|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
8-530 |
0e+00 |
|
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: 1003.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 8 PILVLKEDTDTSQGKSQIISNINACQAVTNCIKTTLGPRGMDKLIHAEN-KVTITNDGATVLALLDIVHPAAAVLVDIAK 86
Cdd:cd03340 1 PIILLKEGTDTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRgKVTISNDGATILKLLDIVHPAAKTLVDIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 87 SQDDEVGDGTTSVTVLAGEFLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAINLSNKPYEETQKLLLRCAETTLN 166
Cdd:cd03340 81 SQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKEEQRELLEKCAATALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 167 SKLVSTYRSFFAKMVVDAVNILEDDMDKDMIGIKKVPGATCLDSMLIKGVAFKKTFSYAGFEQQPKKFKNPKILLLNVEL 246
Cdd:cd03340 161 SKLIASEKEFFAKMVVDAVLSLDDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAGFEQQPKKFKNPKILLLNVEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 247 ELKAEKDNAEIRINDPLIYQSIIDAEWKIIYDKLEAIYDIGANVVLSKLPIGDIATQFFAEKNIFCAGRVDEIDMKRVAK 326
Cdd:cd03340 241 ELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 327 ATGGLVQTTIHGITDCCLGTCGVFEEMQLGSERYNIFTECPNTKTTTIILRGGAQQFIDEAERSLHDAIMIVRRSIKTNS 406
Cdd:cd03340 321 ATGGSIQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 407 IVVGGGAIEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLRKEYAmnKGQGMKYGVDCIN 486
Cdd:cd03340 401 VVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHA--QGGGKWYGVDINN 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 18250944 487 GGICDAYAACIWEPSLVKRNAIYSATEAACLVLSIDETIKQQNS 530
Cdd:cd03340 479 EGIADNFEAFVWEPSLVKINALTAATEAACLILSVDETIKNPKS 522
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
8-530 |
0e+00 |
|
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: 782.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 8 PILVLKEDTDTSQGKSQIISNINACQAVTNCIKTTLGPRGMDKLIH-AENKVTITNDGATVLALLDIVHPAAAVLVDIAK 86
Cdd:TIGR02345 3 TIVLLKEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVgSNGKATISNDGATILKLLDIVHPAAKTLVDIAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 87 SQDDEVGDGTTSVTVLAGEFLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAINLSNKPyEETQKLLLRCAETTLN 166
Cdd:TIGR02345 83 SQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEK-GEQRELLEKCAATALS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 167 SKLVSTYRSFFAKMVVDAVNILE-DDMDKDMIGIKKVPGATCLDSMLIKGVAFKKTFSYAGFEQQPKKFKNPKILLLNVE 245
Cdd:TIGR02345 162 SKLISHNKEFFSKMIVDAVLSLDrDDLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAGFEQQPKKFANPKILLLNVE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 246 LELKAEKDNAEIRINDPLIYQSIIDAEWKIIYDKLEAIYDIGANVVLSKLPIGDIATQFFAEKNIFCAGRVDEIDMKRVA 325
Cdd:TIGR02345 242 LELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 326 KATGGLVQTTIHGITDCCLGTCGVFEEMQLGSERYNIFTECPNTKTTTIILRGGAQQFIDEAERSLHDAIMIVRRSIKTN 405
Cdd:TIGR02345 322 KACGGSIQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 406 SIVVGGGAIEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLRKEYAMnkgQGMKYGVDCI 485
Cdd:TIGR02345 402 KIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAK---GGKWYGVDIN 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 18250944 486 NGGICDAYAACIWEPSLVKRNAIYSATEAACLVLSIDETIKQQNS 530
Cdd:TIGR02345 479 TEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETITNPKS 523
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
16-526 |
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 18250944 16 TDTSQGKSQIISNINACQAVTNCIKTTLGPRGMDK-LIHAENKVTITNDGATVLALLDIVHPAAAVLVDIAKSQDDEVGD 94
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKmLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 95 GTTSVTVLAGEFLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAINLSnkpyEETQKLLLRCAETTLNSKLVSTYR 174
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPID----VEDREELLKVATTSLNSKLVSGGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 175 SFFAKMVVDAVNILEDDM---DKDMIGIKKVPGATCLDSMLIKGVAFKKTFSYAGFeqqPKKFKNPKILLLNVELElkae 251
Cdd:cd00309 157 DFLGELVVDAVLKVGKENgdvDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYM---PKRLENAKILLLDCKLE---- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 252 kdnaeirindpliyqsiidaewkiiydkleaiydigaNVVLSKLPIGDIATQFFAEKNIFCAGRVDEIDMKRVAKATGGL 331
Cdd:cd00309 230 -------------------------------------YVVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGAT 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 332 VQTTIHGITDCCLGTCGVFEEMQLGSERYNIFTECPNTKTTTIILRGGAQQFIDEAERSLHDAIMIVRRSIKTNSIVVGG 411
Cdd:cd00309 273 IVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 412 GAIEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLRKEYAMNKGqgmKYGVDCINGGICD 491
Cdd:cd00309 353 GAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGG---NAGGDVETGEIVD 429
|
490 500 510
....*....|....*....|....*....|....*
gi 18250944 492 AYAACIWEPSLVKRNAIYSATEAACLVLSIDETIK 526
Cdd:cd00309 430 MKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
35-526 |
2.04e-179 |
|
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: 514.06 E-value: 2.04e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 35 VTNCIKTTLGPRGMDKLIHAEN-KVTITNDGATVLALLDIVHPAAAVLVDIAKSQDDEVGDGTTSVTVLAGEFLSKAKDF 113
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGgDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 114 IMEGMAPQTIIKYYREACKQALNIIDKIAINLSNKPYEETqklLLRCAETTLNSKLVSTYRSFFAKMVVDAVNILEDDM- 192
Cdd:pfam00118 81 LAAGVHPTTIIEGYEKALEKALEILDSIISIPVEDVDRED---LLKVARTSLSSKIISRESDFLAKLVVDAVLAIPKNDg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 193 --DKDMIGIKKVPGATCLDSMLIKGVAFKKTFSYagfEQQPKKFKNPKILLLNVELELKAEKDNAEIRINDPLIYQSIID 270
Cdd:pfam00118 158 sfDLGNIGVVKILGGSLEDSELVDGVVLDKGPLH---PDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 271 AEWKIIYDKLEAIYDIGANVVLSKLPIGDIATQFFAEKNIFCAGRVDEIDMKRVAKATGGLVQTTIHGITDCCLGTCGVF 350
Cdd:pfam00118 235 AEEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 351 EEMQLGSERYNIFTECPNTKTTTIILRGGAQQFIDEAERSLHDAIMIVRRSIKTNSIVVGGGAIEMEISRILREYSLSIM 430
Cdd:pfam00118 315 EEEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 431 GKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLRKEYamNKGQgMKYGVDCINGGICDAYAACIWEPSLVKRNAIYS 510
Cdd:pfam00118 395 GKEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAH--ASGE-KHAGIDVETGEIIDMKEAGVVDPLKVKRQALKS 471
|
490
....*....|....*.
gi 18250944 511 ATEAACLVLSIDETIK 526
Cdd:pfam00118 472 ATEAASTILRIDDIIK 487
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
8-525 |
4.05e-163 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 473.60 E-value: 4.05e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 8 PILVLKEDTDTSQGKSQIISNINACQAVTNCIKTTLGPRGMDK-LIHAENKVTITNDGATVLALLDIVHPAAAVLVDIAK 86
Cdd:NF041082 2 PILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKmLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 87 SQDDEVGDGTTSVTVLAGEFLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAINLSnkpyEETQKLLLRCAETTLN 166
Cdd:NF041082 82 TQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVD----PDDKETLKKIAATAMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 167 SKLVSTYRSFFAKMVVDAVNILEDD-----MDKDMIGIKKVPGATCLDSMLIKGVAFKKTFSYAGFeqqPKKFKNPKILL 241
Cdd:NF041082 158 GKGAEAAKDKLADLVVDAVKAVAEKdggynVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPGM---PKRVENAKIAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 242 LNVELELKAEKDNAEIRINDPLIYQSIIDAEWKIIYDKLEAIYDIGANVVLSKLPIGDIATQFFAEKNIFCAGRVDEIDM 321
Cdd:NF041082 235 LDAPLEVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 322 KRVAKATGGLVQTTIHGITDCCLGTCGVFEEMQLGSERYNIFTECPNTKTTTIILRGGAQQFIDEAERSLHDAIMIVRRS 401
Cdd:NF041082 315 EKLAKATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 402 IKTNSIVVGGGAIEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLRKEYAmnKGQGmKYG 481
Cdd:NF041082 395 LEDGKVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHE--KGNK-TAG 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 18250944 482 VDCINGGICDAYAACIWEPSLVKRNAIYSATEAACLVLSIDETI 525
Cdd:NF041082 472 LDVYTGKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVI 515
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
8-525 |
3.97e-162 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 470.97 E-value: 3.97e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 8 PILVLKEDTDTSQGKSQIISNINACQAVTNCIKTTLGPRGMDK-LIHAENKVTITNDGATVLALLDIVHPAAAVLVDIAK 86
Cdd:NF041083 2 PVLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKmLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 87 SQDDEVGDGTTSVTVLAGEFLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAINLSnkpyEETQKLLLRCAETTLN 166
Cdd:NF041083 82 TQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVD----PDDRETLKKIAETSLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 167 SKLVSTYRSFFAKMVVDAVN-ILEDD-----MDKDMIGIKKVPGATCLDSMLIKGVAFKKTFSYAGFeqqPKKFKNPKIL 240
Cdd:NF041083 158 SKGVEEARDYLAEIAVKAVKqVAEKRdgkyyVDLDNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGM---PKRVENAKIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 241 LLNVELELKAEKDNAEIRINDPLIYQSIIDAEWKIIYDKLEAIYDIGANVVLSKLPIGDIATQFFAEKNIFCAGRVDEID 320
Cdd:NF041083 235 LLDAPLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 321 MKRVAKATGGLVQTTIHGITDCCLGTCGVFEEMQLGSERYNIFTECPNTKTTTIILRGGAQQFIDEAERSLHDAIMIVRR 400
Cdd:NF041083 315 MEKLAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVAD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 401 SIKTNSIVVGGGAIEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLRKEYAMNKGQgmkY 480
Cdd:NF041083 395 AVEDGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAHEKGKKW---A 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 18250944 481 GVDCINGGICDAYAACIWEPSLVKRNAIYSATEAACLVLSIDETI 525
Cdd:NF041083 472 GINVFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVI 516
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
9-526 |
2.77e-158 |
|
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: 461.35 E-value: 2.77e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 9 ILVLKEDTDTSQGKSQIISNINACQAVTNCIKTTLGPRGMDK-LIHAENKVTITNDGATVLALLDIVHPAAAVLVDIAKS 87
Cdd:cd03343 1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKmLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 88 QDDEVGDGTTSVTVLAGEFLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAINLSnkpyEETQKLLLRCAETTLNS 167
Cdd:cd03343 81 QDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVD----PDDKDTLRKIAKTSLTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 168 KLVSTYRSFFAKMVVDAVNILEDD------MDKDMIGIKKVPGATCLDSMLIKGVAFKKTFSYagfEQQPKKFKNPKILL 241
Cdd:cd03343 157 KGAEAAKDKLADLVVDAVLQVAEKrdgkyvVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVH---PGMPKRVENAKIAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 242 LNVELELKAEKDNAEIRINDPLIYQSIIDAEWKIIYDKLEAIYDIGANVVLSKLPIGDIATQFFAEKNIFCAGRVDEIDM 321
Cdd:cd03343 234 LDAPLEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 322 KRVAKATGGLVQTTIHGITDCCLGTCGVFEEMQLGSERYNIFTECPNTKTTTIILRGGAQQFIDEAERSLHDAIMIVRRS 401
Cdd:cd03343 314 EKLARATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 402 IKTNSIVVGGGAIEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLRKEYAmnkgQGMK-Y 480
Cdd:cd03343 394 LEDGKVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHE----KGNKnA 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 18250944 481 GVDCINGGICDAYAACIWEPSLVKRNAIYSATEAACLVLSIDETIK 526
Cdd:cd03343 470 GLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIA 515
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
8-525 |
6.80e-156 |
|
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: 455.30 E-value: 6.80e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 8 PILVLKEDTDTSQGKSQIISNINACQAVTNCIKTTLGPRGMDK-LIHAENKVTITNDGATVLALLDIVHPAAAVLVDIAK 86
Cdd:TIGR02339 1 PVFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKmLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 87 SQDDEVGDGTTSVTVLAGEFLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAINLSnkpyEETQKLLLRCAETTLN 166
Cdd:TIGR02339 81 TQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKIS----PEDRDLLKKIAYTSLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 167 SKLVST-YRSFFAKMVVDAVNILED-------DMDKDMIGIKKVPGATCLDSMLIKGVAFKKTFSYAGFeqqPKKFKNPK 238
Cdd:TIGR02339 157 SKASAEvAKDKLADLVVEAVKQVAElrgdgkyYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPGM---PKRVENAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 239 ILLLNVELELKAEKDNAEIRINDPLIYQSIIDAEWKIIYDKLEAIYDIGANVVLSKLPIGDIATQFFAEKNIFCAGRVDE 318
Cdd:TIGR02339 234 IALLDAPLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 319 IDMKRVAKATGGLVQTTIHGITDCCLGTCGVFEEMQLGSERYNIFTECPNTKTTTIILRGGAQQFIDEAERSLHDAIMIV 398
Cdd:TIGR02339 314 SDIEKLARATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 399 RRSIKTNSIVVGGGAIEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLRKEYAmnKGQgM 478
Cdd:TIGR02339 394 ANALEDGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHE--KGN-K 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 18250944 479 KYGVDCINGGICDAYAACIWEPSLVKRNAIYSATEAACLVLSIDETI 525
Cdd:TIGR02339 471 NAGINVFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVI 517
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
28-526 |
6.50e-131 |
|
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: 391.65 E-value: 6.50e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 28 NINACQAVTNCIKTTLGPRGMDK-LIHAENKVTITNDGATVLALLDIVHPAAAVLVDIAKSQDDEVGDGTTSVTVLAGEF 106
Cdd:cd03335 13 NVTAAMAIANIVKSSLGPVGLDKmLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 107 LSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKiaiNLSNKPYEETQKLLLRCAETTLNSKLVSTYRSFFAKMVVDAVN 186
Cdd:cd03335 93 LKRANELVKQKIHPTTIISGYRLACKEAVKYIKE---HLSISVDNLGKESLINVAKTSMSSKIIGADSDFFANMVVDAIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 187 ILE--DDMDKDM-----IGIKKVPGATCLDSMLIKGVAFKKTfsyAGFEQQPKKFKNPKILLLNVELELKAEKDNAEIRI 259
Cdd:cd03335 170 AVKttNEKGKTKypikaVNILKAHGKSAKESYLVNGYALNCT---RASQGMPTRVKNAKIACLDFNLQKTKMKLGVQVVV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 260 NDPLIYQSIIDAEWKIIYDKLEAIYDIGANVVLSKLPIGDIATQFFAEKNIFCAGRVDEIDMKRVAKATGGLVQTTIHGI 339
Cdd:cd03335 247 TDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVSTLANL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 340 ------TDCCLGTCGVFEEMQLGSERYNIFTECPNTKTTTIILRGGAQQFIDEAERSLHDAIMIVRRSIKTNSIVVGGGA 413
Cdd:cd03335 327 egeetfDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGGA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 414 IEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLR----KEYAMNKGQGMK-YGVDCINGG 488
Cdd:cd03335 407 VETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRayhaAAQVKPDKKHLKwYGLDLINGK 486
|
490 500 510
....*....|....*....|....*....|....*...
gi 18250944 489 ICDAYAACIWEPSLVKRNAIYSATEAACLVLSIDETIK 526
Cdd:cd03335 487 VRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
17-532 |
3.81e-130 |
|
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: 389.85 E-value: 3.81e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 17 DTSQGKSQIISNINACQAVTNCIKTTLGPRGMDK-LIHAENKVTITNDGATVLALLDIVHPAAAVLVDIAKSQDDEVGDG 95
Cdd:TIGR02340 6 ERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKmLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 96 TTSVTVLAGEFLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKiaiNLSNKPYEETQKLLLRCAETTLNSKLVSTYRS 175
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKE---NLSVSVDELGREALINVAKTSMSSKIIGLDSD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 176 FFAKMVVDAVNILE--DDMDKDM-----IGIKKVPGATCLDSMLIKGVAFKKTfsyAGFEQQPKKFKNPKILLLNVELEL 248
Cdd:TIGR02340 163 FFSNIVVDAVLAVKttNENGETKypikaINILKAHGKSARESMLVKGYALNCT---VASQQMPKRIKNAKIACLDFNLQK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 249 KAEKDNAEIRINDPLIYQSIIDAEWKIIYDKLEAIYDIGANVVLSKLPIGDIATQFFAEKNIFCAGRVDEIDMKRVAKAT 328
Cdd:TIGR02340 240 AKMALGVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKAT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 329 GGLVQTTI------HGITDCCLGTCGVFEEMQLGSERYNIFTECPNTKTTTIILRGGAQQFIDEAERSLHDAIMIVRRSI 402
Cdd:TIGR02340 320 GATLVSTLadlegeETFEASYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 403 KTNSIVVGGGAIEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLR----KEYAMNKGQGM 478
Cdd:TIGR02340 400 ESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRayhaAAQLKPEKKHL 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 18250944 479 K-YGVDCINGGICDAYAACIWEPSLVKRNAIYSATEAACLVLSIDETIK--QQNSQD 532
Cdd:TIGR02340 480 KwYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIKlnPEQSKG 536
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
11-526 |
1.49e-121 |
|
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: 367.42 E-value: 1.49e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 11 VLKEDTDTSQGKSQIISNINACQAVTNCIKTTLGPRGMDKL---IHAENKVTITNDGATVLALLDIVHPAAAVLVDIAKS 87
Cdd:cd03336 1 ILKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKIlqsVGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 88 QDDEVGDGTTSVTVLAGEFLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAINLSNKPyEETQKLLLRCAETTLNS 167
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDE-EAFREDLLNIARTTLSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 168 KLVSTYRSFFAKMVVDAVNILEDDMDKDMIGIKKVPGATCLDSMLIKGVAFKKTFSYAgfeqQPKKFKNPKILLLNVELE 247
Cdd:cd03336 160 KILTQDKEHFAELAVDAVLRLKGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVN----QPKRIENAKILIANTPMD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 248 L-KAEKDNAEIRINDPLIYQSIIDAEWKIIYDKLEAIYDIGANVVLSKLPIGDIATQFFAEKNIFCAGRVDEIDMKRVAK 326
Cdd:cd03336 236 TdKIKIFGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHADFDGVERLAL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 327 ATGGLVQTTIHGITDCCLGTCGVFEEMQLGSERYNIFTECPNTKTTTIILRGGAQQFIDEAERSLHDAIMIVRRSIKTNS 406
Cdd:cd03336 316 VTGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDTR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 407 IVVGGGAIEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLRKEYAMNKgqgMKYGVDCIN 486
Cdd:cd03336 396 VVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGN---TTAGLDMRK 472
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 18250944 487 GGICDAYAACIWEPSLVKRNAIYSATEAACLVLSIDETIK 526
Cdd:cd03336 473 GTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIK 512
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
5-526 |
8.39e-119 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 360.88 E-value: 8.39e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 5 MNLPILVLKEDTDTSQGKSQIISNINACQAVTNCIKTTLGPRGMDKLIHA------ENKVTITNDGATVLALLDIVHPAA 78
Cdd:PTZ00212 4 ANVPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQPmsegprSGNVTVTNDGATILKSVWLDNPAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 79 AVLVDIAKSQDDEVGDGTTSVTVLAGEFLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAINLSNKPyEETQKLLL 158
Cdd:PTZ00212 84 KILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDE-EKFKEDLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 159 RCAETTLNSKLVSTYRSFFAKMVVDAVNILEDDMDKDMIGIKKVPGATCLDSMLIKGVAFKKTFSYAgfeqQPKKFKNPK 238
Cdd:PTZ00212 163 NIARTTLSSKLLTVEKDHFAKLAVDAVLRLKGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVG----QPKRLENCK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 239 ILLLNVELEL-KAEKDNAEIRINDPLIYQSIIDAEWKIIYDKLEAIYDIGANVVLSKLPIGDIATQFFAEKNIFCAGRVD 317
Cdd:PTZ00212 239 ILVANTPMDTdKIKIYGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMAIEHAD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 318 EIDMKRVAKATGGLVQTTIHGITDCCLGTCGVFEEMQLGSERYNIFTECPNTKTTTIILRGGAQQFIDEAERSLHDAIMI 397
Cdd:PTZ00212 319 FDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 398 VRRSIKTNSIVVGGGAIEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLRKEYAMNKgqg 477
Cdd:PTZ00212 399 LSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHYKGN--- 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 18250944 478 MKYGVDCINGGICDAYAACIWEPSLVKRNAIYSATEAACLVLSIDETIK 526
Cdd:PTZ00212 476 KTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIR 524
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
8-525 |
2.90e-115 |
|
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: 349.67 E-value: 2.90e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 8 PILVLKEDTDTSQGKSQIISNINACQAVTNCIKTTLGPRGMDK-LIHAENKVTITNDGATVLALLDIVHPAAAVLVDIAK 86
Cdd:cd03337 1 PVLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKmLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 87 SQDDEVGDGTTSVTVLAGEFLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAINLSnkpyEETQKLLLRCAETTLN 166
Cdd:cd03337 81 TQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVD----VNDRAQMLKIIKSCIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 167 SKLVSTYRSFFAKMVVDAVNI--LEDDMDKDMIGIK------KVPGATCLDSMLIKGVAFKKTFSYAGFEqqpKKFKNPK 238
Cdd:cd03337 157 TKFVSRWSDLMCNLALDAVKTvaVEENGRKKEIDIKryakveKIPGGEIEDSRVLDGVMLNKDVTHPKMR---RRIENPR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 239 ILLLNVELElkaekdnaeirindpliYqsiidaewkiiydkleaiydiganVVLSKLPIGDIATQFFAEKNIFCAGRVDE 318
Cdd:cd03337 234 IVLLDCPLE-----------------Y------------------------LVITEKGVSDLAQHYLVKAGITALRRVRK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 319 IDMKRVAKATGGLVQTTIHGITDCCLGT-CGVFEEMQLGSERYNIFTECPNTKTTTIILRGGAQQFIDEAERSLHDAIMI 397
Cdd:cd03337 273 TDNNRIARACGATIVNRPEELTESDVGTgAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 398 VRRSIKTNSIVVGGGAIEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLRKEYAMNKGQg 477
Cdd:cd03337 353 ARNIILNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENS- 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 18250944 478 mKYGVDCINGGICDAYAACIWEPSLVKRNAIYSATEAACLVLSIDETI 525
Cdd:cd03337 432 -TWGIDGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
8-525 |
3.28e-112 |
|
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: 343.64 E-value: 3.28e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 8 PILVLKEDTDTSQGKSQIISNINACQAVTNCIKTTLGPRGMDK-LIHAENKVTITNDGATVLALLDIVHPAAAVLVDIAK 86
Cdd:TIGR02344 1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKmLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 87 SQDDEVGDGTTSVTVLAGEFLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAINLSNKPYEETQKLLLRCaettLN 166
Cdd:TIGR02344 81 TQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSC----IG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 167 SKLVSTYRSFFAKMVVDAV-NILEDDMDKDMIGIK------KVPGATCLDSMLIKGVAFKKTFSYagfeqqPK---KFKN 236
Cdd:TIGR02344 157 TKFVSRWSDLMCDLALDAVrTVQRDENGRKEIDIKryakveKIPGGDIEDSCVLKGVMINKDVTH------PKmrrYIEN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 237 PKILLLNVELELKAEKDNAEIRINDPLIYQSIIDAEWKIIYDKLEAIYDIGANVVLSKLPIGDIATQFFAEKNIFCAGRV 316
Cdd:TIGR02344 231 PRIVLLDCPLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 317 DEIDMKRVAKATGGLVQTTIHGITDCCLGT-CGVFEEMQLGSERYNIFTECPNTKTTTIILRGGAQQFIDEAERSLHDAI 395
Cdd:TIGR02344 311 RKTDNNRIARACGATIVNRPEELRESDVGTgCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 396 MIVRRSIKTNSIVVGGGAIEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLRKEYAmnKG 475
Cdd:TIGR02344 391 AVARNVLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHA--QE 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 18250944 476 QGMKYGVDCINGGICDAYAACIWEPSLVKRNAIYSATEAACLVLSIDETI 525
Cdd:TIGR02344 469 NNCTWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
27-525 |
4.85e-112 |
|
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: 342.73 E-value: 4.85e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 27 SNINACQAVTNCIKTTLGPRGMDKLIHAENK-VTITNDGATVLALLDIVHPAAAVLVDIAKSQDDEVGDGTTSVTVLAGE 105
Cdd:cd03338 12 SNIQAAKAVADAIRTSLGPRGMDKMIQTGKGeVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 106 FLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIA--INLSNKpyeetqKLLLRCAETTLNSKLVSTYRSFFAKMVVD 183
Cdd:cd03338 92 LLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSipVDLNDR------ESLIKSATTSLNSKVVSQYSSLLAPIAVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 184 AVNILED-----DMDKDMIGIKKVPGATCLDSMLIKGVAFKKTFSYAGfeQQPKKFKNPKILLLNVELE-LKAEKDNaEI 257
Cdd:cd03338 166 AVLKVIDpatatNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKA--GGPTRIEKAKIGLIQFCLSpPKTDMDN-NI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 258 RINDPLIYQSIIDAEWKIIYDKLEAIYDIGANVVL---SKL--PIGDIATQFFAEKNIFCAGRVDEIDMKRVAKATGGLV 332
Cdd:cd03338 243 VVNDYAQMDRILREERKYILNMCKKIKKSGCNVLLiqkSILrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 333 QTTIHGITDCCLGTCGVFEEMQLGSERYNIFTECPNT-KTTTIILRGGAQQFIDEAERSLHDAIMIVRRSIKTNSIVVGG 411
Cdd:cd03338 323 VASIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 412 GAIEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLRKEYAmnkgQGMK-YGVDCINGGIC 490
Cdd:cd03338 403 GAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHA----QGEKnAGINVRKGAIT 478
|
490 500 510
....*....|....*....|....*....|....*
gi 18250944 491 DAYAACIWEPSLVKRNAIYSATEAACLVLSIDETI 525
Cdd:cd03338 479 NILEENVVQPLLVSTSAITLATETVRMILKIDDIV 513
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
8-526 |
1.18e-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: 339.66 E-value: 1.18e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 8 PILVLKEDTDTS--QGKSQIISNINACQAVTNCIKTTLGPRGMDK-LIHAENKVTITNDGATVLALLDIVHPAAAVLVDI 84
Cdd:cd03339 6 PFIIVREQEKKKrlKGLEAHKSHILAAKSVANILRTSLGPRGMDKiLVSPDGEVTVTNDGATILEKMDVDHQIAKLLVEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 85 AKSQDDEVGDGTTSVTVLAGEFLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAINLSNKPyeETQKLLLRCAETT 164
Cdd:cd03339 86 SKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSP--DNKEPLIQTAMTS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 165 LNSKLVSTYRSFFAKMVVDAVNILED----DMDKDMIGIKKVPGATCLDSMLIKGVAFKKTFSYAgfeQQPKKFKNPKIL 240
Cdd:cd03339 164 LGSKIVSRCHRQFAEIAVDAVLSVADlerkDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHP---QMPKEVKDAKIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 241 LLNVELELKAEKDNAEIRINDPLIYQSIIDAEWKIIYDKLEAIYDIGANVVLSKLPIGDIATQFFAEKNIFCAGRVDEID 320
Cdd:cd03339 241 ILTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 321 MKRVAKATGGLVQTTIHGITDCCLGTCGVFEEMQLGS--ERYNIFTECPNTKTTTIILRGGAQQFIDEAERSLHDAIMIV 398
Cdd:cd03339 321 IELIAIATGGRIVPRFEDLSPEKLGKAGLVREISFGTtkDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 399 RRSIKTNSIVVGGGAIEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLRKEyaMNKGQGM 478
Cdd:cd03339 401 RNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKAR--QVKEKNP 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 18250944 479 KYGVDCINGGICDAYAACIWEPSLVKRNAIYSATEAACLVLSIDETIK 526
Cdd:cd03339 479 HLGIDCLGRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
27-523 |
1.89e-103 |
|
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: 320.58 E-value: 1.89e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 27 SNINACQAVTNCIKTTLGPRGMDKLIHAEN-KVTITNDGATVLALLDIVHPAAAVLVDIAKSQDDEVGDGTTSVTVLAGE 105
Cdd:TIGR02342 13 SNIVAAKAVADAIRTSLGPKGMDKMIQDGKgEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 106 FLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAINLSNKPYEetqkLLLRCAETTLNSKLVSTYRSFFAKMVVDAV 185
Cdd:TIGR02342 93 LLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDRE----QLLKSATTSLSSKVVSQYSSLLAPLAVDAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 186 NILED-----DMDKDMIGIKKVPGATCLDSMLIKGVAFKKTFSYAgfEQQPKKFKNPKILLLNVELEL-KAEKDNaEIRI 259
Cdd:TIGR02342 169 LKVIDpenakNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKS--AGGPTRIEKAKIGLIQFQISPpKTDMEN-QIIV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 260 NDPLIYQSIIDAEWKIIYDKLEAIYDIGANVVLSKLPI-----GDIATQFFAEKNIFCAGRVDEIDMKRVAKATGGLVQT 334
Cdd:TIGR02342 246 NDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 335 TIHGITDCCLGTCGVFEEMQLGSERYNIFTECPNT-KTTTIILRGGAQQFIDEAERSLHDAIMIVRRSIKTNSIVVGGGA 413
Cdd:TIGR02342 326 SIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 414 IEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLRKEYAMNKgqgMKYGVDCINGGICDAY 493
Cdd:TIGR02342 406 PEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGE---KTAGISVRKGGITNML 482
|
490 500 510
....*....|....*....|....*....|
gi 18250944 494 AACIWEPSLVKRNAIYSATEAACLVLSIDE 523
Cdd:TIGR02342 483 EEHVLQPLLVTTSAITLASETVRSILKIDD 512
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
8-526 |
1.83e-100 |
|
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: 313.28 E-value: 1.83e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 8 PILVLKEDTDTSQ--GKSQIISNINACQAVTNCIKTTLGPRGMDK-LIHAENKVTITNDGATVLALLDIVHPAAAVLVDI 84
Cdd:TIGR02343 10 PFIIIKDQDNKKRlkGLEAKKSNIAAAKSVASILRTSLGPKGMDKmLISPDGDITVTNDGATILSQMDVDNQIAKLMVEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 85 AKSQDDEVGDGTTSVTVLAGEFLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIA--INLSNKPYEEtqklLLRCAE 162
Cdd:TIGR02343 90 SKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISdeISADNNNREP----LIQAAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 163 TTLNSKLVSTYRSFFAKMVVDAVNILED----DMDKDMIGIKKVPGATCLDSMLIKGVAFKKTFSYAgfeQQPKKFKNPK 238
Cdd:TIGR02343 166 TSLGSKIVSKCHRRFAEIAVDAVLNVADmerrDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHP---QMPKEVEDAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 239 ILLLNVELELKAEKDNAEIRINDPLIYQSIIDAEWKIIYDKLEAIYDIGANVVLSKLPIGDIATQFFAEKNIFCAGRVDE 318
Cdd:TIGR02343 243 IAILTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 319 IDMKRVAKATGGLVQTTIHGITDCCLGTCGVFEEMQLGS--ERYNIFTECPNTKTTTIILRGGAQQFIDEAERSLHDAIM 396
Cdd:TIGR02343 323 QELELIAIATGGRIVPRFQELSKDKLGKAGLVREISFGTtkDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALC 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 397 IVRRSIKTNSIVVGGGAIEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLRKEyaMNKGQ 476
Cdd:TIGR02343 403 VVRNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSL--QLKEK 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 18250944 477 GMKYGVDCINGGICDAYAACIWEPSLVKRNAIYSATEAACLVLSIDETIK 526
Cdd:TIGR02343 481 NPNLGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVIS 530
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
25-525 |
8.48e-97 |
|
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: 301.83 E-value: 8.48e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 25 IISNINACQAVTNCIKTTLGPRGMDKLI--HaENKVTITNDGATVLALLDIVHPAAAVLVDIAKSQDDEVGDGTTSVTVL 102
Cdd:cd03341 10 VLRNIEACKELSQITRTSYGPNGMNKMVinH-LEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 103 AGEFLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAI-NLSNKPYEETQKLLLRcaeTTLNSKlVSTYRSFFAKMV 181
Cdd:cd03341 89 AGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVyKIEDLRNKEEVSKALK---TAIASK-QYGNEDFLSPLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 182 VDA-VNILEDDMDK---DMIGIKKVPGATCLDSMLIKGVAFKKtfsyaGFEQQPKKFKNPKILLLNVELelkaekdnaei 257
Cdd:cd03341 165 AEAcISVLPENIGNfnvDNIRVVKILGGSLEDSKVVRGMVFKR-----EPEGSVKRVKKAKVAVFSCPF----------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 258 rindpliyqsiidaewkiiydkleaiyDIGANVVLSKLPIGDIAtQFFAEKNIFCAGRV-DEIDMKRVAKATGGLVQTTI 336
Cdd:cd03341 229 ---------------------------DIGVNVIVAGGSVGDLA-LHYCNKYGIMVIKInSKFELRRLCRTVGATPLPRL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 337 HGITDCCLGTCGVFEEMQLGSERYNIFTECPN-TKTTTIILRGGAQQFIDEAERSLHDAIMIVRRSIKTNSIVVGGGAIE 415
Cdd:cd03341 281 GAPTPEEIGYCDSVYVEEIGDTKVVVFRQNKEdSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 416 MEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLrkeYAMNKGQGMKYGVD--CINGGICDAY 493
Cdd:cd03341 361 IELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSEL---YAAHQKGNKSAGVDieSGDEGTKDAK 437
|
490 500 510
....*....|....*....|....*....|..
gi 18250944 494 AACIWEPSLVKRNAIYSATEAACLVLSIDETI 525
Cdd:cd03341 438 EAGIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
11-526 |
9.41e-96 |
|
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: 301.01 E-value: 9.41e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 11 VLKEDTDTSQGKSQIISNINACQAVTNCIKTTLGPRGMDKLIHA---ENKVTITNDGATVLALLDIVHPAAAVLVDIAKS 87
Cdd:TIGR02341 2 IFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSsssDASIMVTNDGATILKSIGVDNPAAKVLVDMSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 88 QDDEVGDGTTSVTVLAGEFLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAINLSNKPYEETQKLLlRCAETTLNS 167
Cdd:TIGR02341 82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEVKFRQDLM-NIARTTLSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 168 KLVSTYRSFFAKMVVDAVNILEDDMDKDMIGIKKVPGATCLDSMLIKGVAFKKTFSYagfeQQPKKFKNPKILLLNVELE 247
Cdd:TIGR02341 161 KILSQHKDHFAQLAVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKIGV----NQPKRIENAKILIANTGMD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 248 L-KAEKDNAEIRINDPLIYQSIIDAEWKIIYDKLEAIYDIGANVVLSKLPIGDIATQFFAEKNIFCAGRVDEIDMKRVAK 326
Cdd:TIGR02341 237 TdKVKIFGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVERLAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 327 ATGGLVQTTIHGITDCCLGTCGVFEEMQLGSERYNIFTECPNTKTTTIILRGGAQQFIDEAERSLHDAIMIVRRSIKTNS 406
Cdd:TIGR02341 317 VTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKESR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 407 IVVGGGAIEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLRKEYAMNKGQGmkyGVDCIN 486
Cdd:TIGR02341 397 TVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHYNGNTTM---GLDMNE 473
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 18250944 487 GGICDAYAACIWEPSLVKRNAIYSATEAACLVLSIDETIK 526
Cdd:TIGR02341 474 GTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIK 513
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
27-525 |
1.33e-92 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 291.98 E-value: 1.33e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 27 SNINACQAVTNCIKTTLGPRGMDKLIhaENK---VTITNDGATVLALLDIVHP----AAAVLVDIAKSQDDEVGDGTTSV 99
Cdd:COG0459 14 ANIRGVKALADAVKVTLGPKGRNVML--VKSfgdPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTTTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 100 TVLAGEFLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAINLSNKpyeetqKLLLRCAETTLNSKlvstyrSFFAK 179
Cdd:COG0459 92 TVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDK------EELAQVATISANGD------EEIGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 180 MVVDAVNILEDDmdkdmiGIKKV--PGATCLDSMLIKGVAFKKTFSYAGF----EQQPKKFKNPKILLLNVELELKAEkd 253
Cdd:COG0459 160 LIAEAMEKVGKD------GVITVeeGKGLETELEVVEGMQFDKGYLSPYFvtdpEKMPAELENAYILLTDKKISSIQD-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 254 naeirindpliyqsiidaewkiIYDKLEAIYDIGANVVLSKLPIGDIATQFFAEKNIFCAGRVDEI-----------DMK 322
Cdd:COG0459 232 ----------------------LLPLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVkapgfgdrrkaMLE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 323 RVAKATGGLVQTTIHGIT-------DccLGTCGVFEEmqlGSERYNIFTECPNTKTTTIILRGGAQQFIDEAERSLHDAI 395
Cdd:COG0459 290 DIAILTGGRVISEDLGLKledvtldD--LGRAKRVEV---DKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDAL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 396 MIVRRSIKtNSIVVGGGAIEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLRKEyamnKG 475
Cdd:COG0459 365 HATRAAVE-EGIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA----KD 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 18250944 476 QGmkYGVDCINGGICDAYAACIWEPSLVKRNAIYSATEAACLVLSIDETI 525
Cdd:COG0459 440 KG--FGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVI 487
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
11-525 |
2.29e-88 |
|
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: 281.99 E-value: 2.29e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 11 VLKEDTDTSQG-KSQIISNINACQAVTNCIKTTLGPRGMDKLI--HAEnKVTITNDGATVLALLDIVHPAAAVLVDIAKS 87
Cdd:TIGR02346 5 LLKEGYRHFSGlEEAVIKNIEACKELSQITRTSLGPNGMNKMVinHLE-KLFVTNDAATILRELEVQHPAAKLLVMASEM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 88 QDDEVGDGTTSVTVLAGEFLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAINLSNKPYEETQklLLRCAETTLNS 167
Cdd:TIGR02346 84 QENEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEVKDLRDKDE--LIKALKASISS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 168 KLVSTYrSFFAKMVVDAVNIL----EDDMDKDMIGIKKVPGATCLDSMLIKGVAFKKTFsyagfEQQPKKFKNPKILLLN 243
Cdd:TIGR02346 162 KQYGNE-DFLAQLVAQACSTVlpknPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNREA-----EGSVKSVKNAKVAVFS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 244 VELELKAEKDNAEIRINDPliyQSIID---AEWKIIYDKLEAIYDIGANVVLSKLPIGDIATQFFAEKNIFCAGRVDEID 320
Cdd:TIGR02346 236 CPLDTATTETKGTVLIHNA---EELLNyskGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 321 MKRVAKATGGLVQTTIHGITDCCLGTCGVFEEMQLGSERYNIF-TECPNTKTTTIILRGGAQQFIDEAERSLHDAIMIVR 399
Cdd:TIGR02346 313 LRRLCKTVGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFkQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 400 RSIKTNSIVVGGGAIEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLrkeYAMNKGQGMK 479
Cdd:TIGR02346 393 ALVKDGRLLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKL---YAAHKKGNKS 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 18250944 480 YGVDcINGGIC---DAYAACIWEPSLVKRNAIYSATEAACLVLSIDETI 525
Cdd:TIGR02346 470 KGID-IEAESDgvkDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQII 517
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
28-526 |
8.78e-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: 8.78e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 28 NINACQAVTNCIKTTLGPRGMDK-LIHAENKVTITNDGATVLALLDIVHPAAAVLVDIAKSQDDEVGDGTTSVTVLAGEF 106
Cdd:TIGR02347 21 NINAARGLQDVLKTNLGPKGTLKmLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 107 LSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAINlsnKPYEETQKLLLRCAETTLNSKLVSTYRSFFAKMVVDAVN 186
Cdd:TIGR02347 101 LKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVK---KEDEVDREFLLNVARTSLRTKLPADLADQLTEIVVDAVL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 187 ILEDD---MDKDMIGIKKVPGATCLDSMLIKGVAFKKTFSYAGFeqqPKKFKNPKILLLNVELELKAEKDNAEIRINDPL 263
Cdd:TIGR02347 178 AIKKDgedIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPDM---PRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 264 IYQSIIDAEWKIIYDKLEAIYDIGANV----------VLSKLPIGDIATQFFAEKNIFCAGRVDEIDMKRVAKATGGLVQ 333
Cdd:TIGR02347 255 QREKLVKAERKFVDDRVKKIIELKKKVcgkspdkgfvVINQKGIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEAL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 334 TTIHGITDCCLGTCGVFEEMQLGSERYNIFTECPNTKTTTIILRGGAQQFIDEAERSLHDAIMIVRRSIKTNSIVVGGGA 413
Cdd:TIGR02347 335 NSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAGA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 414 IEMEISRILREYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLRKEYamNKGQGMKyGVDCINGGICDAY 493
Cdd:TIGR02347 415 FEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEH--DEGGEVV-GVDLNTGEPIDPE 491
|
490 500 510
....*....|....*....|....*....|...
gi 18250944 494 AACIWEPSLVKRNAIYSATEAACLVLSIDETIK 526
Cdd:TIGR02347 492 IKGIWDNYRVKKQLIQSATVIASQLLLVDEVMR 524
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
28-526 |
8.56e-76 |
|
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: 247.56 E-value: 8.56e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 28 NINACQAVTNCIKTTLGPRGMDK-LIHAENKVTITNDGATVLALLDIVHPAAAVLVDIAKSQDDEVGDGTTSVTVLAGEF 106
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKmLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 107 LSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAINLSNKPYEETqklLLRCAETTLNSKLVSTYRSFFAKMVVDAVN 186
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDTDREL---LLSVARTSLRTKLHADLADQLTEIVVDAVL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 187 ILEDD---MDKDMIGIKKVPGATCLDSMLIKGVAFKKTFSYAGFeqqPKKFKNPKILLLNVELEL-KAEkdnaeirINDP 262
Cdd:cd03342 174 AIYKPdepIDLHMVEIMQMQHKSDSDTKLIRGLVLDHGARHPDM---PKRVENAYILTCNVSLEYeKTE-------VNSG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 263 LIYqsiidaewkiiydkleaiydigaNVVLSKLPIGDIATQFFAEKNIFCAGRVDEIDMKRVAKATGGLVQTTIHGITDC 342
Cdd:cd03342 244 FFY-----------------------SVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSPE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 343 CLGTCGVFEEMQLGSERYNIFTECPNTKTTTIILRGGAQQFIDEAERSLHDAIMIVRRSIKTNSIVVGGGAIEMEISRIL 422
Cdd:cd03342 301 CLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAHL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 423 REYSLSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKLRKEYAMNkgqGMKYGVDCINGGICDAYAACIWEPSL 502
Cdd:cd03342 381 KEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEG---GQVGGVDLDTGEPMDPESEGIWDNYS 457
|
490 500
....*....|....*....|....
gi 18250944 503 VKRNAIYSATEAACLVLSIDETIK 526
Cdd:cd03342 458 VKRQILHSATVIASQLLLVDEIIR 481
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
155-403 |
1.35e-65 |
|
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: 211.94 E-value: 1.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 155 KLLLRCAETTLNSKlVSTYRSFFAKMVVDAVNILEDDM---DKDMIGIKKVPGATCLDSMLIKGVAFKKTFSYAGFeqqP 231
Cdd:cd03333 2 ELLLQVATTSLNSK-LSSWDDFLGKLVVDAVLKVGPDNrmdDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYM---P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 232 KKFKNPKILLLNVELElkaekdnaeirindpliyqsiidaewkiiydkleaiydigaNVVLSKLPIGDIATQFFAEKNIF 311
Cdd:cd03333 78 KRLENAKILLLDCPLE-----------------------------------------YVVIAEKGIDDLALHYLAKAGIM 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 312 CAGRVDEIDMKRVAKATGGLVQTTIHGITDCCLGTCGVFEEMQLGSERYNIFTECPNTKTTTIILRGGAQQFIDEAERSL 391
Cdd:cd03333 117 AVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRSL 196
|
250
....*....|..
gi 18250944 392 HDAIMIVRRSIK 403
Cdd:cd03333 197 HDALCAVRAAVE 208
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
190-379 |
1.53e-19 |
|
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: 88.43 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 190 DDMDK-DMIGIKKVPGATCLDSMLIKGVAFKKTfsyAGFEQQPKKFKNPKILLLNVELELKaekdnaeiRINDPLIY-QS 267
Cdd:cd03334 42 DDMDIrQYVKIKKIPGGSPSDSEVVDGVVFTKN---VAHKRMPSKIKNPRILLLQGPLEYQ--------RVENKLLSlDP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 268 IIDAE---WKIIYDKLEAiydIGANVVLSKLPIGDIATQFFAEKNIFCAgrvdeIDMK-----RVAKATGG-LVQTTIHG 338
Cdd:cd03334 111 VILQEkeyLKNLVSRIVA---LRPDVILVEKSVSRIAQDLLLEAGITLV-----LNVKpsvleRISRCTGAdIISSMDDL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 18250944 339 ITDCCLGTCGVFE-----EMQLGSERYNIFTECPNTKTTTIILRGG 379
Cdd:cd03334 183 LTSPKLGTCESFRvrtyvEEHGRSKTLMFFEGCPKELGCTILLRGG 228
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
32-519 |
4.79e-12 |
|
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). With the aid of cochaperonin GroES, GroEL encapsulates non-native substrate proteins inside the cavity of the GroEL-ES complex and promotes folding by using energy derived from ATP hydrolysis.
Pssm-ID: 239460 Cd Length: 520 Bit Score: 68.25 E-value: 4.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 32 CQAVTNCIKTTLGPRGMDKLIhaENKV---TITNDGATV---LALLDIVHPAAAVLV-DIAKSQDDEVGDGTTSVTVLAG 104
Cdd:cd03344 17 VNKLADAVKVTLGPKGRNVVI--EKSFgspKITKDGVTVakeIELEDPFENMGAQLVkEVASKTNDVAGDGTTTATVLAR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 105 EFLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAINLSNKpyEEtqklLLRCAETTLNSKlvstyrSFFAKMVVDA 184
Cdd:cd03344 95 AIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTK--EE----IAQVATISANGD------EEIGELIAEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 185 vnileddMDKdmIGIKKV----PGATCLDSM-LIKGVAFKKTFSYAGFEQQPKK----FKNPKILLlnVELELKAEKD-- 253
Cdd:cd03344 163 -------MEK--VGKDGVitveEGKTLETELeVVEGMQFDRGYLSPYFVTDPEKmeveLENPYILL--TDKKISSIQEll 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 254 ---NAEIRINDPLIyqsII------DAEWKIIYDKLEAiydiGANVVLSKLP---------IGDIAT----QFFAEKNIF 311
Cdd:cd03344 232 pilELVAKAGRPLL---IIaedvegEALATLVVNKLRG----GLKVCAVKAPgfgdrrkamLEDIAIltggTVISEELGL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 312 CAGRVDEIDMKRVAKATGGLVQTTIHG-------ITDCCLGTCGVFEEMQLGSERyniftecpnTKTTT----------I 374
Cdd:cd03344 305 KLEDVTLEDLGRAKKVVVTKDDTTIIGgagdkaaIKARIAQIRKQIEETTSDYDK---------EKLQErlaklsggvaV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 375 ILRGGAQqfidEAERS-----LHDAIMIVRRSIKtNSIVVGGGAIEMEISRILREYSLSIMGkQQLIIHAYAKALECIPQ 449
Cdd:cd03344 376 IKVGGAT----EVELKekkdrVEDALNATRAAVE-EGIVPGGGVALLRASPALDKLKALNGD-EKLGIEIVRRALEAPLR 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 450 TLARNSGFDATDVLNKLRKEYAmnkgqgmKYGVDCINGGICDAYAACIWEPSLVKRNAIYSATEAACLVL 519
Cdd:cd03344 450 QIAENAGVDGSVVVEKVLESPD-------GFGYDAATGEYVDMIEAGIIDPTKVVRSALQNAASVASLLL 512
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
29-148 |
6.42e-09 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 58.39 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 29 INACQAVTNCIKTTLGPRGMDKLIHAENKVT-ITNDGATV---LALLDIVHPAAAVLV-DIAKSQDDEVGDGTTSVTVLA 103
Cdd:PTZ00114 28 LKGIERLADAVAVTLGPKGRNVIIEQEYGSPkITKDGVTVakaIEFSDRFENVGAQLIrQVASKTNDKAGDGTTTATILA 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 18250944 104 GEFLSKAKDFIMEGMAPQTIIKYYREACKQALNIIDKIAINLSNK 148
Cdd:PTZ00114 108 RAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTK 152
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
42-532 |
1.13e-08 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 57.81 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 42 TLGPRGMDKLIhaENKV---TITNDGATV---LALLDIVHPAAAVLVDIAKSQDDEV-GDGTTSVTVLAGEFLSKAKDFI 114
Cdd:CHL00093 29 TLGPKGRNVVL--EKKYgspQIVNDGVTIakeIELEDHIENTGVALIRQAASKTNDVaGDGTTTATVLAYAIVKQGMKNV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 115 MEGMAPQTIIKYYREACKQALNIIDKIAinlsnKPYEETQKLLLRCAETTLNSKLVstyrsffAKMVVDAVnileDDMDK 194
Cdd:CHL00093 107 AAGANPISLKRGIEKATQYVVSQIAEYA-----RPVEDIQAITQVASISAGNDEEV-------GSMIADAI----EKVGR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 195 DMIgIKKVPGATCLDSMLIK-GVAFKKTFSYAGFEQQPKK----FKNPKILLLNVELELkAEKDNAEI-----RINDPLI 264
Cdd:CHL00093 171 EGV-ISLEEGKSTVTELEITeGMRFEKGFISPYFVTDTERmevvQENPYILLTDKKITL-VQQDLLPIleqvtKTKRPLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 265 yqsII------DAEWKIIYDKLEAIydigANVVLSKLP-IGDIATQFfaeknifcagrvdeidMKRVAKATGGLVQTTIH 337
Cdd:CHL00093 249 ---IIaedvekEALATLVLNKLRGI----VNVVAVRAPgFGDRRKAM----------------LEDIAILTGGQVITEDA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 338 GITdcclgtcgvFEEMQ---LGSERYNIFTEcpntKTTTIILRGGAQQF----------IDEAERS-------------- 390
Cdd:CHL00093 306 GLS---------LETIQldlLGQARRIIVTK----DSTTIIADGNEEQVkarceqlrkqIEIADSSyekeklqerlakls 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 391 ----------------------LHDAIMIVRRSIKtNSIVVGGGAIEMEISRILREYSLSIMGKQQLI-IHAYAKALECI 447
Cdd:CHL00093 373 ggvavikvgaatetemkdkklrLEDAINATKAAVE-EGIVPGGGATLVHLSENLKTWAKNNLKEDELIgALIVARAILAP 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 448 PQTLARNSGFDATDVLNKLrkeyamnKGQGMKYGVDCINGGICDAYAACIWEPSLVKRNAIYSATEAACLVLSIDETIKQ 527
Cdd:CHL00093 452 LKRIAENAGKNGSVIIEKV-------QEQDFEIGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVD 524
|
....*
gi 18250944 528 QNSQD 532
Cdd:CHL00093 525 KKESS 529
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
35-533 |
4.17e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 56.01 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 35 VTNCIKTTLGPRGMDKLIH-AENKVTITNDGATVLALLDIV----HPAAAVLVDIAKSQDDEVGDGTTSVTVLAGEFLSK 109
Cdd:PRK12852 23 LANAVKVTLGPKGRNVVIEkSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKTNDLAGDGTTTATVLAQAIVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 110 AKDFIMEGMAPQTIikyyreacKQALNiidkIAINLSNKPYEETQKLLLRCAETTLNSKLVSTYRSFFAKMVVDAVNILE 189
Cdd:PRK12852 103 GAKAVAAGMNPMDL--------KRGID----IAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGKMIAQAMQKVG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 190 DDmdkdmiGIKKVPGATCLDSML--IKGVAFKKTFSYAGF----EQQPKKFKNPKILLLNVELE-LKAEKD--NAEIRIN 260
Cdd:PRK12852 171 NE------GVITVEENKSLETEVdiVEGMKFDRGYLSPYFvtnaEKMTVELDDAYILLHEKKLSgLQAMLPvlEAVVQSG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 261 DPLIyqsII--DAEWK----IIYDKLEAiydiGANVVLSKLP-IGDIATQFFAEKNIFCAGRV---------DEIDMKRV 324
Cdd:PRK12852 245 KPLL---IIaeDVEGEalatLVVNRLRG----GLKVAAVKAPgFGDRRKAMLEDIAILTGGQLisedlgiklENVTLKML 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 325 AKATGGLVQTTIHGITDcclgtcGVFEEMQLGSERYNIFTECPNTKT-----------------TTIILRGGAQQF-IDE 386
Cdd:PRK12852 318 GRAKKVVIDKENTTIVN------GAGKKADIEARVGQIKAQIEETTSdydreklqerlaklaggVAVIRVGGATEVeVKE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 387 AERSLHDAIMIVRRSIKtNSIVVGGGAIEMEISRILREYSlSIMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKL 466
Cdd:PRK12852 392 KKDRVEDALNATRAAVQ-EGIVPGGGVALLRAKKAVGRIN-NDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKI 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18250944 467 RkeyamnKGQGMKYGVDCINGGICDAYAACIWEPSLVKRNAIYSATEAACLVLSIDETIKQQNSQDK 533
Cdd:PRK12852 470 L------ENKSETFGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDA 530
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
34-120 |
7.73e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 55.11 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 34 AVTNCIKTTLGPRG----MDKLIHAEnkvTITNDGATV---LALLDIVHPAAAVLV-DIAKSQDDEVGDGTTSVTVLAGE 105
Cdd:PRK12850 22 ILANAVKVTLGPKGrnvvLEKSFGAP---RITKDGVTVakeIELEDKFENMGAQMVkEVASKTNDLAGDGTTTATVLAQA 98
|
90
....*....|....*
gi 18250944 106 FLSKAKDFIMEGMAP 120
Cdd:PRK12850 99 IVREGAKLVAAGMNP 113
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
34-120 |
2.69e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 53.21 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 34 AVTNCIKTTLGPRGMDKLIhaENKV---TITNDGATVLALLDIVHP----AAAVLVDIAKSQDDEVGDGTTSVTVLAGEF 106
Cdd:PRK12851 22 ILADAVKVTLGPKGRNVVI--DKSFgapTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAI 99
|
90
....*....|....
gi 18250944 107 LSKAKDFIMEGMAP 120
Cdd:PRK12851 100 VREGAKAVAAGANP 113
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
34-103 |
7.28e-07 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 51.73 E-value: 7.28e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18250944 34 AVTNCIKTTLGPRGMDKLIhaENKV---TITNDGATVLALLDIVHP----AAAVLVDIAKSQDDEVGDGTTSVTVLA 103
Cdd:PRK12849 21 KLADAVKVTLGPKGRNVVI--DKSFgapTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLA 95
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
35-527 |
1.66e-06 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 50.80 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 35 VTNCIKTTLGPRG----MDKLIHAENkvtITNDGATV---LALLDIVHPAAAVLV-DIAKSQDDEVGDGTTSVTVLAGEF 106
Cdd:PRK14104 23 LANAVKVTLGPKGrnvvLDKSFGAPR---ITKDGVTVakeIELEDKFENMGAQMVrEVASKSADAAGDGTTTATVLAQAI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 107 LSKAKDFIMEGMAPQTIikyyreacKQALNI-IDKIAINLsnkpyEETQKLLLRCAETTLNSKLVSTYRSFFAKMVVDAV 185
Cdd:PRK14104 100 VREGAKSVAAGMNPMDL--------KRGIDLaVEAVVADL-----VKNSKKVTSNDEIAQVGTISANGDAEIGKFLADAM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 186 NILEDDmdkdmiGIKKVPGATCLDSML--IKGVAFKKTFSYAGFEQQPKKFK---NPKILLLNvELELKAEKD-----NA 255
Cdd:PRK14104 167 KKVGNE------GVITVEEAKSLETELdvVEGMQFDRGYISPYFVTNADKMRvemDDAYILIN-EKKLSSLNEllpllEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 256 EIRINDPL-IYQSIIDAE--WKIIYDKLEAiydiGANVVLSKLP-IGDIATQFFAEKNIFCAG---------RVDEIDMK 322
Cdd:PRK14104 240 VVQTGKPLvIVAEDVEGEalATLVVNRLRG----GLKVAAVKAPgFGDRRKAMLQDIAILTGGqaisedlgiKLENVTLQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 323 RVAKATGGLVQ----TTIHG------ITDCCLGTCGVFEEMQLGSERYNIFTECPNTKTTTIILRGGAQQFIDEAERS-- 390
Cdd:PRK14104 316 MLGRAKKVMIDkentTIVNGagkkadIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKdr 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 391 LHDAIMIVRRSIKtNSIVVGGGAIEMEISRILREYSLSiMGKQQLIIHAYAKALECIPQTLARNSGFDATDVLNKL--RK 468
Cdd:PRK14104 396 VDDAMHATRAAVE-EGIVPGGGVALLRASEQLKGIKTK-NDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKIleKE 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 18250944 469 EYAmnkgqgmkYGVDCINGGICDAYAACIWEPSLVKRNAIYSATEAACLVLSIDETIKQ 527
Cdd:PRK14104 474 QYS--------YGFDSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAE 524
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
34-103 |
5.52e-06 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 48.97 E-value: 5.52e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18250944 34 AVTNCIKTTLGPRGMDKLIhaENKV---TITNDGATV---LALLDIVHPAAAVLV-DIAKSQDDEVGDGTTSVTVLA 103
Cdd:PRK00013 21 KLADAVKVTLGPKGRNVVL--EKSFgapTITKDGVTVakeIELEDPFENMGAQLVkEVASKTNDVAGDGTTTATVLA 95
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
42-125 |
3.75e-03 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 39.91 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18250944 42 TLGPRGMDKLIHAE-NKVTITNDGATV---LALLDIVHPAAAVLVDIAKSQ-DDEVGDGTTSVTVLAGEFLSKAKDFIME 116
Cdd:PLN03167 85 TLGPKGRNVVLESKyGSPKIVNDGVTVakeVELEDPVENIGAKLVRQAAAKtNDLAGDGTTTSVVLAQGLIAEGVKVVAA 164
|
....*....
gi 18250944 117 GMAPQTIIK 125
Cdd:PLN03167 165 GANPVQITR 173
|
|
| |
