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Conserved domains on  [gi|100816407|ref|NP_078961|]
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Bardet-Biedl syndrome 10 protein [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cpn60_TCP1 super family cl28953
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 21-427 5.38e-19

TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.


The actual alignment was detected with superfamily member pfam00118:

Pssm-ID: 395068 [Multi-domain]  Cd Length: 489  Bit Score: 90.72  E-value: 5.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407   21 LEAIVSCCVGPEGRQVLCTKPTGEVLLSRNGGRLLEALHLEHPIARMIVDCVSSHLKKTGDGAKTFIIFLCHLLrglhai 100
Cdd:pfam00118   1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELL------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  101 tdrekdplmceniqthgrhwKNCSRWkfISQALLTfqTQILDGI-------MDQYLSRHFLSIFSSAKE--RTLCRSSLe 171
Cdd:pfam00118  75 --------------------EEAEKL--LAAGVHP--TTIIEGYekalekaLEILDSIISIPVEDVDREdlLKVARTSL- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  172 llleayfCGRVGRNNHKFISQLMCDyffkcmTCKSGIGVFELVDDHFVELnVGVTGLPVSDSRIIAGLVLQKDFSVY-RP 250
Cdd:pfam00118 130 -------SSKIISRESDFLAKLVVD------AVLAIPKNDGSFDLGNIGV-VKILGGSLEDSELVDGVVLDKGPLHPdMP 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  251 AD-GDMRMVIVTETIQPLFSTSGSEFILNSEAQFQTsqfwIMEKTKAIMKH----LHSQNVKLLISSVKQPDLVSYYAGV 325
Cdd:pfam00118 196 KRlENAKVLLLNCSLEYEKTETKATVVLSDAEQLER----FLKAEEEQILEivekIIDSGVNVVVCQKGIDDLALHFLAK 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  326 NGISVVECLSSEEVSLIRRIIGLSPFVPPQAFSQCEIPNTALVKFCKpliLRSKRYVhlgLISTCAFIPH-SIVLCGPVH 404
Cdd:pfam00118 272 NGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEK---IGDEKYT---FIEGCKSPKAaTILLRGATD 345

                         410       420
                  ....*....|....*....|...
gi 100816407  405 GLIEQHEDALHGALKMLRQLFKD 427
Cdd:pfam00118 346 HVLDEIERSIHDALCVVKNAIED 368
chaperonin_like super family cl02777
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
 597-644 6.53e-04

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.


The actual alignment was detected with superfamily member cd03342:

Pssm-ID: 351886 [Multi-domain]  Cd Length: 484  Bit Score: 43.02  E-value: 6.53e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 100816407 597 GCVLPVGGNFEILLHYYLLNYAKKCHQSEETMVsMIIANALLGIPKVL 644
Cdd:cd03342  363 KCVVPGAGAFEVALYAHLKEFKKSVKGKAKLGV-QAFADALLVIPKTL 409
chap_CCT_zeta super family cl28957
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
 597-705 9.08e-04

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.


The actual alignment was detected with superfamily member TIGR02347:

Pssm-ID: 274088 [Multi-domain]  Cd Length: 531  Bit Score: 42.41  E-value: 9.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  597 GCVLPVGGNFEILLHYYLLNYAKKCHQSEETMVSmIIANALLGIPKVLykSKTGKYSfPHTYIRAVHA------------ 664
Cdd:TIGR02347 406 KCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVE-AFANALLVIPKTL--AENSGFD-AQDTLVKLEDehdeggevvgvd 481

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 100816407  665 LQTNQPLVSSQTGL-ESVMGKYQLLTSVLQCLTKILTIDMVI 705
Cdd:TIGR02347 482 LNTGEPIDPEIKGIwDNYRVKKQLIQSATVIASQLLLVDEVM 523
 
Name Accession Description Interval E-value
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 21-427 5.38e-19

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: 90.72  E-value: 5.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407   21 LEAIVSCCVGPEGRQVLCTKPTGEVLLSRNGGRLLEALHLEHPIARMIVDCVSSHLKKTGDGAKTFIIFLCHLLrglhai 100
Cdd:pfam00118   1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELL------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  101 tdrekdplmceniqthgrhwKNCSRWkfISQALLTfqTQILDGI-------MDQYLSRHFLSIFSSAKE--RTLCRSSLe 171
Cdd:pfam00118  75 --------------------EEAEKL--LAAGVHP--TTIIEGYekalekaLEILDSIISIPVEDVDREdlLKVARTSL- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  172 llleayfCGRVGRNNHKFISQLMCDyffkcmTCKSGIGVFELVDDHFVELnVGVTGLPVSDSRIIAGLVLQKDFSVY-RP 250
Cdd:pfam00118 130 -------SSKIISRESDFLAKLVVD------AVLAIPKNDGSFDLGNIGV-VKILGGSLEDSELVDGVVLDKGPLHPdMP 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  251 AD-GDMRMVIVTETIQPLFSTSGSEFILNSEAQFQTsqfwIMEKTKAIMKH----LHSQNVKLLISSVKQPDLVSYYAGV 325
Cdd:pfam00118 196 KRlENAKVLLLNCSLEYEKTETKATVVLSDAEQLER----FLKAEEEQILEivekIIDSGVNVVVCQKGIDDLALHFLAK 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  326 NGISVVECLSSEEVSLIRRIIGLSPFVPPQAFSQCEIPNTALVKFCKpliLRSKRYVhlgLISTCAFIPH-SIVLCGPVH 404
Cdd:pfam00118 272 NGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEK---IGDEKYT---FIEGCKSPKAaTILLRGATD 345

                         410       420
                  ....*....|....*....|...
gi 100816407  405 GLIEQHEDALHGALKMLRQLFKD 427
Cdd:pfam00118 346 HVLDEIERSIHDALCVVKNAIED 368
chap_CCT_epsi TIGR02343
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
 12-100 1.63e-06

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: 51.34  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407   12 KAALQVAEVLEAIVSCCVGPEGRQVLCTKPTGEVLLSRNGGRLLEALHLEHPIARMIVDCVSSHLKKTGDGAKTFIIFLC 91
Cdd:TIGR02343  30 KSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVVVLAG 109

                          90
                  ....*....|....*..
gi 100816407   92 HLL--------RGLHAI 100
Cdd:TIGR02343 110 ALLeqaeelldKGIHPI 126
TCP1_epsilon cd03339
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
 11-100 2.49e-04

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: 44.21  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  11 VKAALQVAEVLEAIVSCCVGPEGRQVLCTKPTGEVLLSRNGGRLLEALHLEHPIARMIVDCVSSHLKKTGDGAKTFIIFL 90
Cdd:cd03339   25 HKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLA 104

                         90
                 ....*....|....*...
gi 100816407  91 CHLL--------RGLHAI 100
Cdd:cd03339  105 GALLeqaeklldRGIHPI 122
thermosome_beta NF041083
thermosome subunit beta;
13-95 2.80e-04

thermosome subunit beta;


Pssm-ID: 469010  Cd Length: 519  Bit Score: 44.17  E-value: 2.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  13 AALQVAEvleaIVSCCVGPEGRQVLCTKPTGEVLLSRNGGRLLEALHLEHPIARMIVDCVSSHLKKTGDGAKTFIIFLCH 92
Cdd:NF041083  25 AAKAVAE----AVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAVVLAGE 100


                 ...
gi 100816407  93 LLR 95
Cdd:NF041083 101 LLK 103
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
 597-644 6.53e-04

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: 43.02  E-value: 6.53e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 100816407 597 GCVLPVGGNFEILLHYYLLNYAKKCHQSEETMVsMIIANALLGIPKVL 644
Cdd:cd03342  363 KCVVPGAGAFEVALYAHLKEFKKSVKGKAKLGV-QAFADALLVIPKTL 409
chap_CCT_zeta TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
 597-705 9.08e-04

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: 42.41  E-value: 9.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  597 GCVLPVGGNFEILLHYYLLNYAKKCHQSEETMVSmIIANALLGIPKVLykSKTGKYSfPHTYIRAVHA------------ 664
Cdd:TIGR02347 406 KCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVE-AFANALLVIPKTL--AENSGFD-AQDTLVKLEDehdeggevvgvd 481

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 100816407  665 LQTNQPLVSSQTGL-ESVMGKYQLLTSVLQCLTKILTIDMVI 705
Cdd:TIGR02347 482 LNTGEPIDPEIKGIwDNYRVKKQLIQSATVIASQLLLVDEVM 523
 
Name Accession Description Interval E-value
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 21-427 5.38e-19

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: 90.72  E-value: 5.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407   21 LEAIVSCCVGPEGRQVLCTKPTGEVLLSRNGGRLLEALHLEHPIARMIVDCVSSHLKKTGDGAKTFIIFLCHLLrglhai 100
Cdd:pfam00118   1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELL------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  101 tdrekdplmceniqthgrhwKNCSRWkfISQALLTfqTQILDGI-------MDQYLSRHFLSIFSSAKE--RTLCRSSLe 171
Cdd:pfam00118  75 --------------------EEAEKL--LAAGVHP--TTIIEGYekalekaLEILDSIISIPVEDVDREdlLKVARTSL- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  172 llleayfCGRVGRNNHKFISQLMCDyffkcmTCKSGIGVFELVDDHFVELnVGVTGLPVSDSRIIAGLVLQKDFSVY-RP 250
Cdd:pfam00118 130 -------SSKIISRESDFLAKLVVD------AVLAIPKNDGSFDLGNIGV-VKILGGSLEDSELVDGVVLDKGPLHPdMP 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  251 AD-GDMRMVIVTETIQPLFSTSGSEFILNSEAQFQTsqfwIMEKTKAIMKH----LHSQNVKLLISSVKQPDLVSYYAGV 325
Cdd:pfam00118 196 KRlENAKVLLLNCSLEYEKTETKATVVLSDAEQLER----FLKAEEEQILEivekIIDSGVNVVVCQKGIDDLALHFLAK 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  326 NGISVVECLSSEEVSLIRRIIGLSPFVPPQAFSQCEIPNTALVKFCKpliLRSKRYVhlgLISTCAFIPH-SIVLCGPVH 404
Cdd:pfam00118 272 NGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGTAGKVEEEK---IGDEKYT---FIEGCKSPKAaTILLRGATD 345

                         410       420
                  ....*....|....*....|...
gi 100816407  405 GLIEQHEDALHGALKMLRQLFKD 427
Cdd:pfam00118 346 HVLDEIERSIHDALCVVKNAIED 368
chap_CCT_epsi TIGR02343
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
 12-100 1.63e-06

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: 51.34  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407   12 KAALQVAEVLEAIVSCCVGPEGRQVLCTKPTGEVLLSRNGGRLLEALHLEHPIARMIVDCVSSHLKKTGDGAKTFIIFLC 91
Cdd:TIGR02343  30 KSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVVVLAG 109

                          90
                  ....*....|....*..
gi 100816407   92 HLL--------RGLHAI 100
Cdd:TIGR02343 110 ALLeqaeelldKGIHPI 126
chap_CCT_zeta TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
 2-95 4.91e-05

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: 46.65  E-value: 4.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407    2 LSSMAAAGSVKAALQV----AEVLEAIVSCCVGPEGRQVLCTKPTGEVLLSRNGGRLLEALHLEHPIARMIVDCVSSHLK 77
Cdd:TIGR02347   5 LNPKAESLRRDAALMMninaARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDD 84

                          90
                  ....*....|....*...
gi 100816407   78 KTGDGAKTFIIFLCHLLR 95
Cdd:TIGR02347  85 ITGDGTTSTVLLIGELLK 102
chap_CCT_alpha TIGR02340
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
 11-95 5.15e-05

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: 46.64  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407   11 VKAALQVAEvleaIVSCCVGPEGRQVLCTKPTGEVLLSRNGGRLLEALHLEHPIARMIVDCVSSHLKKTGDGAKTFIIFL 90
Cdd:TIGR02340  18 VTAAMAIAN----IVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVIIA 93


                  ....*
gi 100816407   91 CHLLR 95
Cdd:TIGR02340  94 AELLK 98
TCP1_epsilon cd03339
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
 11-100 2.49e-04

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: 44.21  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  11 VKAALQVAEVLEAIVSCCVGPEGRQVLCTKPTGEVLLSRNGGRLLEALHLEHPIARMIVDCVSSHLKKTGDGAKTFIIFL 90
Cdd:cd03339   25 HKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLA 104

                         90
                 ....*....|....*...
gi 100816407  91 CHLL--------RGLHAI 100
Cdd:cd03339  105 GALLeqaeklldRGIHPI 122
TCP1_alpha cd03335
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ...
 11-95 2.66e-04

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: 44.20  E-value: 2.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  11 VKAALQVAEvleaIVSCCVGPEGRQVLCTKPTGEVLLSRNGGRLLEALHLEHPIARMIVDCVSSHLKKTGDGAKTFIIFL 90
Cdd:cd03335   14 VTAAMAIAN----IVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIA 89


                 ....*
gi 100816407  91 CHLLR 95
Cdd:cd03335   90 AELLK 94
thermosome_beta NF041083
thermosome subunit beta;
13-95 2.80e-04

thermosome subunit beta;


Pssm-ID: 469010  Cd Length: 519  Bit Score: 44.17  E-value: 2.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  13 AALQVAEvleaIVSCCVGPEGRQVLCTKPTGEVLLSRNGGRLLEALHLEHPIARMIVDCVSSHLKKTGDGAKTFIIFLCH 92
Cdd:NF041083  25 AAKAVAE----AVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTTAVVLAGE 100


                 ...
gi 100816407  93 LLR 95
Cdd:NF041083 101 LLK 103
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
 13-95 6.32e-04

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: 43.02  E-value: 6.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  13 AALQVAEvleaIVSCCVGPEGRQVLCTKPTGEVLLSRNGGRLLEALHLEHPIARMIVDCVSSHLKKTGDGAKTFIIFLCH 92
Cdd:cd03343   23 AAKAVAE----AVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLAGE 98


                 ...
gi 100816407  93 LLR 95
Cdd:cd03343   99 LLE 101
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
 597-644 6.53e-04

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: 43.02  E-value: 6.53e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 100816407 597 GCVLPVGGNFEILLHYYLLNYAKKCHQSEETMVsMIIANALLGIPKVL 644
Cdd:cd03342  363 KCVVPGAGAFEVALYAHLKEFKKSVKGKAKLGV-QAFADALLVIPKTL 409
TCP1_delta cd03338
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
 2-98 7.31e-04

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: 42.66  E-value: 7.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407   2 LSSMAAAGSVKAAlqvaevleaiVSCCVGPEGRQVLCTKPTGEVLLSRNGGRLLEALHLEHPIARMIVDCVSSHLKKTGD 81
Cdd:cd03338   11 LSNIQAAKAVADA----------IRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGD 80

                         90       100
                 ....*....|....*....|....*
gi 100816407  82 GAKTFIIFLCHLL--------RGLH 98
Cdd:cd03338   81 GTTSVVVLAGALLsacesllkKGIH 105
chap_CCT_zeta TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
 597-705 9.08e-04

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: 42.41  E-value: 9.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  597 GCVLPVGGNFEILLHYYLLNYAKKCHQSEETMVSmIIANALLGIPKVLykSKTGKYSfPHTYIRAVHA------------ 664
Cdd:TIGR02347 406 KCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVE-AFANALLVIPKTL--AENSGFD-AQDTLVKLEDehdeggevvgvd 481

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 100816407  665 LQTNQPLVSSQTGL-ESVMGKYQLLTSVLQCLTKILTIDMVI 705
Cdd:TIGR02347 482 LNTGEPIDPEIKGIwDNYRVKKQLIQSATVIASQLLLVDEVM 523
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
 13-98 9.38e-04

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: 42.25  E-value: 9.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407  13 AALQV----AEVLEAIVSCCVGPEGRQVLCTKPTGEVLLSRNGGRLLEALHLEHPIARMIVDCVSSHLKKTGDGAKTFII 88
Cdd:cd03342   12 QALAVnisaAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVL 91

                         90
                 ....*....|....*...
gi 100816407  89 FLCHLLR--------GLH 98
Cdd:cd03342   92 LIGELLKqaeryiqeGVH 109
chap_CCT_eta TIGR02345
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ...
 11-246 1.25e-03

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: 42.05  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407   11 VKAALQVAEVLEAIVsccvGPEGRQVLCTKPTGEVLLSRNGGRLLEALHLEHPIARMIVDCVSSHLKKTGDGAKTFIIFL 90
Cdd:TIGR02345  24 INACVAIAEALKTTL----GPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407   91 CHLLrglhaitdREKDPLMCENIQTHgrhwkncsrwkFISQALLTFQTQILDGIMDqylsrhflsifsSAKERTLCRSSL 170
Cdd:TIGR02345 100 GELL--------KEAKPFIEEGVHPQ-----------LIIRCYREALSLAVEKIKE------------IAVTIDEEKGEQ 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 100816407  171 ELLLEAyfCGRVGRNNhKFISQlmCDYFFKCMTCKSgigVFELVDDHFVELNVG---VTGLPVSDSRIIAGLVLQKDFS 246
Cdd:TIGR02345 149 RELLEK--CAATALSS-KLISH--NKEFFSKMIVDA---VLSLDRDDLDLKLIGikkVQGGALEDSQLVNGVAFKKTFS 219
chap_CCT_gamma TIGR02344
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
 6-107 4.62e-03

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: 40.11  E-value: 4.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816407    6 AAAGSVKAALQVAEvleaIVSCCVGPEGRQVLCTKPTGEVLLSRNGGRLLEALHLEHPIARMIVDCVSSHLKKTGDGAKT 85
Cdd:TIGR02344  17 AQLSNIQAAKAVAD----IIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTS 92

                          90       100
                  ....*....|....*....|..
gi 100816407   86 FIIFLCHLLRGLHAITDREKDP 107
Cdd:TIGR02344  93 VIILAGEMLSVAEPFLEQNIHP 114
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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