|
Name |
Accession |
Description |
Interval |
E-value |
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
13-526 |
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: 913.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 13 KEGTDTSQGRAQIISNINACQVVVECIKTTLGPRGMDKLIHSGN-DVTITNDGATVLKLLEVAHPAAAVLVDIAKSQDDE 91
Cdd:cd03340 6 KEGTDTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRgKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 92 VGDGTTSVTILAGELLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIISKDDAEKRSLLAKCAETTLNSKLLS 171
Cdd:cd03340 86 VGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDKEEQRELLEKCAATALNSKLIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 172 GHKTFFAKMVVDAVMLLDSDLDQEMIGIKKVTGGSCIDSMLVKGVAFKKTFTYAGAEQQPKKFLNPKILLINIELELKAE 251
Cdd:cd03340 166 SEKEFFAKMVVDAVLSLDDDLDLDMIGIKKVPGGSLEDSQLVNGVAFKKTFSYAGFEQQPKKFKNPKILLLNVELELKAE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 252 KENAEILIKDPKQYQSIIDAEWTILHDKLEKIAKMGTNIVLSKLPIGDIATQFFADRNIFAAGRVEQADMIRTSKATGAS 331
Cdd:cd03340 246 KDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEEDLKRVAQATGGS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 332 IQNTVNGISTDVLGTCGRFEEKQIGNDRFNIFEDCPKTTTATIILRGGAQQFIEESERSLNDAICVVRRTTKTHTIVGGG 411
Cdd:cd03340 326 IQTTVSNITDDVLGTCGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRAIKNDSVVAGG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 412 GAVEMELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHAlsKEGVNWFGVNCMNGDIVD 491
Cdd:cd03340 406 GAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHA--QGGGKWYGVDINNEGIAD 483
|
490 500 510
....*....|....*....|....*....|....*
gi 1624726457 492 TFEECIWEPAMVKKNALYAATEAACQVLSIDETVK 526
Cdd:cd03340 484 NFEAFVWEPSLVKINALTAATEAACLILSVDETIK 518
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
13-526 |
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: 756.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 13 KEGTDTSQGRAQIISNINACQVVVECIKTTLGPRGMDKLIHSGN-DVTITNDGATVLKLLEVAHPAAAVLVDIAKSQDDE 91
Cdd:TIGR02345 8 KEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNgKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 92 VGDGTTSVTILAGELLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIiSKDDAEKRSLLAKCAETTLNSKLLS 171
Cdd:TIGR02345 88 VGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTI-DEEKGEQRELLEKCAATALSSKLIS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 172 GHKTFFAKMVVDAVMLLDSD-LDQEMIGIKKVTGGSCIDSMLVKGVAFKKTFTYAGAEQQPKKFLNPKILLINIELELKA 250
Cdd:TIGR02345 167 HNKEFFSKMIVDAVLSLDRDdLDLKLIGIKKVQGGALEDSQLVNGVAFKKTFSYAGFEQQPKKFANPKILLLNVELELKA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 251 EKENAEILIKDPKQYQSIIDAEWTILHDKLEKIAKMGTNIVLSKLPIGDIATQFFADRNIFAAGRVEQADMIRTSKATGA 330
Cdd:TIGR02345 247 EKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAEDLKRVIKACGG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 331 SIQNTVNGISTDVLGTCGRFEEKQIGNDRFNIFEDCPKTTTATIILRGGAQQFIEESERSLNDAICVVRRTTKTHTIVGG 410
Cdd:TIGR02345 327 SIQSTTSDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVRRALKNKKIVAG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 411 GGAVEMELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHALskeGVNWFGVNCMNGDIV 490
Cdd:TIGR02345 407 GGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAK---GGKWYGVDINTEDIG 483
|
490 500 510
....*....|....*....|....*....|....*.
gi 1624726457 491 DTFEECIWEPAMVKKNALYAATEAACQVLSIDETVK 526
Cdd:TIGR02345 484 DNFEAFVWEPALVKINALKAAFEAACTILSVDETIT 519
|
|
| 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: 550.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 16 TDTSQGRAQIISNINACQVVVECIKTTLGPRGMDKLIHSGN-DVTITNDGATVLKLLEVAHPAAAVLVDIAKSQDDEVGD 94
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLgDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 95 GTTSVTILAGELLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIISKDdaekRSLLAKCAETTLNSKLLSGHK 174
Cdd:cd00309 81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVED----REELLKVATTSLNSKLVSGGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 175 TFFAKMVVDAVMLL---DSDLDQEMIGIKKVTGGSCIDSMLVKGVAFKKTFTYAGAeqqPKKFLNPKILLINIELElkae 251
Cdd:cd00309 157 DFLGELVVDAVLKVgkeNGDVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYM---PKRLENAKILLLDCKLE---- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 252 kenaeilikdpkqyqsiidaewtilhdklekiakmgtNIVLSKLPIGDIATQFFADRNIFAAGRVEQADMIRTSKATGAS 331
Cdd:cd00309 230 -------------------------------------YVVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGAT 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 332 IQNTVNGISTDVLGTCGRFEEKQIGNDRFNIFEDCPKTTTATIILRGGAQQFIEESERSLNDAICVVRRTTKTHTIVGGG 411
Cdd:cd00309 273 IVSRLEDLTPEDLGTAGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 412 GAVEMELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHAlskEGVNWFGVNCMNGDIVD 491
Cdd:cd00309 353 GAAEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHA---EGGGNAGGDVETGEIVD 429
|
490 500 510
....*....|....*....|....*....|....*
gi 1624726457 492 TFEECIWEPAMVKKNALYAATEAACQVLSIDETVK 526
Cdd:cd00309 430 MKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
39-526 |
0e+00 |
|
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: 536.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 39 IKTTLGPRGMDKLIHS-GNDVTITNDGATVLKLLEVAHPAAAVLVDIAKSQDDEVGDGTTSVTILAGELLTEAKQFIIDG 117
Cdd:pfam00118 5 VRTSLGPKGMDKMLVNsGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKLLAAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 118 ISPQVIIKYFRLACERALKQIESMavnIISKDDAEKRSLLAKCAETTLNSKLLSGHKTFFAKMVVDAVMLL---DSDLDQ 194
Cdd:pfam00118 85 VHPTTIIEGYEKALEKALEILDSI---ISIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAIpknDGSFDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 195 EMIGIKKVTGGSCIDSMLVKGVAFKKTFTYagaEQQPKKFLNPKILLINIELELKAEKENAEILIKDPKQYQSIIDAEWT 274
Cdd:pfam00118 162 GNIGVVKILGGSLEDSELVDGVVLDKGPLH---PDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 275 ILHDKLEKIAKMGTNIVLSKLPIGDIATQFFADRNIFAAGRVEQADMIRTSKATGASIQNTVNGISTDVLGTCGRFEEKQ 354
Cdd:pfam00118 239 QILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 355 IGNDRFNIFEDCPKTTTATIILRGGAQQFIEESERSLNDAICVVRRTTKTHTIVGGGGAVEMELSKALREYSLSVVGKQQ 434
Cdd:pfam00118 319 IGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSGKEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 435 LIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHAlskEGVNWFGVNCMNGDIVDTFEECIWEPAMVKKNALYAATEA 514
Cdd:pfam00118 399 LAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAHA---SGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEA 475
|
490
....*....|..
gi 1624726457 515 ACQVLSIDETVK 526
Cdd:pfam00118 476 ASTILRIDDIIK 487
|
|
| thermosome_alpha |
NF041082 |
thermosome subunit alpha; |
13-522 |
4.54e-163 |
|
thermosome subunit alpha;
Pssm-ID: 469009 Cd Length: 518 Bit Score: 473.22 E-value: 4.54e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 13 KEGTDTSQGRAQIISNINACQVVVECIKTTLGPRGMDK-LIHSGNDVTITNDGATVLKLLEVAHPAAAVLVDIAKSQDDE 91
Cdd:NF041082 7 KEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKmLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAKTQDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 92 VGDGTTSVTILAGELLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIiskdDAEKRSLLAKCAETTLNSKLLS 171
Cdd:NF041082 87 VGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKV----DPDDKETLKKIAATAMTGKGAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 172 GHKTFFAKMVVDAVMLL-----DSDLDQEMIGIKKVTGGSCIDSMLVKGVAFKKTFTYAGaeqQPKKFLNPKILLINIEL 246
Cdd:NF041082 163 AAKDKLADLVVDAVKAVaekdgGYNVDLDNIKVEKKVGGSIEDSELVEGVVIDKERVHPG---MPKRVENAKIALLDAPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 247 ELKAEKENAEILIKDPKQYQSIIDAEWTILHDKLEKIAKMGTNIVLSKLPIGDIATQFFADRNIFAAGRVEQADMIRTSK 326
Cdd:NF041082 240 EVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 327 ATGASIQNTVNGISTDVLGTCGRFEEKQIGNDRFNIFEDCPKTTTATIILRGGAQQFIEESERSLNDAICVVRRTTKTHT 406
Cdd:NF041082 320 ATGARIVTSIDDLSPEDLGYAGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDGK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 407 IVGGGGAVEMELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHAlskEGVNWFGVNCMN 486
Cdd:NF041082 400 VVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAHE---KGNKTAGLDVYT 476
|
490 500 510
....*....|....*....|....*....|....*.
gi 1624726457 487 GDIVDTFEECIWEPAMVKKNALYAATEAACQVLSID 522
Cdd:NF041082 477 GKVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRID 512
|
|
| thermosome_beta |
NF041083 |
thermosome subunit beta; |
13-523 |
2.00e-159 |
|
thermosome subunit beta;
Pssm-ID: 469010 Cd Length: 519 Bit Score: 464.04 E-value: 2.00e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 13 KEGTDTSQGRAQIISNINACQVVVECIKTTLGPRGMDK-LIHSGNDVTITNDGATVLKLLEVAHPAAAVLVDIAKSQDDE 91
Cdd:NF041083 7 KEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKmLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 92 VGDGTTSVTILAGELLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVniisKDDAEKRSLLAKCAETTLNSKLLS 171
Cdd:NF041083 87 VGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAE----KVDPDDRETLKKIAETSLTSKGVE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 172 GHKTFFAKMVVDAVMLL--------DSDLDQemIGIKKVTGGSCIDSMLVKGVAFKKTFTYAGaeqQPKKFLNPKILLIN 243
Cdd:NF041083 163 EARDYLAEIAVKAVKQVaekrdgkyYVDLDN--IQIEKKHGGSIEDTQLIYGIVIDKEVVHPG---MPKRVENAKIALLD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 244 IELELKAEKENAEILIKDPKQYQSIIDAEWTILHDKLEKIAKMGTNIVLSKLPIGDIATQFFADRNIFAAGRVEQADMIR 323
Cdd:NF041083 238 APLEVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 324 TSKATGASIQNTVNGISTDVLGTCGRFEEKQIGNDRFNIFEDCPKTTTATIILRGGAQQFIEESERSLNDAICVVRRTTK 403
Cdd:NF041083 318 LAKATGARIVTNIDDLTPEDLGYAELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 404 THTIVGGGGAVEMELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHalsKEGVNWFGVN 483
Cdd:NF041083 398 DGKIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAH---EKGKKWAGIN 474
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1624726457 484 CMNGDIVDTFEECIWEPAMVKKNALYAATEAACQVLSIDE 523
Cdd:NF041083 475 VFTGEVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDD 514
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
13-523 |
2.12e-159 |
|
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: 463.66 E-value: 2.12e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 13 KEGTDTSQGRAQIISNINACQVVVECIKTTLGPRGMDK-LIHSGNDVTITNDGATVLKLLEVAHPAAAVLVDIAKSQDDE 91
Cdd:cd03343 5 KEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKmLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 92 VGDGTTSVTILAGELLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIiskdDAEKRSLLAKCAETTLNSKLLS 171
Cdd:cd03343 85 VGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKV----DPDDKDTLRKIAKTSLTGKGAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 172 GHKTFFAKMVVDAVMLLDSD------LDQEMIGIKKVTGGSCIDSMLVKGVAFKKTFTYagaEQQPKKFLNPKILLINIE 245
Cdd:cd03343 161 AAKDKLADLVVDAVLQVAEKrdgkyvVDLDNIKIEKKTGGSVDDTELIRGIVIDKEVVH---PGMPKRVENAKIALLDAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 246 LELKAEKENAEILIKDPKQYQSIIDAEWTILHDKLEKIAKMGTNIVLSKLPIGDIATQFFADRNIFAAGRVEQADMIRTS 325
Cdd:cd03343 238 LEVKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 326 KATGASIQNTVNGISTDVLGTCGRFEEKQIGNDRFNIFEDCPKTTTATIILRGGAQQFIEESERSLNDAICVVRRTTKTH 405
Cdd:cd03343 318 RATGAKIVTNIDDLTPEDLGEAELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 406 TIVGGGGAVEMELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHAlskEGVNWFGVNCM 485
Cdd:cd03343 398 KVVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHE---KGNKNAGLDVY 474
|
490 500 510
....*....|....*....|....*....|....*...
gi 1624726457 486 NGDIVDTFEECIWEPAMVKKNALYAATEAACQVLSIDE 523
Cdd:cd03343 475 TGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDD 512
|
|
| thermosome_arch |
TIGR02339 |
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ... |
13-525 |
6.64e-154 |
|
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: 449.91 E-value: 6.64e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 13 KEGTDTSQGRAQIISNINACQVVVECIKTTLGPRGMDK-LIHSGNDVTITNDGATVLKLLEVAHPAAAVLVDIAKSQDDE 91
Cdd:TIGR02339 6 KEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKmLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 92 VGDGTTSVTILAGELLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIiskdDAEKRSLLAKCAETTLNSKLLS 171
Cdd:TIGR02339 86 VGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKI----SPEDRDLLKKIAYTSLTSKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 172 GH-KTFFAKMVVDAVMLL-------DSDLDQEMIGIKKVTGGSCIDSMLVKGVAFKKTFTYAGaeqQPKKFLNPKILLIN 243
Cdd:TIGR02339 162 EVaKDKLADLVVEAVKQVaelrgdgKYYVDLDNIKIVKKKGGSIEDTELVEGIVVDKEVVHPG---MPKRVENAKIALLD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 244 IELELKAEKENAEILIKDPKQYQSIIDAEWTILHDKLEKIAKMGTNIVLSKLPIGDIATQFFADRNIFAAGRVEQADMIR 323
Cdd:TIGR02339 239 APLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 324 TSKATGASIQNTVNGISTDVLGTCGRFEEKQIGNDRFNIFEDCPKTTTATIILRGGAQQFIEESERSLNDAICVVRRTTK 403
Cdd:TIGR02339 319 LARATGARIVSSIDEITESDLGYAELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 404 THTIVGGGGAVEMELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHAlskEGVNWFGVN 483
Cdd:TIGR02339 399 DGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHE---KGNKNAGIN 475
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1624726457 484 CMNGDIVDTFEECIWEPAMVKKNALYAATEAACQVLSIDETV 525
Cdd:TIGR02339 476 VFTGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVI 517
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
28-526 |
4.43e-140 |
|
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: 414.76 E-value: 4.43e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 28 NINACQVVVECIKTTLGPRGMDK-LIHSGNDVTITNDGATVLKLLEVAHPAAAVLVDIAKSQDDEVGDGTTSVTILAGEL 106
Cdd:cd03335 13 NVTAAMAIANIVKSSLGPVGLDKmLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIAAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 107 LTEAKQFIIDGISPQVIIKYFRLACERALKQI-ESMAVNIiskDDAEKRSLLaKCAETTLNSKLLSGHKTFFAKMVVDAV 185
Cdd:cd03335 93 LKRANELVKQKIHPTTIISGYRLACKEAVKYIkEHLSISV---DNLGKESLI-NVAKTSMSSKIIGADSDFFANMVVDAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 186 MLLDS-DLDQEM------IGIKKVTGGSCIDSMLVKGVAFKKTftyAGAEQQPKKFLNPKILLINIELELKAEKENAEIL 258
Cdd:cd03335 169 LAVKTtNEKGKTkypikaVNILKAHGKSAKESYLVNGYALNCT---RASQGMPTRVKNAKIACLDFNLQKTKMKLGVQVV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 259 IKDPKQYQSIIDAEWTILHDKLEKIAKMGTNIVLSKLPIGDIATQFFADRNIFAAGRVEQADMIRTSKATGASIQNTVNG 338
Cdd:cd03335 246 VTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVSTLAN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 339 I------STDVLGTCGRFEEKQIGNDRFNIFEDCPKTTTATIILRGGAQQFIEESERSLNDAICVVRRTTKTHTIVGGGG 412
Cdd:cd03335 326 LegeetfDPSYLGEAEEVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVVPGGG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 413 AVEMELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHALS-----KEGVNWFGVNCMNG 487
Cdd:cd03335 406 AVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHAAAqvkpdKKHLKWYGLDLING 485
|
490 500 510
....*....|....*....|....*....|....*....
gi 1624726457 488 DIVDTFEECIWEPAMVKKNALYAATEAACQVLSIDETVK 526
Cdd:cd03335 486 KVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLIK 524
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
15-526 |
1.19e-136 |
|
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: 406.41 E-value: 1.19e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 15 GTDTSQGRAQIISNINACQVVVECIKTTLGPRGMDK-LIHSGNDVTITNDGATVLKLLEVAHPAAAVLVDIAKSQDDEVG 93
Cdd:TIGR02340 4 GGERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKmLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 94 DGTTSVTILAGELLTEAKQFIIDGISPQVIIKYFRLACERALKQI-ESMAVNIiskdDAEKRSLLAKCAETTLNSKLLSG 172
Cdd:TIGR02340 84 DGTTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIkENLSVSV----DELGREALINVAKTSMSSKIIGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 173 HKTFFAKMVVDAVMLLDSDLDQ-------EMIGIKKVTGGSCIDSMLVKGVAFKKTftyAGAEQQPKKFLNPKILLINIE 245
Cdd:TIGR02340 160 DSDFFSNIVVDAVLAVKTTNENgetkypiKAINILKAHGKSARESMLVKGYALNCT---VASQQMPKRIKNAKIACLDFN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 246 LELKAEKENAEILIKDPKQYQSIIDAEWTILHDKLEKIAKMGTNIVLSKLPIGDIATQFFADRNIFAAGRVEQADMIRTS 325
Cdd:TIGR02340 237 LQKAKMALGVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 326 KATGASIQNTVNGISTD------VLGTCGRFEEKQIGNDRFNIFEDCPKTTTATIILRGGAQQFIEESERSLNDAICVVR 399
Cdd:TIGR02340 317 KATGATLVSTLADLEGEetfeasYLGFADEVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 400 RTTKTHTIVGGGGAVEMELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHALS-----K 474
Cdd:TIGR02340 397 RTLESNSVVPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHAAAqlkpeK 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1624726457 475 EGVNWFGVNCMNGDIVDTFEECIWEPAMVKKNALYAATEAACQVLSIDETVK 526
Cdd:TIGR02340 477 KHLKWYGLDLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIK 528
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
13-533 |
1.78e-130 |
|
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: 389.77 E-value: 1.78e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 13 KEGTDTSQGRAQIISNINACQVVVECIKTTLGPRGMDKLIHSG---NDVTITNDGATVLKLLEVAHPAAAVLVDIAKSQD 89
Cdd:cd03336 3 KDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILQSVgrsGGVTVTNDGATILKSIGVDNPAAKVLVDISKVQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 90 DEVGDGTTSVTILAGELLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIISKDDAEKRSLLaKCAETTLNSKL 169
Cdd:cd03336 83 DEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEEAFREDLL-NIARTTLSSKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 170 LSGHKTFFAKMVVDAVMLLDSDLDQEMIGIKKVTGGSCIDSMLVKGVAFKKTFTYAgaeqQPKKFLNPKILLINIELEL- 248
Cdd:cd03336 162 LTQDKEHFAELAVDAVLRLKGSGNLDAIQIIKKLGGSLKDSYLDEGFLLDKKIGVN----QPKRIENAKILIANTPMDTd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 249 KAEKENAEILIKDPKQYQSIIDAEWTILHDKLEKIAKMGTNIVLSKLPIGDIATQFFADRNIFAagrVEQAD---MIRTS 325
Cdd:cd03336 238 KIKIFGAKVRVDSTAKVAEIEEAEKEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMA---IEHADfdgVERLA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 326 KATGASIQNTVNGISTDVLGTCGRFEEKQIGNDRFNIFEDCPKTTTATIILRGGAQQFIEESERSLNDAICVVRRTTKTH 405
Cdd:cd03336 315 LVTGGEIASTFDHPELVKLGTCKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALCVLAQTVKDT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 406 TIVGGGGAVEMELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHAlskEGVNWFGVNCM 485
Cdd:cd03336 395 RVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHY---NGNTTAGLDMR 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1624726457 486 NGDIVDTFEECIWEPAMVKKNALYAATEAACQVLSIDETVKhaaqAAP 533
Cdd:cd03336 472 KGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIK----CAP 515
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
13-528 |
7.70e-130 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 389.00 E-value: 7.70e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 13 KEGTDTSQGRAQIISNINACQVVVECIKTTLGPRGMDKLIHS------GNDVTITNDGATVLKLLEVAHPAAAVLVDIAK 86
Cdd:PTZ00212 12 KQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDKILQPmsegprSGNVTVTNDGATILKSVWLDNPAAKILVDISK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 87 SQDDEVGDGTTSVTILAGELLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIiSKDDAEKRSLLAKCAETTLN 166
Cdd:PTZ00212 92 TQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDH-GSDEEKFKEDLLNIARTTLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 167 SKLLSGHKTFFAKMVVDAVMLLDSDLDQEMIGIKKVTGGSCIDSMLVKGVAFKKTFTYAgaeqQPKKFLNPKILLINIEL 246
Cdd:PTZ00212 171 SKLLTVEKDHFAKLAVDAVLRLKGSGNLDYIQIIKKPGGTLRDSYLEDGFILEKKIGVG----QPKRLENCKILVANTPM 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 247 EL-KAEKENAEILIKDPKQYQSIIDAEWTILHDKLEKIAKMGTNIVLSKLPIGDIATQFFADRNIFAagrVEQAD---MI 322
Cdd:PTZ00212 247 DTdKIKIYGAKVKVDSMEKVAEIEAAEKEKMKNKVDKILAHGCNVFINRQLIYNYPEQLFAEAGIMA---IEHADfdgME 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 323 RTSKATGASIQNTVNGISTDVLGTCGRFEEKQIGNDRFNIFEDCPKTTTATIILRGGAQQFIEESERSLNDAICVVRRTT 402
Cdd:PTZ00212 324 RLAAALGAEIVSTFDTPEKVKLGHCDLIEEIMIGEDKLIRFSGCAKGEACTIVLRGASTHILDEAERSLHDALCVLSQTV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 403 KTHTIVGGGGAVEMELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHAlskEGVNWFGV 482
Cdd:PTZ00212 404 KDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVSKLRAEHY---KGNKTAGI 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1624726457 483 NCMNGDIVDTFEECIWEPAMVKKNALYAATEAACQVLSIDETVKHA 528
Cdd:PTZ00212 481 DMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIRCA 526
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
27-525 |
5.07e-122 |
|
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: 368.15 E-value: 5.07e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 27 SNINACQVVVECIKTTLGPRGMDKLIHSGN-DVTITNDGATVLKLLEVAHPAAAVLVDIAKSQDDEVGDGTTSVTILAGE 105
Cdd:cd03338 12 SNIQAAKAVADAIRTSLGPRGMDKMIQTGKgEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGDGTTSVVVLAGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 106 LLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIISKDdaekRSLLAKCAETTLNSKLLSGHKTFFAKMVVDAV 185
Cdd:cd03338 92 LLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLND----RESLIKSATTSLNSKVVSQYSSLLAPIAVDAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 186 MLL-----DSDLDQEMIGIKKVTGGSCIDSMLVKGVAFKKTFTYAGAeqQPKKFLNPKILLINIELE-LKAEKENaEILI 259
Cdd:cd03338 168 LKVidpatATNVDLKDIRIVKKLGGTIEDTELVDGLVFTQKASKKAG--GPTRIEKAKIGLIQFCLSpPKTDMDN-NIVV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 260 KDPKQYQSIIDAEWTILHDKLEKIAKMGTNIVL---SKL--PIGDIATQFFADRNIFAAGRVEQADMIRTSKATGASIQN 334
Cdd:cd03338 245 NDYAQMDRILREERKYILNMCKKIKKSGCNVLLiqkSILrdAVSDLALHFLAKLKIMVVKDIEREEIEFICKTIGCKPVA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 335 TVNGISTDVLGTCGRFEEKQIGNDRFNIFEDCPKTT-TATIILRGGAQQFIEESERSLNDAICVVRRTTKTHTIVGGGGA 413
Cdd:cd03338 325 SIDHFTEDKLGSADLVEEVSLGDGKIVKITGVKNPGkTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRALIPGGGA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 414 VEMELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHAlskEGVNWFGVNCMNGDIVDTF 493
Cdd:cd03338 405 PEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHA---QGEKNAGINVRKGAITNIL 481
|
490 500 510
....*....|....*....|....*....|..
gi 1624726457 494 EECIWEPAMVKKNALYAATEAACQVLSIDETV 525
Cdd:cd03338 482 EENVVQPLLVSTSAITLATETVRMILKIDDIV 513
|
|
| TCP1_gamma |
cd03337 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ... |
13-525 |
2.81e-120 |
|
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: 362.38 E-value: 2.81e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 13 KEGTDTSQGRAQIISNINACQVVVECIKTTLGPRGMDK-LIHSGNDVTITNDGATVLKLLEVAHPAAAVLVDIAKSQDDE 91
Cdd:cd03337 6 NQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKmLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 92 VGDGTTSVTILAGELLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIISKDDAEkrslLAKCAETTLNSKLLS 171
Cdd:cd03337 86 VGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQ----MLKIIKSCIGTKFVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 172 GHKTFFAKMVVDAVMLLDSDLDQEM--IGIK------KVTGGSCIDSMLVKGVAFKKTFTYAGAEqqpKKFLNPKILLIN 243
Cdd:cd03337 162 RWSDLMCNLALDAVKTVAVEENGRKkeIDIKryakveKIPGGEIEDSRVLDGVMLNKDVTHPKMR---RRIENPRIVLLD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 244 IELElkaekenaeilikdpkqYqsiidaewtilhdklekiakmgtnIVLSKLPIGDIATQFFADRNIFAAGRVEQADMIR 323
Cdd:cd03337 239 CPLE-----------------Y------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 324 TSKATGASIQNTVNGISTDVLGT-CGRFEEKQIGNDRFNIFEDCPKTTTATIILRGGAQQFIEESERSLNDAICVVRRTT 402
Cdd:cd03337 278 IARACGATIVNRPEELTESDVGTgAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNII 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 403 KTHTIVGGGGAVEMELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHALskEGVNWFGV 482
Cdd:cd03337 358 LNPKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQ--GENSTWGI 435
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1624726457 483 NCMNGDIVDTFEECIWEPAMVKKNALYAATEAACQVLSIDETV 525
Cdd:cd03337 436 DGETGDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIV 478
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
13-525 |
7.73e-111 |
|
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: 339.79 E-value: 7.73e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 13 KEGTDTSQGRAQIISNINACQVVVECIKTTLGPRGMDK-LIHSGNDVTITNDGATVLKLLEVAHPAAAVLVDIAKSQDDE 91
Cdd:TIGR02344 6 NQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKmLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 92 VGDGTTSVTILAGELLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIISKDDAEKRSLLAKCaettLNSKLLS 171
Cdd:TIGR02344 86 VGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSC----IGTKFVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 172 GHKTFFAKMVVDAVMLLDSDLD-QEMIGIK------KVTGGSCIDSMLVKGVAFKKTFTYagaeqqPK---KFLNPKILL 241
Cdd:TIGR02344 162 RWSDLMCDLALDAVRTVQRDENgRKEIDIKryakveKIPGGDIEDSCVLKGVMINKDVTH------PKmrrYIENPRIVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 242 INIELELKAEKENAEILIKDPKQYQSIIDAEWTILHDKLEKIAKMGTNIVLSKLPIGDIATQFFADRNIFAAGRVEQADM 321
Cdd:TIGR02344 236 LDCPLEYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 322 IRTSKATGASIQNTVNGISTDVLGT-CGRFEEKQIGNDRFNIFEDCPKTTTATIILRGGAQQFIEESERSLNDAICVVRR 400
Cdd:TIGR02344 316 NRIARACGATIVNRPEELRESDVGTgCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 401 TTKTHTIVGGGGAVEMELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHAlsKEGVNWF 480
Cdd:TIGR02344 396 VLLDPKLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHA--QENNCTW 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1624726457 481 GVNCMNGDIVDTFEECIWEPAMVKKNALYAATEAACQVLSIDETV 525
Cdd:TIGR02344 474 GIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIV 518
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
27-525 |
5.17e-109 |
|
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: 334.83 E-value: 5.17e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 27 SNINACQVVVECIKTTLGPRGMDKLIHSGN-DVTITNDGATVLKLLEVAHPAAAVLVDIAKSQDDEVGDGTTSVTILAGE 105
Cdd:TIGR02342 13 SNIVAAKAVADAIRTSLGPKGMDKMIQDGKgEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVILAGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 106 LLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIISKDdaekRSLLAKCAETTLNSKLLSGHKTFFAKMVVDAV 185
Cdd:TIGR02342 93 LLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSD----REQLLKSATTSLSSKVVSQYSSLLAPLAVDAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 186 MLL-----DSDLDQEMIGIKKVTGGSCIDSMLVKGVAFKKTFTYAGAEqqPKKFLNPKILLINIELEL-KAEKENaEILI 259
Cdd:TIGR02342 169 LKVidpenAKNVDLNDIKVVKKLGGTIDDTELIEGLVFTQKASKSAGG--PTRIEKAKIGLIQFQISPpKTDMEN-QIIV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 260 KDPKQYQSIIDAEWTILHDKLEKIAKMGTNIVLSKLPI-----GDIATQFFADRNIFAAGRVEQADMIRTSKATGASIQN 334
Cdd:TIGR02342 246 NDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGCKPIA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 335 TVNGISTDVLGTCGRFEEKQIGNDRFNIFEDCPKTT-TATIILRGGAQQFIEESERSLNDAICVVRRTTKTHTIVGGGGA 413
Cdd:TIGR02342 326 SIDHFTADKLGSAELVEEVDSDGGKIIKITGIQNAGkTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLIAGGGA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 414 VEMELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHALskeGVNWFGVNCMNGDIVDTF 493
Cdd:TIGR02342 406 PEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHAN---GEKTAGISVRKGGITNML 482
|
490 500 510
....*....|....*....|....*....|..
gi 1624726457 494 EECIWEPAMVKKNALYAATEAACQVLSIDETV 525
Cdd:TIGR02342 483 EEHVLQPLLVTTSAITLASETVRSILKIDDIV 514
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
27-526 |
3.81e-108 |
|
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: 332.73 E-value: 3.81e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 27 SNINACQVVVECIKTTLGPRGMDKLIHSG-NDVTITNDGATVLKLLEVAHPAAAVLVDIAKSQDDEVGDGTTSVTILAGE 105
Cdd:cd03339 27 SHILAAKSVANILRTSLGPRGMDKILVSPdGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 106 LLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIisKDDAEKRSLLAKCAETTLNSKLLSGHKTFFAKMVVDAV 185
Cdd:cd03339 107 LLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKI--EFSPDNKEPLIQTAMTSLGSKIVSRCHRQFAEIAVDAV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 186 M----LLDSDLDQEMIGIKKVTGGSCIDSMLVKGVAFKKTFTYAgaeQQPKKFLNPKILLINIELELKAEKENAEILIKD 261
Cdd:cd03339 185 LsvadLERKDVNFELIKVEGKVGGRLEDTKLVKGIVIDKDFSHP---QMPKEVKDAKIAILTCPFEPPKPKTKHKLDITS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 262 PKQYQSIIDAEWTILHDKLEKIAKMGTNIVLSKLPIGDIATQFFADRNIFAAGRVEQADMIRTSKATGASIQNTVNGIST 341
Cdd:cd03339 262 VEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGGVEIELIAIATGGRIVPRFEDLSP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 342 DVLGTCGRFEEKQIG--NDRFNIFEDCPKTTTATIILRGGAQQFIEESERSLNDAICVVRRTTKTHTIVGGGGAVEMELS 419
Cdd:cd03339 342 EKLGKAGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDALCVVRNLIRDNRIVYGGGAAEISCS 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 420 KALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHAlsKEGVNWFGVNCMNGDIVDTFEECIWE 499
Cdd:cd03339 422 LAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQV--KEKNPHLGIDCLGRGTNDMKEQKVFE 499
|
490 500
....*....|....*....|....*..
gi 1624726457 500 PAMVKKNALYAATEAACQVLSIDETVK 526
Cdd:cd03339 500 TLISKKQQILLATQVVKMILKIDDVIV 526
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
13-532 |
3.79e-103 |
|
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: 319.88 E-value: 3.79e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 13 KEGTDTSQGRAQIISNINACQVVVECIKTTLGPRGMDKLIHSGN---DVTITNDGATVLKLLEVAHPAAAVLVDIAKSQD 89
Cdd:TIGR02341 4 KDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQSSSsdaSIMVTNDGATILKSIGVDNPAAKVLVDMSKVQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 90 DEVGDGTTSVTILAGELLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIiSKDDAEKRSLLAKCAETTLNSKL 169
Cdd:TIGR02341 84 DEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDN-GSDEVKFRQDLMNIARTTLSSKI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 170 LSGHKTFFAKMVVDAVMLLDSDLDQEMIGIKKVTGGSCIDSMLVKGVAFKKTFtyagAEQQPKKFLNPKILLINIELEL- 248
Cdd:TIGR02341 163 LSQHKDHFAQLAVDAVLRLKGSGNLEAIQIIKKLGGSLADSYLDEGFLLDKKI----GVNQPKRIENAKILIANTGMDTd 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 249 KAEKENAEILIKDPKQYQSIIDAEWTILHDKLEKIAKMGTNIVLSKLPIGDIATQFFADRNIFAagrVEQADMI---RTS 325
Cdd:TIGR02341 239 KVKIFGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMA---IEHADFEgveRLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 326 KATGASIQNTVNGISTDVLGTCGRFEEKQIGNDRFNIFEDCPKTTTATIILRGGAQQFIEESERSLNDAICVVRRTTKTH 405
Cdd:TIGR02341 316 LVTGGEIVSTFDHPELVKLGSCDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTVKES 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 406 TIVGGGGAVEMELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHAlskEGVNWFGVNCM 485
Cdd:TIGR02341 396 RTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHY---NGNTTMGLDMN 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1624726457 486 NGDIVDTFEECIWEPAMVKKNALYAATEAACQVLSIDETVKHAAQAA 532
Cdd:TIGR02341 473 EGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPRKR 519
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
27-525 |
1.92e-99 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 309.32 E-value: 1.92e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 27 SNINACQVVVECIKTTLGPRGMDK-LIHSGNDVTITNDGATVLKLLEVAHP----AAAVLVDIAKSQDDEVGDGTTSVTI 101
Cdd:COG0459 14 ANIRGVKALADAVKVTLGPKGRNVmLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDGTTTATV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 102 LAGELLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIISKDDaekrslLAKCAETTLNSKllsghkTFFAKMV 181
Cdd:COG0459 94 LAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEE------LAQVATISANGD------EEIGELI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 182 VDAVMLLDSDldqemiGIKKV--TGGSCIDSMLVKGVAFKKTF----TYAGAEQQPKKFLNPKILLINIELElkaekeNA 255
Cdd:COG0459 162 AEAMEKVGKD------GVITVeeGKGLETELEVVEGMQFDKGYlspyFVTDPEKMPAELENAYILLTDKKIS------SI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 256 EILIkdpkqyqsiidaewtilhDKLEKIAKMGTNIVLSKLPIGDIATQFFADRNIFAAGRV-----------EQADMIRT 324
Cdd:COG0459 230 QDLL------------------PLLEKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgdrRKAMLEDI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 325 SKATGASI-----QNTVNGISTDVLGTCGRFEekqIGNDRFNIFEDCPKTTTATIILRGGAQQFIEESERSLNDAICVVR 399
Cdd:COG0459 292 AILTGGRVisedlGLKLEDVTLDDLGRAKRVE---VDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRVEDALHATR 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 400 RTTKtHTIVGGGGAVEMELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRrdhalsKEGVNW 479
Cdd:COG0459 369 AAVE-EGIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVR------AAKDKG 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1624726457 480 FGVNCMNGDIVDTFEECIWEPAMVKKNALYAATEAACQVLSIDETV 525
Cdd:COG0459 442 FGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVI 487
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
20-526 |
4.18e-98 |
|
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: 307.11 E-value: 4.18e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 20 QGRAQIISNINACQVVVECIKTTLGPRGMDKLIHSGN-DVTITNDGATVLKLLEVAHPAAAVLVDIAKSQDDEVGDGTTS 98
Cdd:TIGR02343 24 KGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDgDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 99 VTILAGELLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIisKDDAEKRSLLAKCAETTLNSKLLSGHKTFFA 178
Cdd:TIGR02343 104 VVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEI--SADNNNREPLIQAAKTSLGSKIVSKCHRRFA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 179 KMVVDAV-MLLD---SDLDQEMIGIKKVTGGSCIDSMLVKGVAFKKTFTYAgaeQQPKKFLNPKILLINIELELKAEKEN 254
Cdd:TIGR02343 182 EIAVDAVlNVADmerRDVDFDLIKVEGKVGGSLEDTKLIKGIIIDKDFSHP---QMPKEVEDAKIAILTCPFEPPKPKTK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 255 AEILIKDPKQYQSIIDAEWTILHDKLEKIAKMGTNIVLSKLPIGDIATQFFADRNIFAAGRVEQADMIRTSKATGASIQN 334
Cdd:TIGR02343 259 HKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQELELIAIATGGRIVP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 335 TVNGISTDVLGTCGRFEEKQIG--NDRFNIFEDCPKTTTATIILRGGAQQFIEESERSLNDAICVVRRTTKTHTIVGGGG 412
Cdd:TIGR02343 339 RFQELSKDKLGKAGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSRIVYGGG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 413 AVEMELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHAlsKEGVNWFGVNCMNGDIVDT 492
Cdd:TIGR02343 419 AAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQL--KEKNPNLGVDCLGYGTNDM 496
|
490 500 510
....*....|....*....|....*....|....
gi 1624726457 493 FEECIWEPAMVKKNALYAATEAACQVLSIDETVK 526
Cdd:TIGR02343 497 KEQFVFETLIGKKQQILLATQLVRMILKIDDVIS 530
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
25-525 |
2.42e-95 |
|
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: 297.98 E-value: 2.42e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 25 IISNINACQVVVECIKTTLGPRGMDKLI--HSGNdVTITNDGATVLKLLEVAHPAAAVLVDIAKSQDDEVGDGTTSVTIL 102
Cdd:cd03341 10 VLRNIEACKELSQITRTSYGPNGMNKMVinHLEK-LFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 103 AGELLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIISkdDAEKRSLLAKCAETTLNSKLLsGHKTFFAKMVV 182
Cdd:cd03341 89 AGELLEKAEELLRMGLHPSEIIEGYEKALKKALEILEELVVYKIE--DLRNKEEVSKALKTAIASKQY-GNEDFLSPLVA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 183 DAVMLL----DSDLDQEMIGIKKVTGGSCIDSMLVKGVAFKKtftyaGAEQQPKKFLNPKILLINIELElkaekenaeil 258
Cdd:cd03341 166 EACISVlpenIGNFNVDNIRVVKILGGSLEDSKVVRGMVFKR-----EPEGSVKRVKKAKVAVFSCPFD----------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 259 ikdpkqyqsiidaewtilhdklekiakMGTNIVLSKLPIGDIAtQFFADR-NIFAAGRVEQADMIRTSKATGASIQNTVN 337
Cdd:cd03341 230 ---------------------------IGVNVIVAGGSVGDLA-LHYCNKyGIMVIKINSKFELRRLCRTVGATPLPRLG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 338 GISTDVLGTCGRFEEKQIGNDRFNIFEDCPKTT-TATIILRGGAQQFIEESERSLNDAICVVRRTTKTHTIVGGGGAVEM 416
Cdd:cd03341 282 APTPEEIGYCDSVYVEEIGDTKVVVFRQNKEDSkIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGATEI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 417 ELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHalsKEGVNWFGVNCMNGD--IVDTFE 494
Cdd:cd03341 362 ELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAH---QKGNKSAGVDIESGDegTKDAKE 438
|
490 500 510
....*....|....*....|....*....|.
gi 1624726457 495 ECIWEPAMVKKNALYAATEAACQVLSIDETV 525
Cdd:cd03341 439 AGIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
13-525 |
5.15e-91 |
|
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: 288.54 E-value: 5.15e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 13 KEGTDTSQG-RAQIISNINACQVVVECIKTTLGPRGMDKLI--HSGNdVTITNDGATVLKLLEVAHPAAAVLVDIAKSQD 89
Cdd:TIGR02346 7 KEGYRHFSGlEEAVIKNIEACKELSQITRTSLGPNGMNKMVinHLEK-LFVTNDAATILRELEVQHPAAKLLVMASEMQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 90 DEVGDGTTSVTILAGELLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIIsKDDAEKRSLLaKCAETTLNSKL 169
Cdd:TIGR02346 86 NEIGDGTNLVLVLAGELLNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVVWEV-KDLRDKDELI-KALKASISSKQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 170 LsGHKTFFAKMVVDAVMLL----DSDLDQEMIGIKKVTGGSCIDSMLVKGVAFKKTftyagAEQQPKKFLNPKILLINIE 245
Cdd:TIGR02346 164 Y-GNEDFLAQLVAQACSTVlpknPQNFNVDNIRVCKILGGSLSNSEVLKGMVFNRE-----AEGSVKSVKNAKVAVFSCP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 246 LELKAEKENAEILIKDPKQYQSIIDAEWTILHDKLEKIAKMGTNIVLSKLPIGDIATQFFADRNIFAAGRVEQADMIRTS 325
Cdd:TIGR02346 238 LDTATTETKGTVLIHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLC 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 326 KATGASIQNTVNGISTDVLGTCGRFEEKQIGNDRFNIFEDCPK-TTTATIILRGGAQQFIEESERSLNDAICVVRRTTKT 404
Cdd:TIGR02346 318 KTVGATPLPRLGAPTPEEIGYVDSVYVSEIGGDKVTVFKQENGdSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 405 HTIVGGGGAVEMELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHalsKEGVNWFGVNC 484
Cdd:TIGR02346 398 GRLLPGAGATEIELASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAH---KKGNKSKGIDI 474
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1624726457 485 MNGD--IVDTFEECIWEPAMVKKNALYAATEAACQVLSIDETV 525
Cdd:TIGR02346 475 EAESdgVKDASEAGIYDMLATKKWAIKLATEAAVTVLRVDQII 517
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
28-526 |
1.55e-81 |
|
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: 263.90 E-value: 1.55e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 28 NINACQVVVECIKTTLGPRGMDKLIHSGN-DVTITNDGATVLKLLEVAHPAAAVLVDIAKSQDDEVGDGTTSVTILAGEL 106
Cdd:TIGR02347 21 NINAARGLQDVLKTNLGPKGTLKMLVSGAgDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 107 LTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIISKDDaekRSLLAKCAETTLNSKLLSGHKTFFAKMVVDAVM 186
Cdd:TIGR02347 101 LKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKEDEVD---REFLLNVARTSLRTKLPADLADQLTEIVVDAVL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 187 LL---DSDLDQEMIGIKKVTGGSCIDSMLVKGVAFKKTFTYAGaeqQPKKFLNPKILLINIELELKAEKENAEILIKDPK 263
Cdd:TIGR02347 178 AIkkdGEDIDLFMVEIMEMKHKSATDTTLIRGLVLDHGARHPD---MPRRVKNAYILTCNVSLEYEKTEVNSGFFYSSAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 264 QYQSIIDAEWTILHDKLEKIAKMgTNIVLSKLP-----------IGDIATQFFADRNIFAAGRVEQADMIRTSKATGASI 332
Cdd:TIGR02347 255 QREKLVKAERKFVDDRVKKIIEL-KKKVCGKSPdkgfvvinqkgIDPPSLDLLAKEGIMALRRAKRRNMERLTLACGGEA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 333 QNTVNGISTDVLGTCGRFEEKQIGNDRFNIFEDCPKTTTATIILRGGAQQFIEESERSLNDAICVVRRTTKTHTIVGGGG 412
Cdd:TIGR02347 334 LNSVEDLTPECLGWAGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLRAVKNAIEDKCVVPGAG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 413 AVEMELSKALREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHalsKEGVNWFGVNCMNGDIVDT 492
Cdd:TIGR02347 414 AFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEH---DEGGEVVGVDLNTGEPIDP 490
|
490 500 510
....*....|....*....|....*....|....
gi 1624726457 493 FEECIWEPAMVKKNALYAATEAACQVLSIDETVK 526
Cdd:TIGR02347 491 EIKGIWDNYRVKKQLIQSATVIASQLLLVDEVMR 524
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
28-526 |
4.49e-81 |
|
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: 261.42 E-value: 4.49e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 28 NINACQVVVECIKTTLGPRGMDKLIHSGN-DVTITNDGATVLKLLEVAHPAAAVLVDIAKSQDDEVGDGTTSVTILAGEL 106
Cdd:cd03342 17 NISAAKGLQDVLKTNLGPKGTLKMLVSGAgDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 107 LTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIISKDDaekRSLLAKCAETTLNSKLLSGHKTFFAKMVVDAVM 186
Cdd:cd03342 97 LKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIDTD---RELLLSVARTSLRTKLHADLADQLTEIVVDAVL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 187 LL---DSDLDQEMIGIKKVTGGSCIDSMLVKGVAFKKtftyaGAEQ--QPKKFLNPKILLINIELELKAEKENAEILIKd 261
Cdd:cd03342 174 AIykpDEPIDLHMVEIMQMQHKSDSDTKLIRGLVLDH-----GARHpdMPKRVENAYILTCNVSLEYEKTEVNSGFFYS- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 262 pkqyqsiidaewtilhdklekiakmgtnIVLSKLPIGDIATQFFADRNIFAAGRVEQADMIRTSKATGASIQNTVNGIST 341
Cdd:cd03342 248 ----------------------------VVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLACGGVAMNSVDDLSP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 342 DVLGTCGRFEEKQIGNDRFNIFEDCPKTTTATIILRGGAQQFIEESERSLNDAICVVRRTTKTHTIVGGGGAVEMELSKA 421
Cdd:cd03342 300 ECLGYAGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKCVVPGAGAFEVALYAH 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 422 LREYSLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRRDHALSKEGVnwfGVNCMNGDIVDTFEECIWEPA 501
Cdd:cd03342 380 LKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYAEGGQVG---GVDLDTGEPMDPESEGIWDNY 456
|
490 500
....*....|....*....|....*
gi 1624726457 502 MVKKNALYAATEAACQVLSIDETVK 526
Cdd:cd03342 457 SVKRQILHSATVIASQLLLVDEIIR 481
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
154-403 |
2.26e-62 |
|
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: 203.47 E-value: 2.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 154 RSLLAKCAETTLNSKLlSGHKTFFAKMVVDAVMLL---DSDLDQEMIGIKKVTGGSCIDSMLVKGVAFKKTFTYAGAeqq 230
Cdd:cd03333 1 RELLLQVATTSLNSKL-SSWDDFLGKLVVDAVLKVgpdNRMDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPYM--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 231 PKKFLNPKILLINIELElkaekenaeilikdpkqyqsiidaewtilhdklekiakmgtNIVLSKLPIGDIATQFFADRNI 310
Cdd:cd03333 77 PKRLENAKILLLDCPLE-----------------------------------------YVVIAEKGIDDLALHYLAKAGI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 311 FAAGRVEQADMIRTSKATGASIQNTVNGISTDVLGTCGRFEEKQIGNDRFNIFEDCPKTTTATIILRGGAQQFIEESERS 390
Cdd:cd03333 116 MAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGTAELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVKRS 195
|
250
....*....|...
gi 1624726457 391 LNDAICVVRRTTK 403
Cdd:cd03333 196 LHDALCAVRAAVE 208
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
39-533 |
9.37e-21 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 95.56 E-value: 9.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 39 IKTTLGPRGMDKLIHSGNDV-TITNDGATVLKLLEVAHPAA---AVLV-DIAKSQDDEVGDGTTSVTILAGELLTEAKQF 113
Cdd:PRK12850 27 VKVTLGPKGRNVVLEKSFGApRITKDGVTVAKEIELEDKFEnmgAQMVkEVASKTNDLAGDGTTTATVLAQAIVREGAKL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 114 IIDGISPQVIIKYFRLACERALKQIESMAVNIISKDDaekrslLAKCAETTLNSKLLSGHktffakMVVDAVmlldsdld 193
Cdd:PRK12850 107 VAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKE------IAQVATISANGDESIGE------MIAEAM-------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 194 qEMIGIKKV-------TGGSCIDsmLVKGVAFKKTFT----YAGAEQQPKKFLNPKILLINIEL-ELKAEKENAEILIKD 261
Cdd:PRK12850 167 -DKVGKEGVitveeakTLGTELD--VVEGMQFDRGYLspyfVTNPEKMRAELEDPYILLHEKKIsNLQDLLPILEAVVQS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 262 PKQYQSI---IDAE--WTILHDKLEKIAKmgtnIVLSKLP-IGDIATQFFADRNIFAAGRVeqadmirTSKATGASIQNt 335
Cdd:PRK12850 244 GRPLLIIaedVEGEalATLVVNKLRGGLK----SVAVKAPgFGDRRKAMLEDIAVLTGGQV-------ISEDLGIKLEN- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 336 vngISTDVLGTCGR------------------------------FEEKQIGNDRFNIFEDCPKTTTATIILRGGAQQFIE 385
Cdd:PRK12850 312 ---VTLDMLGRAKRvlitkenttiidgagdkkniearvkqiraqIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 386 ESERSL--NDAICVVRRTTKtHTIVGGGGAVEMELSKALREYsLSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVI 463
Cdd:PRK12850 389 VKEKKDrvDDALHATRAAVE-EGIVPGGGVALLRARSALRGL-KGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVV 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1624726457 464 SKLRrdhalskEGVNWFGVNCMNGDIVDTFEECIWEPAMVKKNALYAATEAACQVLSIDETV-----KHAAQAAP 533
Cdd:PRK12850 467 GKVA-------ELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVaeapkKAAAAAAG 534
|
|
| Fab1_TCP |
cd03334 |
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ... |
189-379 |
1.82e-20 |
|
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: 91.13 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 189 DSDLDQEMIGIKKVTGGSCIDSMLVKGVAFKKTFTYagaEQQPKKFLNPKILLINIELELkaEKENAEILIKDPkqyqsI 268
Cdd:cd03334 42 DDMDIRQYVKIKKIPGGSPSDSEVVDGVVFTKNVAH---KRMPSKIKNPRILLLQGPLEY--QRVENKLLSLDP-----V 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 269 IDAEWTILHDKLEKIAKMGTNIVLSKLPIGDIATQFFADRNIFAAGRVEQADMIRTSKATGASIQNTVNGISTD-VLGTC 347
Cdd:cd03334 112 ILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISRCTGADIISSMDDLLTSpKLGTC 191
|
170 180 190
....*....|....*....|....*....|....*..
gi 1624726457 348 GRFEEKQIGNDR-----FNIFEDCPKTTTATIILRGG 379
Cdd:cd03334 192 ESFRVRTYVEEHgrsktLMFFEGCPKELGCTILLRGG 228
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
20-519 |
9.99e-20 |
|
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: 92.13 E-value: 9.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 20 QGRAQIISNINAcqvVVECIKTTLGPRGMDKLI-HSGNDVTITNDGATVLKLLEVAHP----AAAVLVDIAKSQDDEVGD 94
Cdd:cd03344 8 EARKALLRGVNK---LADAVKVTLGPKGRNVVIeKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 95 GTTSVTILAGELLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIISKDDaekrslLAKCAETTLNSKLLSGhk 174
Cdd:cd03344 85 GTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEE------IAQVATISANGDEEIG-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 175 tffaKMVVDAVmlldsdldqEMIGIKKV----TGGSCIDSM-LVKGVAFKKTftyagaeqqpkkFLNPKilLINIELELK 249
Cdd:cd03344 157 ----ELIAEAM---------EKVGKDGVitveEGKTLETELeVVEGMQFDRG------------YLSPY--FVTDPEKME 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 250 AEKENAEILIKDPK--QYQSIIDAewtilhdkLEKIAKMG---------------TNIVLSKL-----------P----- 296
Cdd:cd03344 210 VELENPYILLTDKKisSIQELLPI--------LELVAKAGrplliiaedvegealATLVVNKLrgglkvcavkaPgfgdr 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 297 ----IGDIAT----QFFADRNIFAAGRVEQADMIRTSKAT--------------GASIQNTVNGIstdvlgtCGRFEEKQ 354
Cdd:cd03344 282 rkamLEDIAIltggTVISEELGLKLEDVTLEDLGRAKKVVvtkddttiiggagdKAAIKARIAQI-------RKQIEETT 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 355 IGNDRFNIFEDCPKTTTATIILRGGAQQFIEESER--SLNDAICVVRRTTKThTIVGGGGAVEMELSKALrEYSLSVVGK 432
Cdd:cd03344 355 SDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKkdRVEDALNATRAAVEE-GIVPGGGVALLRASPAL-DKLKALNGD 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 433 QQLIINAFARALEVIPKTLAQNAGFNATDVISKLrrdhalsKEGVNWFGVNCMNGDIVDTFEECIWEPAMVKKNALYAAT 512
Cdd:cd03344 433 EKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKV-------LESPDGFGYDAATGEYVDMIEAGIIDPTKVVRSALQNAA 505
|
....*..
gi 1624726457 513 EAACQVL 519
Cdd:cd03344 506 SVASLLL 512
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
34-533 |
1.02e-18 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 89.13 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 34 VVVECIKTTLGPRGMDKLIH-SGNDVTITNDGATVLKLLEVA----HPAAAVLVDIAKSQDDEVGDGTTSVTILAGELLT 108
Cdd:PRK12852 22 ILANAVKVTLGPKGRNVVIEkSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKTNDLAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 109 EAKQFIIDGISPQviikyfrlacerALKQIESMAVNIISKDDAEKRSLLAKCAETTLNSKLLSGHKTFFAKMVVDAVMLL 188
Cdd:PRK12852 102 EGAKAVAAGMNPM------------DLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGKMIAQAMQKV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 189 DSDldqemiGIKKVTGGSCIDSML--VKGVAFKKTFT----YAGAEQQPKKFLNPKILLINIELE-LKAEKENAEILIKD 261
Cdd:PRK12852 170 GNE------GVITVEENKSLETEVdiVEGMKFDRGYLspyfVTNAEKMTVELDDAYILLHEKKLSgLQAMLPVLEAVVQS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 262 PKQYQSII-DAEWTILHDKLEKIAKMGTNIVLSKLP-IGDIATQFFADRNIFAAGRV---------EQADMIRTSKATGA 330
Cdd:PRK12852 244 GKPLLIIAeDVEGEALATLVVNRLRGGLKVAAVKAPgFGDRRKAMLEDIAILTGGQLisedlgiklENVTLKMLGRAKKV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 331 SIQ--NT--VNG------ISTDVLGTCGRFEEKQIGNDRFNIFEDCPKTTTATIILRGGAQQFIEESERS--LNDAICVV 398
Cdd:PRK12852 324 VIDkeNTtiVNGagkkadIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKdrVEDALNAT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 399 RRTTKtHTIVGGGGAVEMELSKALREYSlSVVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLrrdhaLSKEGVN 478
Cdd:PRK12852 404 RAAVQ-EGIVPGGGVALLRAKKAVGRIN-NDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKI-----LENKSET 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 479 wFGVNCMNGDIVDTFEECIWEPAMVKKNALYAATEAACQVLSIDETV-----KHAAQAAP 533
Cdd:PRK12852 477 -FGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVaelpkKDAAPAMP 535
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
29-515 |
4.38e-17 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 84.19 E-value: 4.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 29 INACQVVVECIKTTLGPRGMDKLIHS--GNDvTITNDGATVLKLLEVAHPA----AAVLVDIAKSQDDEVGDGTTSVTIL 102
Cdd:PTZ00114 28 LKGIERLADAVAVTLGPKGRNVIIEQeyGSP-KITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKAGDGTTTATIL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 103 AGELLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIISKDDAEKrslLAKCAeTTLNSKLlsghktffAKMVV 182
Cdd:PTZ00114 107 ARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILN---VATIS-ANGDVEI--------GSLIA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 183 DAVmlldsdldqEMIG----IKKVTGGSCIDS-MLVKGVAFkktftyagaeqqPKKFLNPKilLINIELELKAEKENAEI 257
Cdd:PTZ00114 175 DAM---------DKVGkdgtITVEDGKTLEDElEVVEGMSF------------DRGYISPY--FVTNEKTQKVELENPLI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 258 LIKDPK--QYQSII----------------------DAEWTILHDKLEKIAK--------MGTNivlSKLPIGDIAT--- 302
Cdd:PTZ00114 232 LVTDKKisSIQSILpilehavknkrplliiaedvegEALQTLIINKLRGGLKvcavkapgFGDN---RKDILQDIAVltg 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 303 -QFF-----------ADRNIFA-AGRVEQaDMIRTSKATG----ASIQNTVNGIStDVLGTCGRFEEKQIGNDRFNIFed 365
Cdd:PTZ00114 309 aTVVsednvglklddFDPSMLGsAKKVTV-TKDETVILTGggdkAEIKERVELLR-SQIERTTSEYDKEKLKERLAKL-- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 366 cpkTTTATIILRGGAQQF-IEESERSLNDAICVVRRTTKThTIVGGGGAVEMELSKALR--EYSLSVVGKQQLIINAFAR 442
Cdd:PTZ00114 385 ---SGGVAVIKVGGASEVeVNEKKDRIEDALNATRAAVEE-GIVPGGGVALLRASKLLDklEEDNELTPDQRTGVKIVRN 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624726457 443 ALEVIPKTLAQNAGFNATDVISKLRrdhalsKEGVNWFGVNCMNGDIVDTFEECIWEPAMVKKNALYAATEAA 515
Cdd:PTZ00114 461 ALRLPTKQIAENAGVEGAVVVEKIL------EKKDPSFGYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVA 527
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
34-533 |
3.51e-16 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 81.33 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 34 VVVECIKTTLGPRGMDKLIHSGNDV-TITNDGATVLKLLEVAHP----AAAVLVDIAKSQDDEVGDGTTSVTILAGELLT 108
Cdd:PRK12851 22 ILADAVKVTLGPKGRNVVIDKSFGApTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAGDGTTTATVLAQAIVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 109 EAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIISKDDAEKRSLLAKCAETTLnskllsghktffAKMVVDAVMLL 188
Cdd:PRK12851 102 EGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEI------------GRLVAEAMEKV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 189 DSDldqemiGIKKVTGGSCIDSML--VKGVAFKKTFT----YAGAEQQPKKFLNPKILLINIEL-ELKAEKENAEILIKD 261
Cdd:PRK12851 170 GNE------GVITVEESKTAETELevVEGMQFDRGYLspyfVTDADKMEAELEDPYILIHEKKIsNLQDLLPVLEAVVQS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 262 PKQYqsIIDAE-------WTILHDKLEKIAKmgtnIVLSKLP-IGDIATQFFADRNIFAAGRVEQADM-IRTSKAT---- 328
Cdd:PRK12851 244 GKPL--LIIAEdvegealATLVVNKLRGGLK----VAAVKAPgFGDRRKAMLEDIAILTGGTVISEDLgIKLENVTleql 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 329 GASIQNTVNGISTDVLGTCGRFEE-----KQIGN---------DRFNIFEDCPKTTTATIILRGGAQQFIEESER--SLN 392
Cdd:PRK12851 318 GRAKKVVVEKENTTIIDGAGSKTEiegrvAQIRAqieettsdyDREKLQERLAKLAGGVAVIRVGASTEVEVKEKkdRVD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 393 DAICVVRRTTKtHTIVGGGGAVEMELSKALREYSLSvVGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRrdhal 472
Cdd:PRK12851 398 DALHATRAAVE-EGIVPGGGVALLRAVKALDKLETA-NGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLR----- 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1624726457 473 skEGVNWFGVNCMNGDIVDTFEECIWEPAMVKKNALYAATEAACQVLSIDETVKHAAQAAP 533
Cdd:PRK12851 471 --EKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEP 529
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
39-519 |
1.88e-14 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 76.00 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 39 IKTTLGPRGMDKLI-HSGNDVTITNDGATVLKLLEVAHP----AAAVLVDIAKSQDDEVGDGTTSVTILAGELLTEAKQF 113
Cdd:PRK12849 26 VKVTLGPKGRNVVIdKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQALVQEGLKN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 114 IIDGISPQVIIKYFRLACERALKQIESMAVNIISKDDaekrslLAKCAETTlnskllSGHKTFFAKMVVDAVMLLDSDld 193
Cdd:PRK12849 106 VAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEE------IAQVATIS------ANGDEEIGELIAEAMEKVGKD-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 194 qemiGIKKVTGGSCIDSML--VKGVAFKktftyagaeqqpKKFLNPkiLLINIELELKAEKENAEILIKDpKQYQSIIDa 271
Cdd:PRK12849 172 ----GVITVEESKTLETELevTEGMQFD------------RGYLSP--YFVTDPERMEAVLEDPLILLTD-KKISSLQD- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 272 ewtILHdKLEKIAKMG---------------TNIVLSK----LPIGDIATQFFADRN--------IFAAGRVeqadmirT 324
Cdd:PRK12849 232 ---LLP-LLEKVAQSGkplliiaedvegealATLVVNKlrggLKVAAVKAPGFGDRRkamlediaILTGGTV-------I 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 325 SKATGASIQNtvngISTDVLGTCGRFE-------------------------EKQIGN-----DRFNIFEDCPKTTTATI 374
Cdd:PRK12849 301 SEDLGLKLEE----VTLDDLGRAKRVTitkdnttivdgagdkeaiearvaqiRRQIEEttsdyDREKLQERLAKLAGGVA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 375 ILRGGAQQFIEESER--SLNDAICVVRRTTKtHTIVGGGGAVEMELSKALREYsLSVVGKQQLIINAFARALEVIPKTLA 452
Cdd:PRK12849 377 VIKVGAATEVELKERkdRVEDALNATRAAVE-EGIVPGGGVALLRAAKALDEL-AGLNGDQAAGVEIVRRALEAPLRQIA 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624726457 453 QNAGFNATDVISKLRrdhalskEGVNWFGVNCMNGDIVDTFEECIWEPAMVKKNALYAATEAACQVL 519
Cdd:PRK12849 455 ENAGLDGSVVVAKVL-------ELEDGFGFNAATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLL 514
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
33-520 |
1.48e-11 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 66.67 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 33 QVVVECIKTTLGPRG----MDKLIHSGNdvtITNDGATVLKLLEVAHPA---AAVLVDIAKSQDDEV-GDGTTSVTILAG 104
Cdd:CHL00093 20 DILAEAVSVTLGPKGrnvvLEKKYGSPQ---IVNDGVTIAKEIELEDHIentGVALIRQAASKTNDVaGDGTTTATVLAY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 105 ELLTEAKQFIIDGISPQVIIKYFRLACERALKQIESMAVNIISKDDAEKRSLLAkcaettlnskllSGHKTFFAKMVVDA 184
Cdd:CHL00093 97 AIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASIS------------AGNDEEVGSMIADA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 185 VMLLDSDldqemiGIKKVTGGSCIDSML--VKGVAFKKTFT----YAGAEQQPKKFLNPKILLINIELELkAEKENAEIL 258
Cdd:CHL00093 165 IEKVGRE------GVISLEEGKSTVTELeiTEGMRFEKGFIspyfVTDTERMEVVQENPYILLTDKKITL-VQQDLLPIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 259 --IKDPKQYQSII------DAEWTILHDKLEKIakmgTNIVLSKLP-IGDIATQFFADRNIFAAGRVEQADmirtskaTG 329
Cdd:CHL00093 238 eqVTKTKRPLLIIaedvekEALATLVLNKLRGI----VNVVAVRAPgFGDRRKAMLEDIAILTGGQVITED-------AG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 330 ASIQNtvngISTDVLGTCGRFE------------------------EKQI-----GNDRFNIFEDCPKTTTATIILRGGA 380
Cdd:CHL00093 307 LSLET----IQLDLLGQARRIIvtkdsttiiadgneeqvkarceqlRKQIeiadsSYEKEKLQERLAKLSGGVAVIKVGA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 381 QQFIEESERS--LNDAICVVRRTTKtHTIVGGGGAVEMELSKALREYSLSVVGKQQLI-INAFARALEVIPKTLAQNAGF 457
Cdd:CHL00093 383 ATETEMKDKKlrLEDAINATKAAVE-EGIVPGGGATLVHLSENLKTWAKNNLKEDELIgALIVARAILAPLKRIAENAGK 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624726457 458 NATDVISKLrrdhalsKEGVNWFGVNCMNGDIVDTFEECIWEPAMVKKNALYAATEAACQVLS 520
Cdd:CHL00093 462 NGSVIIEKV-------QEQDFEIGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILT 517
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
42-535 |
1.30e-08 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 57.63 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 42 TLGPRGMDKLIHSG-NDVTITNDGATVLKLLEVAHPA---AAVLVDIAKSQ-DDEVGDGTTSVTILAGELLTEAKQFIID 116
Cdd:PLN03167 85 TLGPKGRNVVLESKyGSPKIVNDGVTVAKEVELEDPVeniGAKLVRQAAAKtNDLAGDGTTTSVVLAQGLIAEGVKVVAA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 117 GISPQVIIKYFRLACERALKQIESMAVNIiskDDAEkrslLAKCAETTlnskllSGHKTFFAKMVVDAVmlldsdldqEM 196
Cdd:PLN03167 165 GANPVQITRGIEKTAKALVKELKKMSKEV---EDSE----LADVAAVS------AGNNYEVGNMIAEAM---------SK 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 197 IGIKKVT----GGSCIDSM-LVKGVAFKKTFT----YAGAEQQPKKFLNPKILLIN---------IELELKAEKENAEIL 258
Cdd:PLN03167 223 VGRKGVVtleeGKSAENNLyVVEGMQFDRGYIspyfVTDSEKMSVEYDNCKLLLVDkkitnardlIGILEDAIRGGYPLL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 259 I--KDPKQyqsiiDAEWTILHDKLEKIAKmgtnIVLSKLP-IGDIATQFFADRNIFAAGRVEQADMIRTSKATGASIQNT 335
Cdd:PLN03167 303 IiaEDIEQ-----EALATLVVNKLRGSLK----IAALKAPgFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 336 VNGI-----STDVLGTCGRFEE-----KQIGN---------DRFNIFEDCPKTTTATIILRGGAQQFIEESERSL--NDA 394
Cdd:PLN03167 374 AAKVvltkdTTTIVGDGSTQEAvnkrvAQIKNlieaaeqdyEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLrvEDA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 395 ICVVRRTTKTHTIVGGGGAVeMELSKALREYSLSVVGKQQLI-INAFARALEVIPKTLAQNAGFNATDVISKLrrdhaLS 473
Cdd:PLN03167 454 LNATKAAVEEGIVVGGGCTL-LRLASKVDAIKDTLENDEQKVgADIVKRALSYPLKLIAKNAGVNGSVVSEKV-----LS 527
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1624726457 474 KEGVNwFGVNCMNGDIVDTFEECIWEPAMVKKNALYAATEAA-------CQVLSIDETvKHAAQAAPLD 535
Cdd:PLN03167 528 NDNPK-FGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAktfltsdCVVVEIKEP-EPVPAGNPMD 594
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
39-150 |
2.38e-08 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 56.67 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 39 IKTTLGPRG----MDKlihSGNDVTITNDGATVLKLLEVAHP----AAAVLVDIAKSQDDEVGDGTTSVTILAGELLTEA 110
Cdd:PRK00013 26 VKVTLGPKGrnvvLEK---SFGAPTITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLAQAIVREG 102
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1624726457 111 KQFIIDGISPQVIIKYFRLACERALKQIESMAVNIISKDD 150
Cdd:PRK00013 103 LKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEE 142
|
|
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
407-515 |
3.99e-06 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 49.35 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624726457 407 IVGGGGAVEMELSKALREYSLSVvGKQQLIINAFARALEVIPKTLAQNAGFNATDVISKLRrdhalSKEGVNwFGVNCMN 486
Cdd:PRK00013 410 IVPGGGVALLRAAPALEALKGLN-GDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVK-----NGKGKG-YGYNAAT 482
|
90 100 110
....*....|....*....|....*....|
gi 1624726457 487 GDIVDTFEECIWEPAMVKKNAL-YAATEAA 515
Cdd:PRK00013 483 GEYVDMIEAGIIDPTKVTRSALqNAASVAG 512
|
|
| |
