKKLGGSMNESYLDEGFLLEK---LPGMfqPRRVEKAKI 231
Cdd:TIGR02343 166 TSLGSKIVSKCHRRFAEIAVDAVLNVadmeRRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKdfsHPQM--PKEVEDAKI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 232 LIANTPMDTDKVKVfGSRVRVDGVAKVAELEAAEKLKMKEKVDKILAHNCNVFINRQLIYNYPEQLFADAKVMAIEHADF 311
Cdd:TIGR02343 244 AILTCPFEPPKPKT-KHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 312 EGIERLALVLGGEIVSTFDSPQTAQFGSCDLIEEIMIG--EDRLLRFSGVKLGEACSVVLRGATQQILDESERSLHDALC 389
Cdd:TIGR02343 323 QELELIAIATGGRIVPRFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALC 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 390 VLVTHVKESKTVAGAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHANGRH- 468
Cdd:TIGR02343 403 VVRNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNp 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 25147750 469 NMGIDIEKGEVADVTKLGVIESYNVKLCMVSSAAEATEQILRVDDIIK 516
Cdd:TIGR02343 483 NLGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVIS 530
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
13-518 |
3.30e-104 |
|
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: 322.12 E-value: 3.30e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 13 EERGESARLSSFVGAIAIGDLVKSTLGPKGMDKILISGNpesaGGIKVTNDGATILKSIGVDNPAAKVLVDMSMTQDHEV 92
Cdd:TIGR02342 4 KDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGK----GEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 93 GDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDNIRDDLLKIARTTLGSKILSQHKEH 172
Cdd:TIGR02342 80 GDGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 173 FAQLAVDAVLRLKGSG-----NLDAIQIIKKLGGSMNESYLDEGFLLEKLPGMFQ--PRRVEKAKI-----LIANTPMDT 240
Cdd:TIGR02342 160 LAPLAVDAVLKVIDPEnaknvDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAggPTRIEKAKIgliqfQISPPKTDM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 241 DKVKVFGSRVRVDGVAKvaeleaAEKLKMKEKVDKILAHNCNVF-----INRQLIYNYPEQLFADAKVMAIEHADFEGIE 315
Cdd:TIGR02342 240 ENQIIVNDYAQMDRVLK------EERAYILNIVKKIKKTGCNVLliqksILRDAVNDLALHFLAKMKIMVVKDIEREEIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 316 RLALVLGGEIVSTFDSPQTAQFGSCDLIEEIMIGEDRLLRFSGVK-LGEACSVVLRGATQQILDESERSLHDALCVLVTH 394
Cdd:TIGR02342 314 FICKTIGCKPIASIDHFTADKLGSAELVEEVDSDGGKIIKITGIQnAGKTVTVVVRGSNKLVIDEAERSLHDALCVIRCL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 395 VKESKTVAGAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHANGRHNMGIDI 474
Cdd:TIGR02342 394 VKKRGLIAGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGEKTAGISV 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 25147750 475 EKGEVADVTKLGVIESYNVKLCMVSSAAEATEQILRVDDIIKAA 518
Cdd:TIGR02342 474 RKGGITNMLEEHVLQPLLVTTSAITLASETVRSILKIDDIVFTR 517
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
3-515 |
3.56e-100 |
|
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: 310.38 E-value: 3.56e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 3 PVQILKDNAQEERGESARLSSFVGAIAIGDLVKSTLGPKGMDKILIsgnpESAGGIKVTNDGATILKSIGVDNPAAKVLV 82
Cdd:cd03337 1 PVLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLL----DPMGGIVLTNDGNAILREIDVAHPAAKSMI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 83 DMSMTQDHEVGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDNIRDDLLKIARTTLG 162
Cdd:cd03337 77 ELSRTQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 163 SKILSQHKEHFAQLAVDAVLRLKGSGNLDAIQI-IKK-------LGGSMNESYLDEGFLLEK---LPGMfqPRRVEKAKI 231
Cdd:cd03337 157 TKFVSRWSDLMCNLALDAVKTVAVEENGRKKEIdIKRyakvekiPGGEIEDSRVLDGVMLNKdvtHPKM--RRRIENPRI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 232 LIANTPMdtdkvkvfgsrvrvdgvakvaeleaaEKLKMKEKVDKILAhncnvfinrqliynypEQLFADAKVMAIEHADF 311
Cdd:cd03337 235 VLLDCPL--------------------------EYLVITEKGVSDLA----------------QHYLVKAGITALRRVRK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 312 EGIERLALVLGGEIVSTFDSPQTAQFG-SCDLIEEIMIGEDRLLRFSGVKLGEACSVVLRGATQQILDESERSLHDALCV 390
Cdd:cd03337 273 TDNNRIARACGATIVNRPEELTESDVGtGAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 391 LVTHVKESKTVAGAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHANGR-HN 469
Cdd:cd03337 353 ARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGEnST 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 25147750 470 MGIDIEKGEVADVTKLGVIESYNVKLCMVSSAAEATEQILRVDDII 515
Cdd:cd03337 433 WGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
3-515 |
1.76e-94 |
|
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: 297.42 E-value: 1.76e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 3 PVQILKDNAQEERGESARLSSFVGAIAIGDLVKSTLGPKGMDKILIsgnpESAGGIKVTNDGATILKSIGVDNPAAKVLV 82
Cdd:TIGR02344 1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLL----DPMGGIVMTNDGNAILREIDVAHPAAKSMI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 83 DMSMTQDHEVGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDNIRDDLLKIARTTLG 162
Cdd:TIGR02344 77 ELSRTQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 163 SKILSQHKEHFAQLAVDAVLRLKGSGNLDAIQIIKKL-------GGSMNESYLDEGFLLEK---LPGMfqPRRVEKAKIL 232
Cdd:TIGR02344 157 TKFVSRWSDLMCDLALDAVRTVQRDENGRKEIDIKRYakvekipGGDIEDSCVLKGVMINKdvtHPKM--RRYIENPRIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 233 IANTPMDTDKVKVfGSRVRVDGVAKVAELEAAEKLKMKEKVDKILAHNCNVFINRQLIYNYPEQLFADAKVMAIEHADFE 312
Cdd:TIGR02344 235 LLDCPLEYKKGES-QTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 313 GIERLALVLGGEIVSTFDSPQTAQFGS-CDLIEEIMIGEDRLLRFSGVKLGEACSVVLRGATQQILDESERSLHDALCVL 391
Cdd:TIGR02344 314 DNNRIARACGATIVNRPEELRESDVGTgCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 392 VTHVKESKTVAGAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHANG-RHNM 470
Cdd:TIGR02344 394 RNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQEnNCTW 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 25147750 471 GIDIEKGEVADVTKLGVIESYNVKLCMVSSAAEATEQILRVDDII 515
Cdd:TIGR02344 474 GIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
16-519 |
6.90e-90 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 284.28 E-value: 6.90e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 16 GESARLSSFVGAIAIGDLVKSTLGPKGMDKILISgnpeSAGGIKVTNDGATILKSIGVDNP----AAKVLVDMSMTQDHE 91
Cdd:COG0459 8 GEDARRANIRGVKALADAVKVTLGPKGRNVMLVK----SFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 92 VGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDniRDDLLKIARTTLGSkilsqhKE 171
Cdd:COG0459 84 AGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDD--KEELAQVATISANG------DE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 172 HFAQLAVDAVLRLkgsGNLDAIQIIKKlGGSMNESYLDEGFLLEK---LPGMF-----QPRRVEKAKILIantpmdTDKv 243
Cdd:COG0459 156 EIGELIAEAMEKV---GKDGVITVEEG-KGLETELEVVEGMQFDKgylSPYFVtdpekMPAELENAYILL------TDK- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 244 kvfgsrvrvdgvakvaELEAAEKLkmKEKVDKILAHNCNVFINRQLIYNYPEQLFADAKVMAIE-----HADFEG----- 313
Cdd:COG0459 225 ----------------KISSIQDL--LPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLrvvavKAPGFGdrrka 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 314 -IERLALVLGGEIVS-----TFDSPQTAQFGSCDLIEeimIGEDRLLRFSGVKLGEACSVVLRGATQQILDESERSLHDA 387
Cdd:COG0459 287 mLEDIAILTGGRVISedlglKLEDVTLDDLGRAKRVE---VDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 388 LCVlVTHVKESKTVAGAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEhanGR 467
Cdd:COG0459 364 LHA-TRAAVEEGIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA---KD 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 25147750 468 HNMGIDIEKGEVADVTKLGVIESYNVKLCMVSSAAEATEQILRVDDIIKAAP 519
Cdd:COG0459 440 KGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKP 491
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
30-517 |
8.75e-87 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239457 [Multi-domain] Cd Length: 472 Bit Score: 275.64 E-value: 8.75e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 30 IGDLVKSTLGPKGMDKILIsgNPEsaGGIKVTNDGATILKSIGVDNPAAKVLVDMSMTQDHEVGDGTTSVTVLAAELLKE 109
Cdd:cd03341 20 LSQITRTSYGPNGMNKMVI--NHL--EKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGELLEK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 110 AEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDNIRD--DLLKIARTTLGSKILSqHKEHFAQLAVDAVLRLK-- 185
Cdd:cd03341 96 AEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIEDLRNkeEVSKALKTAIASKQYG-NEDFLSPLVAEACISVLpe 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 186 --GSGNLDAIQIIKKLGGSMNESYLDEGFLLEKLPGMfQPRRVEKAKILIANTPMDtdkvkvFGSRVRVDGvakvaelea 263
Cdd:cd03341 175 niGNFNVDNIRVVKILGGSLEDSKVVRGMVFKREPEG-SVKRVKKAKVAVFSCPFD------IGVNVIVAG--------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 264 aeklkmkEKVDKILAHNCNVFinrqliynypeqlfadaKVMAIE-HADFEgIERLALVLGGEIVSTFDSPQTAQFGSCDL 342
Cdd:cd03341 239 -------GSVGDLALHYCNKY-----------------GIMVIKiNSKFE-LRRLCRTVGATPLPRLGAPTPEEIGYCDS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 343 IEEIMIGEDRLLRFSGVK-LGEACSVVLRGATQQILDESERSLHDALCVLVTHVKESKTVAGAGASEILMSSAIAVEAQK 421
Cdd:cd03341 294 VYVEEIGDTKVVVFRQNKeDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEIELAKKLKEYGEK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 422 VAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHANGRHNMGIDIEKGE--VADVTKLGVIESYNVKLCMVS 499
Cdd:cd03341 374 TPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSAGVDIESGDegTKDAKEAGIFDHLATKKWAIK 453
|
490
....*....|....*...
gi 25147750 500 SAAEATEQILRVDDIIKA 517
Cdd:cd03341 454 LATEAAVTVLRVDQIIMA 471
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
5-519 |
4.43e-80 |
|
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: 260.03 E-value: 4.43e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 5 QILKDNAQEERG-ESARLSSFVGAIAIGDLVKSTLGPKGMDKILISgnpeSAGGIKVTNDGATILKSIGVDNPAAKVLVD 83
Cdd:TIGR02346 4 SLLKEGYRHFSGlEEAVIKNIEACKELSQITRTSLGPNGMNKMVIN----HLEKLFVTNDAATILRELEVQHPAAKLLVM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 84 MSMTQDHEVGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDNIRD--DLLKIARTTL 161
Cdd:TIGR02346 80 ASEMQENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDLRDkdELIKALKASI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 162 GSKILSqHKEHFAQLAVDAVLRLK----GSGNLDAIQIIKKLGGSMNESYLDEGFLLEKLP-GMFqpRRVEKAKILIANT 236
Cdd:TIGR02346 160 SSKQYG-NEDFLAQLVAQACSTVLpknpQNFNVDNIRVCKILGGSLSNSEVLKGMVFNREAeGSV--KSVKNAKVAVFSC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 237 PMDTDKVKVFGSrVRVDGVAKVAELEAAEKLKMKEKVDKILAHNCNVFINRQLIYNYPEQLFADAKVMAIE-HADFEgIE 315
Cdd:TIGR02346 237 PLDTATTETKGT-VLIHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKiPSKFE-LR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 316 RLALVLGGEIVSTFDSPQTAQFGSCDLIEEIMIGEDRLLRFSGVKLGEACS-VVLRGATQQILDESERSLHDALCVLVTH 394
Cdd:TIGR02346 315 RLCKTVGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGDSKIStIILRGSTDNLLDDIERAIDDGVNTVKAL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 395 VKESKTVAGAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHANGRHNMGIDI 474
Cdd:TIGR02346 395 VKDGRLLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAHKKGNKSKGIDI 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 25147750 475 EKG--EVADVTKLGVIESYNVKLCMVSSAAEATEQILRVDDIIKAAP 519
Cdd:TIGR02346 475 EAEsdGVKDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQIIMAKP 521
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
4-517 |
7.15e-77 |
|
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: 251.58 E-value: 7.15e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 4 VQILKDNAQEERGESARLSSFVGAIAIGDLVKSTLGPKGMDKILISGnpesAGGIKVTNDGATILKSIGVDNPAAKVLVD 83
Cdd:TIGR02347 2 VKLLNPKAESLRRDAALMMNINAARGLQDVLKTNLGPKGTLKMLVSG----AGDIKLTKDGNVLLNEMQIQHPTASMIAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 84 MSMTQDHEVGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDNI-RDDLLKIARTTLG 162
Cdd:TIGR02347 78 AATAQDDITGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEVdREFLLNVARTSLR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 163 SKILSQHKEHFAQLAVDAVLRLKGSG---NLDAIQIIKKLGGSMNESYLDEGFLLE---KLPGMfqPRRVEKAKILIANT 236
Cdd:TIGR02347 158 TKLPADLADQLTEIVVDAVLAIKKDGediDLFMVEIMEMKHKSATDTTLIRGLVLDhgaRHPDM--PRRVKNAYILTCNV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 237 PMDTDKVKVFGSRVRVDgVAKVAELEAAEKLKMKEKVDKIL---------AHNCN-VFINRQLIYNYPEQLFADAKVMAI 306
Cdd:TIGR02347 236 SLEYEKTEVNSGFFYSS-AEQREKLVKAERKFVDDRVKKIIelkkkvcgkSPDKGfVVINQKGIDPPSLDLLAKEGIMAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 307 EHADFEGIERLALVLGGEIVSTFDSPQTAQFGSCDLIEEIMIGEDRLLRFSGVKLGEACSVVLRGATQQILDESERSLHD 386
Cdd:TIGR02347 315 RRAKRRNMERLTLACGGEALNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 387 ALCVLVTHVKESKTVAGAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHANG 466
Cdd:TIGR02347 395 GLRAVKNAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHDEG 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 25147750 467 RHNMGIDIEKGEVADVTKLGVIESYNVKLCMVSSAAEATEQILRVDDIIKA 517
Cdd:TIGR02347 475 GEVVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMRA 525
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
26-517 |
3.43e-72 |
|
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: 237.93 E-value: 3.43e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 26 GAIAIGDLVKSTLGPKGMDKILISGnpesAGGIKVTNDGATILKSIGVDNPAAKVLVDMSMTQDHEVGDGTTSVTVLAAE 105
Cdd:cd03342 20 AAKGLQDVLKTNLGPKGTLKMLVSG----AGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 106 LLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESG-DNIRDDLLKIARTTLGSKILSQHKEHFAQLAVDAVLRL 184
Cdd:cd03342 96 LLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEiDTDRELLLSVARTSLRTKLHADLADQLTEIVVDAVLAI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 185 KGSG---NLDAIQIIKKLGGSMNESYLDEGFLLE---KLPGMfqPRRVEKAKILIANTPMDTDKVKVFGSRVRvdgvakv 258
Cdd:cd03342 176 YKPDepiDLHMVEIMQMQHKSDSDTKLIRGLVLDhgaRHPDM--PKRVENAYILTCNVSLEYEKTEVNSGFFY------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 259 aeleaaeklkmkekvdkilahncNVFINRQLIYNYPEQLFADAKVMAIEHADFEGIERLALVLGGEIVSTFDSPQTAQFG 338
Cdd:cd03342 247 -----------------------SVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPECLG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 339 SCDLIEEIMIGEDRLLRFSGVKLGEACSVVLRGATQQILDESERSLHDALCVLVTHVKESKTVAGAGASEILMSSAIAVE 418
Cdd:cd03342 304 YAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHLKEF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 419 AQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRAEHANGRHNMGIDIEKGEVADVTKLGVIESYNVKLCMV 498
Cdd:cd03342 384 KKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVGGVDLDTGEPMDPESEGIWDNYSVKRQIL 463
|
490
....*....|....*....
gi 25147750 499 SSAAEATEQILRVDDIIKA 517
Cdd:cd03342 464 HSATVIASQLLLVDEIIRA 482
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
150-397 |
1.51e-59 |
|
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: 195.76 E-value: 1.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 150 RDDLLKIARTTLGSKIlSQHKEHFAQLAVDAVLRLKGSG---NLDAIQIIKKLGGSMNESYLDEGFLLEK---LPGMfqP 223
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVGPDNrmdDLGVIKVEKIPGGSLEDSELVVGVVFDKgyaSPYM--P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 224 RRVEKAKILIANTPMDTdkvkvfgsrvrvdgvakvaeleaaeklkmkekvdkilahncnVFINRQLIYNYPEQLFADAKV 303
Cdd:cd03333 78 KRLENAKILLLDCPLEY------------------------------------------VVIAEKGIDDLALHYLAKAGI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 304 MAIEHADFEGIERLALVLGGEIVSTFDSPQTAQFGSCDLIEEIMIGEDRLLRFSGVKLGEACSVVLRGATQQILDESERS 383
Cdd:cd03333 116 MAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRS 195
|
250
....*....|....
gi 25147750 384 LHDALCVLVTHVKE 397
Cdd:cd03333 196 LHDALCAVRAAVEE 209
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
16-144 |
1.22e-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: 82.50 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 16 GESARLSSFVGAIAIGDLVKSTLGPKGMDKILisgnPESAGGIKVTNDGATILKSIGVDNP----AAKVLVDMSMTQDHE 91
Cdd:cd03344 6 GEEARKALLRGVNKLADAVKVTLGPKGRNVVI----EKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 25147750 92 VGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIE 144
Cdd:cd03344 82 AGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKP 134
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
16-157 |
7.04e-14 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 74.18 E-value: 7.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 16 GESARLSSFVGAIAIGDLVKSTLGPKGMDKILisgnPESAGGIKVTNDGATILKSI----GVDNPAAKVLVDMSMTQDHE 91
Cdd:PTZ00114 20 GDEARQSLLKGIERLADAVAVTLGPKGRNVII----EQEYGSPKITKDGVTVAKAIefsdRFENVGAQLIRQVASKTNDK 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25147750 92 VGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDNirDDLLKIA 157
Cdd:PTZ00114 96 AGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTK--EDILNVA 159
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
17-157 |
2.06e-12 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 69.36 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 17 ESARLSSFVGAIAIGDLVKSTLGPKGMDKILisgnPESAGGIKVTNDGATILKSIGVDNPAAKVLVDM-----SMTQDhE 91
Cdd:PRK12850 10 TDARDRLLRGVNILANAVKVTLGPKGRNVVL----EKSFGAPRITKDGVTVAKEIELEDKFENMGAQMvkevaSKTND-L 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25147750 92 VGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDNirDDLLKIA 157
Cdd:PRK12850 85 AGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSS--KEIAQVA 148
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
25-157 |
1.55e-11 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 66.75 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 25 VGAIAigDLVKSTLGPKGMDKILisgnPESAGGIKVTNDGATILKSIGVDNP----AAKVLVDMSMTQDHEVGDGTTSVT 100
Cdd:PRK12849 19 VNKLA--DAVKVTLGPKGRNVVI----DKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTAT 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 25147750 101 VLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDNirDDLLKIA 157
Cdd:PRK12849 93 VLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGS--EEIAQVA 147
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
16-148 |
1.35e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 63.60 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 16 GESARLSSFVGAIAIGDLVKSTLGPKGMDKILisgnPESAGGIKVTNDGATILKSIGVDNPAAKVLVDM-----SMTQDh 90
Cdd:PRK00013 8 GEDARRKLLRGVNKLADAVKVTLGPKGRNVVL----EKSFGAPTITKDGVTVAKEIELEDPFENMGAQLvkevaSKTND- 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 25147750 91 EVGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDN 148
Cdd:PRK00013 83 VAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDK 140
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
17-528 |
2.48e-10 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 62.84 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 17 ESARLSSFVGAIAIGDLVKSTLGPKGMDKILisgnPESAGGIKVTNDGATILKSIGVDNP----AAKVLVDMSMTQDHEV 92
Cdd:PRK12851 10 VEAREKMLRGVNILADAVKVTLGPKGRNVVI----DKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 93 GDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDNirDDLLKIArttlgsKILSQHKEH 172
Cdd:PRK12851 86 GDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTN--AEIAQVA------TISANGDAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 173 FAQLAVDAVLRLKGSGnldaiqIIKKLGGSMNESYLD--EGFLLEKlpGMFQPRRVEkakiliantpmDTDKVKVFGSRV 250
Cdd:PRK12851 158 IGRLVAEAMEKVGNEG------VITVEESKTAETELEvvEGMQFDR--GYLSPYFVT-----------DADKMEAELEDP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 251 RVDGV-AKVAELEAAekLKMKEKVDK------ILAHNCNVFINRQLIYNYPEQLFADAKVMAIEHAD--FEGIERLALVL 321
Cdd:PRK12851 219 YILIHeKKISNLQDL--LPVLEAVVQsgkpllIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDrrKAMLEDIAILT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 322 GGEIVS-----TFDSPQTAQFGSCDLI-----EEIMIG-------------------------------EDRLLRFSGvk 360
Cdd:PRK12851 297 GGTVISedlgiKLENVTLEQLGRAKKVvvekeNTTIIDgagskteiegrvaqiraqieettsdydreklQERLAKLAG-- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 361 lGEAcsvVLR--GATQQILDESERSLHDALCVLVTHVKESkTVAGAGASeiLMSSAIAVEAQKVA-GKEALAVEAFGRAL 437
Cdd:PRK12851 375 -GVA---VIRvgASTEVEVKEKKDRVDDALHATRAAVEEG-IVPGGGVA--LLRAVKALDKLETAnGDQRTGVEIVRRAL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 438 AQLPTIICDNAGLDSAELVTRLRaehaNGRHNMGIDIEKGEVADVTKLGVIESYNVKLCMVSSAAEATEQILRVDDIIKA 517
Cdd:PRK12851 448 EAPVRQIAENAGAEGSVVVGKLR----EKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAE 523
|
570
....*....|.
gi 25147750 518 APRARAQDNRP 528
Cdd:PRK12851 524 KPKKEPAPPAP 534
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
26-526 |
1.67e-09 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 60.32 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 26 GAIAIGDLVKSTLGPKGMDKILISgnpeSAGGIKVTNDGATILKSIGVDNP----AAKVLVDMSMTQDHEVGDGTTSVTV 101
Cdd:PLN03167 74 GVNKLADLVGVTLGPKGRNVVLES----KYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGTTTSVV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 102 LAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSSIESGDNirdDLLKIARTTLGS--KILSQHKEHFAQLAVD 179
Cdd:PLN03167 150 LAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDS---ELADVAAVSAGNnyEVGNMIAEAMSKVGRK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 180 AVLRL-KGSGNLDAIQIIKklGGSMNESYLDEGFLL--EKLPGMFqprrvEKAKILIANTPMDT--DKVKVFGSRVR--- 251
Cdd:PLN03167 227 GVVTLeEGKSAENNLYVVE--GMQFDRGYISPYFVTdsEKMSVEY-----DNCKLLLVDKKITNarDLIGILEDAIRggy 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 252 -VDGVAKVAELEAAEKL---KMKEKVdKILAHNCNVFINRQLIYNYPEQLFADAKVMAIEHA-DFEGIERLALVLGGEIV 326
Cdd:PLN03167 300 pLLIIAEDIEQEALATLvvnKLRGSL-KIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGlSLDKVGKEVLGTAAKVV 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 327 STFDSPQTAQFGSC------------DLIEEIMIG-EDRLLRFSGVKLGEACSVVLRGA-TQQILDESERSLHDALCVLV 392
Cdd:PLN03167 379 LTKDTTTIVGDGSTqeavnkrvaqikNLIEAAEQDyEKEKLNERIAKLSGGVAVIQVGAqTETELKEKKLRVEDALNATK 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 393 THVKESKTVAGAGASEILMSSAIAVEAQKVAGKEALAVEAFGRALAQLPTIICDNAGLDSAELVTRLRaehANGRHNMGI 472
Cdd:PLN03167 459 AAVEEGIVVGGGCTLLRLASKVDAIKDTLENDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVL---SNDNPKFGY 535
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 473 DIEKGEVADVTKLGVIESYNVKLCMVSSAAEATEQILRVDDII------KAAPRARAQDN 526
Cdd:PLN03167 536 NAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVveikepEPVPAGNPMDN 595
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
16-149 |
4.33e-09 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 58.89 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 16 GESARLSSFVGAIAIGDLVKSTLGPKGMDKILisgnPESAGGIKVTNDGATILKSIGVD----NPAAKVLVDMSMTQDHE 91
Cdd:PRK14104 9 GVDARDRMLRGVDILANAVKVTLGPKGRNVVL----DKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKSADA 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 92 VGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSS--IESGDNI 149
Cdd:PRK14104 85 AGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSkkVTSNDEI 144
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
18-142 |
4.89e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 55.62 E-value: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 18 SARLSSFVGAIAIGDLVKSTLGPKGMDKILisgnPESAGGIKVTNDGATILKSIGVD----NPAAKVLVDMSMTQDHEVG 93
Cdd:PRK12852 11 DARDRMLRGVDILANAVKVTLGPKGRNVVI----EKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKTNDLAG 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 25147750 94 DGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRALGIAQESLKKSS 142
Cdd:PRK12852 87 DGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRA 135
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
133-394 |
7.76e-07 |
|
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: 50.68 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 133 IAQESLKKSSIESGDNIRDDLLKIARTtlgskilsqhkehfAQLAVDAVLRLKGSGN-LDAIQIIKKLGGSMNESYLDEG 211
Cdd:cd03334 3 LLAQLLKDEGISNDESWLDILLPLVWK--------------AASNVKPDVRAGDDMDiRQYVKIKKIPGGSPSDSEVVDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 212 FLLEK---LPGMfqPRRVEKAKILIANTPMDTDKVKVfgsrvrvdGVAKVAELEAAEKLKMKEKVDKILAHNCNVFINRQ 288
Cdd:cd03334 69 VVFTKnvaHKRM--PSKIKNPRILLLQGPLEYQRVEN--------KLLSLDPVILQEKEYLKNLVSRIVALRPDVILVEK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 289 LIYNYPEQLFADAKVMAIEHADFEGIERLALVLGGEIVSTFDSPQTAQ-FGSCDLIE-EIMIGEDR----LLRFSG--VK 360
Cdd:cd03334 139 SVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDLLTSPkLGTCESFRvRTYVEEHGrsktLMFFEGcpKE 218
|
250 260 270
....*....|....*....|....*....|....
gi 25147750 361 LGeaCSVVLRGATQQILDESERSLHdaLCVLVTH 394
Cdd:cd03334 219 LG--CTILLRGGDLEELKKVKRVVE--FMVFAAY 248
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
5-130 |
9.64e-07 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 51.26 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147750 5 QIL-KDNAQE--ERGesarLSSFVGAIAIgdlvksTLGPKGMDKILisgnPESAGGIKVTNDGATILKSIGVDNPAAKVL 81
Cdd:CHL00093 4 KILyQDNARRalERG----MDILAEAVSV------TLGPKGRNVVL----EKKYGSPQIVNDGVTIAKEIELEDHIENTG 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 25147750 82 VDM-----SMTQDhEVGDGTTSVTVLAAELLKEAEKLVNQRIHPQTIISGYRRA 130
Cdd:CHL00093 70 VALirqaaSKTND-VAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKA 122
|
|
| |
