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Conserved domains on  [gi|254553416|ref|NP_082190|]
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BBSome complex assembly protein BBS10 [Mus musculus]

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 ...
 13-424 1.18e-14

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: 77.24  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416   13 VAEVLESianrCVGPEGGQVLCTKPTGEVLLSRDGGCLLEALHLEHPLARMIVACVSSHLKKTGDGAKTFIIFLCHLLR- 91
Cdd:pfam00118   1 LADIVRT----SLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEe 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416   92 -------GLHAigekgkdSFTSENIQsherhwknccqwKSISQALQTFqtQTLGCIVDRSLSRHYLsvfssstegRKLCR 164
Cdd:pfam00118  77 aekllaaGVHP-------TTIIEGYE------------KALEKALEIL--DSIISIPVEDVDREDL---------LKVAR 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416  165 HSLellleayfCGRVGRNNHRFISQLMCDyvfkcmACESGVEVFELLDhcfaELNVGVTGLP---VSDSRIIDGLVLPRD 241
Cdd:pfam00118 127 TSL--------SSKIISRESDFLAKLVVD------AVLAIPKNDGSFD----LGNIGVVKILggsLEDSELVDGVVLDKG 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416  242 FSMYCPAD--GDIRMVIVTEILQPQFSSAGSEFVLNSETQFQAsqcwitdrtktVMNHLRGQnVKLLLTSVKQ--PDLVI 317
Cdd:pfam00118 189 PLHPDMPKrlENAKVLLLNCSLEYEKTETKATVVLSDAEQLER-----------FLKAEEEQ-ILEIVEKIIDsgVNVVV 256

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416  318 -----------YCARlNSISVVECLSAEEV---------SLVQRITGLSPCVLPEVASQCEISDStlvkfckplilrSKR 377
Cdd:pfam00118 257 cqkgiddlalhFLAK-NGIMALRRVKKRDLerlakatgaRAVSSLDDLTPDDLGTAGKVEEEKIG------------DEK 323

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 254553416  378 YVhlgLISTCAFIPH-SMVLCGPVLGLVEQHERAFHGAFKMLRQLFTD 424
Cdd:pfam00118 324 YT---FIEGCKSPKAaTILLRGATDHVLDEIERSIHDALCVVKNAIED 368
chap_CCT_alpha super family cl28958
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
 562-703 3.22e-04

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.


The actual alignment was detected with superfamily member TIGR02340:

Pssm-ID: 274081 [Multi-domain]  Cd Length: 536  Bit Score: 43.94  E-value: 3.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416  562 YTLPVMRKSLDTCTCqgYCSSTVPAGCVLPVGGSFEILMSYYLLSYAkQCRQSDETVISMLIADALLGIPKILyKPKKGK 641
Cdd:TIGR02340 379 FMLDEMERSLHDALC--VVKRTLESNSVVPGGGAVEAALSIYLENFA-TTLGSREQLAIAEFARALLIIPKTL-AVNAAK 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416  642 DSFPHIY-MRSLHALQASQP-----------MVSG------QSG-FESVAGKYQLLTSVLQCLMKILTIDLIINIKRQPQ 702
Cdd:TIGR02340 455 DSTELVAkLRAYHAAAQLKPekkhlkwygldLVNGkirdnkEAGvLEPTVSKVKSLKFATEAAITILRIDDLIKLNPEQS 534


                  .
gi 254553416  703 K 703
Cdd:TIGR02340 535 K 535
 
Name Accession Description Interval E-value
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 13-424 1.18e-14

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: 77.24  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416   13 VAEVLESianrCVGPEGGQVLCTKPTGEVLLSRDGGCLLEALHLEHPLARMIVACVSSHLKKTGDGAKTFIIFLCHLLR- 91
Cdd:pfam00118   1 LADIVRT----SLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEe 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416   92 -------GLHAigekgkdSFTSENIQsherhwknccqwKSISQALQTFqtQTLGCIVDRSLSRHYLsvfssstegRKLCR 164
Cdd:pfam00118  77 aekllaaGVHP-------TTIIEGYE------------KALEKALEIL--DSIISIPVEDVDREDL---------LKVAR 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416  165 HSLellleayfCGRVGRNNHRFISQLMCDyvfkcmACESGVEVFELLDhcfaELNVGVTGLP---VSDSRIIDGLVLPRD 241
Cdd:pfam00118 127 TSL--------SSKIISRESDFLAKLVVD------AVLAIPKNDGSFD----LGNIGVVKILggsLEDSELVDGVVLDKG 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416  242 FSMYCPAD--GDIRMVIVTEILQPQFSSAGSEFVLNSETQFQAsqcwitdrtktVMNHLRGQnVKLLLTSVKQ--PDLVI 317
Cdd:pfam00118 189 PLHPDMPKrlENAKVLLLNCSLEYEKTETKATVVLSDAEQLER-----------FLKAEEEQ-ILEIVEKIIDsgVNVVV 256

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416  318 -----------YCARlNSISVVECLSAEEV---------SLVQRITGLSPCVLPEVASQCEISDStlvkfckplilrSKR 377
Cdd:pfam00118 257 cqkgiddlalhFLAK-NGIMALRRVKKRDLerlakatgaRAVSSLDDLTPDDLGTAGKVEEEKIG------------DEK 323

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 254553416  378 YVhlgLISTCAFIPH-SMVLCGPVLGLVEQHERAFHGAFKMLRQLFTD 424
Cdd:pfam00118 324 YT---FIEGCKSPKAaTILLRGATDHVLDEIERSIHDALCVVKNAIED 368
chap_CCT_zeta TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
 8-91 8.03e-06

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: 48.96  E-value: 8.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416    8 TAALRV----AEVLESIANRCVGPEGGQVLCTKPTGEVLLSRDGGCLLEALHLEHPLARMIVACVSSHLKKTGDGAKTFI 83
Cdd:TIGR02347  15 DAALMMninaARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTV 94


                  ....*...
gi 254553416   84 IFLCHLLR 91
Cdd:TIGR02347  95 LLIGELLK 102
thermosome_beta NF041083
thermosome subunit beta;
2-91 6.00e-05

thermosome subunit beta;


Pssm-ID: 469010  Cd Length: 519  Bit Score: 46.10  E-value: 6.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416   2 ASQGSVTAALRVAEVLESianrCVGPEGGQVLCTKPTGEVLLSRDGGCLLEALHLEHPLARMIVACVSSHLKKTGDGAKT 81
Cdd:NF041083  18 AQRNNIMAAKAVAEAVRT----TLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTT 93

                         90
                 ....*....|
gi 254553416  82 FIIFLCHLLR 91
Cdd:NF041083  94 AVVLAGELLK 103
TCP1_alpha cd03335
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ...
 7-91 1.08e-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: 45.35  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416   7 VTAALRVAEVLESianrCVGPEGGQVLCTKPTGEVLLSRDGGCLLEALHLEHPLARMIVACVSSHLKKTGDGAKTFIIFL 86
Cdd:cd03335   14 VTAAMAIANIVKS----SLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIA 89


                 ....*
gi 254553416  87 CHLLR 91
Cdd:cd03335   90 AELLK 94
chap_CCT_alpha TIGR02340
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
 562-703 3.22e-04

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: 43.94  E-value: 3.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416  562 YTLPVMRKSLDTCTCqgYCSSTVPAGCVLPVGGSFEILMSYYLLSYAkQCRQSDETVISMLIADALLGIPKILyKPKKGK 641
Cdd:TIGR02340 379 FMLDEMERSLHDALC--VVKRTLESNSVVPGGGAVEAALSIYLENFA-TTLGSREQLAIAEFARALLIIPKTL-AVNAAK 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416  642 DSFPHIY-MRSLHALQASQP-----------MVSG------QSG-FESVAGKYQLLTSVLQCLMKILTIDLIINIKRQPQ 702
Cdd:TIGR02340 455 DSTELVAkLRAYHAAAQLKPekkhlkwygldLVNGkirdnkEAGvLEPTVSKVKSLKFATEAAITILRIDDLIKLNPEQS 534


                  .
gi 254553416  703 K 703
Cdd:TIGR02340 535 K 535
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
 587-634 3.66e-03

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: 40.32  E-value: 3.66e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 254553416 587 GCVLPVGGSFEILMSYYLLSYAKQCrqSDETVISMLI-ADALLGIPKIL 634
Cdd:cd03342  363 KCVVPGAGAFEVALYAHLKEFKKSV--KGKAKLGVQAfADALLVIPKTL 409
 
Name Accession Description Interval E-value
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 13-424 1.18e-14

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: 77.24  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416   13 VAEVLESianrCVGPEGGQVLCTKPTGEVLLSRDGGCLLEALHLEHPLARMIVACVSSHLKKTGDGAKTFIIFLCHLLR- 91
Cdd:pfam00118   1 LADIVRT----SLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEe 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416   92 -------GLHAigekgkdSFTSENIQsherhwknccqwKSISQALQTFqtQTLGCIVDRSLSRHYLsvfssstegRKLCR 164
Cdd:pfam00118  77 aekllaaGVHP-------TTIIEGYE------------KALEKALEIL--DSIISIPVEDVDREDL---------LKVAR 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416  165 HSLellleayfCGRVGRNNHRFISQLMCDyvfkcmACESGVEVFELLDhcfaELNVGVTGLP---VSDSRIIDGLVLPRD 241
Cdd:pfam00118 127 TSL--------SSKIISRESDFLAKLVVD------AVLAIPKNDGSFD----LGNIGVVKILggsLEDSELVDGVVLDKG 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416  242 FSMYCPAD--GDIRMVIVTEILQPQFSSAGSEFVLNSETQFQAsqcwitdrtktVMNHLRGQnVKLLLTSVKQ--PDLVI 317
Cdd:pfam00118 189 PLHPDMPKrlENAKVLLLNCSLEYEKTETKATVVLSDAEQLER-----------FLKAEEEQ-ILEIVEKIIDsgVNVVV 256

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416  318 -----------YCARlNSISVVECLSAEEV---------SLVQRITGLSPCVLPEVASQCEISDStlvkfckplilrSKR 377
Cdd:pfam00118 257 cqkgiddlalhFLAK-NGIMALRRVKKRDLerlakatgaRAVSSLDDLTPDDLGTAGKVEEEKIG------------DEK 323

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 254553416  378 YVhlgLISTCAFIPH-SMVLCGPVLGLVEQHERAFHGAFKMLRQLFTD 424
Cdd:pfam00118 324 YT---FIEGCKSPKAaTILLRGATDHVLDEIERSIHDALCVVKNAIED 368
chap_CCT_zeta TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
 8-91 8.03e-06

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: 48.96  E-value: 8.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416    8 TAALRV----AEVLESIANRCVGPEGGQVLCTKPTGEVLLSRDGGCLLEALHLEHPLARMIVACVSSHLKKTGDGAKTFI 83
Cdd:TIGR02347  15 DAALMMninaARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTV 94


                  ....*...
gi 254553416   84 IFLCHLLR 91
Cdd:TIGR02347  95 LLIGELLK 102
chap_CCT_epsi TIGR02343
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
 2-243 9.51e-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: 48.65  E-value: 9.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416    2 ASQGSVTAALRVAEVLESianrCVGPEGGQVLCTKPTGEVLLSRDGGCLLEALHLEHPLARMIVACVSSHLKKTGDGAKT 81
Cdd:TIGR02343  28 AKKSNIAAAKSVASILRT----SLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416   82 FIIFLCHLL--------RGLHAIgeKGKDSFtSENIQSHERHWKNCCQWKSISQALQTFQTQTlgcivdrslsrhylsvf 153
Cdd:TIGR02343 104 VVVLAGALLeqaeelldKGIHPI--KIADGF-EEAARIAVEHLEEISDEISADNNNREPLIQA----------------- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416  154 ssstegrklCRHSLEllleayfcGRVGRNNHRFISQLMCDYVFKCMACESGVEVFELldhcfaeLNV-GVTGLPVSDSRI 232
Cdd:TIGR02343 164 ---------AKTSLG--------SKIVSKCHRRFAEIAVDAVLNVADMERRDVDFDL-------IKVeGKVGGSLEDTKL 219

                         250
                  ....*....|.
gi 254553416  233 IDGLVLPRDFS 243
Cdd:TIGR02343 220 IKGIIIDKDFS 230
chap_CCT_alpha TIGR02340
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
 7-91 3.41e-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: 47.02  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416    7 VTAALRVAEVLESianrCVGPEGGQVLCTKPTGEVLLSRDGGCLLEALHLEHPLARMIVACVSSHLKKTGDGAKTFIIFL 86
Cdd:TIGR02340  18 VTAAMAIANIVKT----SLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVIIA 93


                  ....*
gi 254553416   87 CHLLR 91
Cdd:TIGR02340  94 AELLK 98
thermosome_beta NF041083
thermosome subunit beta;
2-91 6.00e-05

thermosome subunit beta;


Pssm-ID: 469010  Cd Length: 519  Bit Score: 46.10  E-value: 6.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416   2 ASQGSVTAALRVAEVLESianrCVGPEGGQVLCTKPTGEVLLSRDGGCLLEALHLEHPLARMIVACVSSHLKKTGDGAKT 81
Cdd:NF041083  18 AQRNNIMAAKAVAEAVRT----TLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAKTQDDEVGDGTTT 93

                         90
                 ....*....|
gi 254553416  82 FIIFLCHLLR 91
Cdd:NF041083  94 AVVLAGELLK 103
chap_CCT_gamma TIGR02344
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
 2-84 7.87e-05

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: 45.88  E-value: 7.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416    2 ASQGSVTAALRVAEVLESianrCVGPEGGQVLCTKPTGEVLLSRDGGCLLEALHLEHPLARMIVACVSSHLKKTGDGAKT 81
Cdd:TIGR02344  17 AQLSNIQAAKAVADIIRT----CLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTS 92


                  ...
gi 254553416   82 FII 84
Cdd:TIGR02344  93 VII 95
TCP1_alpha cd03335
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ...
 7-91 1.08e-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: 45.35  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416   7 VTAALRVAEVLESianrCVGPEGGQVLCTKPTGEVLLSRDGGCLLEALHLEHPLARMIVACVSSHLKKTGDGAKTFIIFL 86
Cdd:cd03335   14 VTAAMAIANIVKS----SLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDGTTSVVIIA 89


                 ....*
gi 254553416  87 CHLLR 91
Cdd:cd03335   90 AELLK 94
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
 7-91 3.06e-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: 43.79  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416   7 VTAALRVAEVLESianrCVGPEGGQVLCTKPTGEVLLSRDGGCLLEALHLEHPLARMIVACVSSHLKKTGDGAKTFIIFL 86
Cdd:cd03343   21 IAAAKAVAEAVRT----TLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVLA 96


                 ....*
gi 254553416  87 CHLLR 91
Cdd:cd03343   97 GELLE 101
chap_CCT_alpha TIGR02340
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
 562-703 3.22e-04

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: 43.94  E-value: 3.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416  562 YTLPVMRKSLDTCTCqgYCSSTVPAGCVLPVGGSFEILMSYYLLSYAkQCRQSDETVISMLIADALLGIPKILyKPKKGK 641
Cdd:TIGR02340 379 FMLDEMERSLHDALC--VVKRTLESNSVVPGGGAVEAALSIYLENFA-TTLGSREQLAIAEFARALLIIPKTL-AVNAAK 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416  642 DSFPHIY-MRSLHALQASQP-----------MVSG------QSG-FESVAGKYQLLTSVLQCLMKILTIDLIINIKRQPQ 702
Cdd:TIGR02340 455 DSTELVAkLRAYHAAAQLKPekkhlkwygldLVNGkirdnkEAGvLEPTVSKVKSLKFATEAAITILRIDDLIKLNPEQS 534


                  .
gi 254553416  703 K 703
Cdd:TIGR02340 535 K 535
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
 8-94 4.66e-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: 43.40  E-value: 4.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416   8 TAALRV----AEVLESIANRCVGPEGGQVLCTKPTGEVLLSRDGGCLLEALHLEHPLARMIVACVSSHLKKTGDGAKTFI 83
Cdd:cd03342   11 GQALAVnisaAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNV 90

                         90
                 ....*....|....*....
gi 254553416  84 IFLCHLLR--------GLH 94
Cdd:cd03342   91 LLIGELLKqaeryiqeGVH 109
chap_CCT_zeta TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
 580-703 5.80e-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: 43.18  E-value: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416  580 CSSTVPAGCVLPVGGSFEILMSYYLLSYAKQCRQSDETVISMLiADALLGIPKILYKpKKGKDSFPHIYMRSLHALQASQ 659
Cdd:TIGR02347 399 VKNAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAF-ANALLVIPKTLAE-NSGFDAQDTLVKLEDEHDEGGE 476

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 254553416  660 P----MVSGQSGFESVAG-------KYQLLTSVLQCLMKILTIDLIINIKRQPQK 703
Cdd:TIGR02347 477 VvgvdLNTGEPIDPEIKGiwdnyrvKKQLIQSATVIASQLLLVDEVMRAGRSMLK 531
chap_CCT_eta TIGR02345
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ...
 2-103 9.91e-04

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: 42.44  E-value: 9.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416    2 ASQG------SVTAALRVAEVLESIanrcVGPEGGQVLCTKPTGEVLLSRDGGCLLEALHLEHPLARMIVACVSSHLKKT 75
Cdd:TIGR02345  13 TSQGkgqlisNINACVAIAEALKTT----LGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEV 88

                          90       100
                  ....*....|....*....|....*...
gi 254553416   76 GDGAKTFIIFLCHLLRGLHAIGEKGKDS 103
Cdd:TIGR02345  89 GDGTTSVTILAGELLKEAKPFIEEGVHP 116
TCP1_epsilon cd03339
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
 2-96 1.02e-03

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: 42.29  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416   2 ASQGSVTAALRVAEVLESianrCVGPEGGQVLCTKPTGEVLLSRDGGCLLEALHLEHPLARMIVACVSSHLKKTGDGAKT 81
Cdd:cd03339   24 AHKSHILAAKSVANILRT----SLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTG 99

                         90       100
                 ....*....|....*....|...
gi 254553416  82 FIIFLCHLL--------RGLHAI 96
Cdd:cd03339  100 VVVLAGALLeqaeklldRGIHPI 122
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
 587-634 3.66e-03

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: 40.32  E-value: 3.66e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 254553416 587 GCVLPVGGSFEILMSYYLLSYAKQCrqSDETVISMLI-ADALLGIPKIL 634
Cdd:cd03342  363 KCVVPGAGAFEVALYAHLKEFKKSV--KGKAKLGVQAfADALLVIPKTL 409
TCP1_alpha cd03335
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ...
 562-660 6.68e-03

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: 39.57  E-value: 6.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416 562 YTLPVMRKSLDTCTCqgYCSSTVPAGCVLPVGGSFEILMSYYLLSYAKQCrQSDETVISMLIADALLGIPKILyKPKKGK 641
Cdd:cd03335  375 FMLDEMERSLHDALC--VVKRTLESNSVVPGGGAVETALSIYLENFATTL-GSREQLAIAEFAEALLVIPKTL-AVNAAK 450

                         90       100
                 ....*....|....*....|
gi 254553416 642 DSFPHI-YMRSLHALQASQP 660
Cdd:cd03335  451 DATELVaKLRAYHAAAQVKP 470
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
 2-91 7.11e-03

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: 39.58  E-value: 7.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416   2 ASQG------SVTAALRVAEVLESIanrcVGPEGGQVLCTKPTGEVLLSRDGGCLLEALHLEHPLARMIVACVSSHLKKT 75
Cdd:cd03340   11 TSQGkgqlisNINACQAIADAVRTT----LGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEV 86

                         90
                 ....*....|....*.
gi 254553416  76 GDGAKTFIIFLCHLLR 91
Cdd:cd03340   87 GDGTTSVVVLAGEFLK 102
TCP1_gamma cd03337
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ...
 1-84 8.19e-03

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: 39.20  E-value: 8.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553416   1 MASQGSVTAALRVAEVLESianrCVGPEGGQVLCTKPTGEVLLSRDGGCLLEALHLEHPLARMIVACVSSHLKKTGDGAK 80
Cdd:cd03337   16 KAQLGNIQAAKTVADVIRT----CLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTT 91


                 ....
gi 254553416  81 TFII 84
Cdd:cd03337   92 SVII 95
 
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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