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Conserved domains on  [gi|1238882469|ref|XP_022254114|]
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Bardet-Biedl syndrome 10 protein-like isoform X1 [Limulus polyphemus]

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 ...
16-402 3.35e-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: 91.11  E-value: 3.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469  16 IGSLVEKSYGPYGRSSLCVSAVGQIEITSSGISILETARVNHPVATVITRAVKNHHELVGDGTKTFILLLKAIFNELSKY 95
Cdd:pfam00118   1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469  96 ItessyipqKQG--TMEIRTKLRLELSnllyfmlpeyfgqlRANKMIQNIFFHENNLPLVKScVQNLLKTFLTGKfgqlV 173
Cdd:pfam00118  81 L--------AAGvhPTTIIEGYEKALE--------------KALEILDSIISIPVEDVDRED-LLKVARTSLSSK----I 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469 174 THQLVELCYNLIFFSVSDISKFNEVVqylikNFHllccRINVLPIQL-----SRIVEGFVLTRDFTVPwkDYTSKEEEFN 248
Cdd:pfam00118 134 ISRESDFLAKLVVDAVLAIPKNDGSF-----DLG----NIGVVKILGgsledSELVDGVVLDKGPLHP--DMPKRLENAK 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469 249 FIVILSSQDNQSICNGAILKITQPQDIEMFLLSSSSFYKSAMKAIQQHQIQLILSCNSVSESFKTLCYEEGIAVIAGIPR 328
Cdd:pfam00118 203 VLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKK 282
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238882469 329 EELLHLVSLCGIQPIICLqETLNASKIGKAQFARPITLEAKWYIQI-GIKLSNLDTLLvphylvLCGPTEGICKQ 402
Cdd:pfam00118 283 RDLERLAKATGARAVSSL-DDLTPDDLGTAGKVEEEKIGDEKYTFIeGCKSPKAATIL------LRGATDHVLDE 350
 
Name Accession Description Interval E-value
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
16-402 3.35e-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: 91.11  E-value: 3.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469  16 IGSLVEKSYGPYGRSSLCVSAVGQIEITSSGISILETARVNHPVATVITRAVKNHHELVGDGTKTFILLLKAIFNELSKY 95
Cdd:pfam00118   1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469  96 ItessyipqKQG--TMEIRTKLRLELSnllyfmlpeyfgqlRANKMIQNIFFHENNLPLVKScVQNLLKTFLTGKfgqlV 173
Cdd:pfam00118  81 L--------AAGvhPTTIIEGYEKALE--------------KALEILDSIISIPVEDVDRED-LLKVARTSLSSK----I 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469 174 THQLVELCYNLIFFSVSDISKFNEVVqylikNFHllccRINVLPIQL-----SRIVEGFVLTRDFTVPwkDYTSKEEEFN 248
Cdd:pfam00118 134 ISRESDFLAKLVVDAVLAIPKNDGSF-----DLG----NIGVVKILGgsledSELVDGVVLDKGPLHP--DMPKRLENAK 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469 249 FIVILSSQDNQSICNGAILKITQPQDIEMFLLSSSSFYKSAMKAIQQHQIQLILSCNSVSESFKTLCYEEGIAVIAGIPR 328
Cdd:pfam00118 203 VLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKK 282
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238882469 329 EELLHLVSLCGIQPIICLqETLNASKIGKAQFARPITLEAKWYIQI-GIKLSNLDTLLvphylvLCGPTEGICKQ 402
Cdd:pfam00118 283 RDLERLAKATGARAVSSL-DDLTPDDLGTAGKVEEEKIGDEKYTFIeGCKSPKAATIL------LRGATDHVLDE 350
chap_CCT_theta TIGR02346
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
23-346 7.95e-08

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: 55.49  E-value: 7.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469  23 SYGPYGRSSLCVSAVGQIEITSSGISILETARVNHPVATVITRAVKNHHELVGDGTKTFILLLKAIFNELSKYITESSYI 102
Cdd:TIGR02346  37 SLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGELLNKAEELIRMGLHP 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469 103 PQ-KQGTMEIRTKLRLELSNLLYFMLPEYFGQLRANKMIqniffhennlplvKSCVqnLLKTFLTGKF-GQLVTHQLVEL 180
Cdd:TIGR02346 117 SEiIKGYEMALKKAMEILEELVVWEVKDLRDKDELIKAL-------------KASI--SSKQYGNEDFlAQLVAQACSTV 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469 181 CynliffsVSDISKFNevvqylIKNFHLlcCRINVLPIQLSRIVEGFVLTRDftvPWKDYTSKEEEfNFIVILSSQDNQS 260
Cdd:TIGR02346 182 L-------PKNPQNFN------VDNIRV--CKILGGSLSNSEVLKGMVFNRE---AEGSVKSVKNA-KVAVFSCPLDTAT 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469 261 I-CNGAILkITQPQDIEMFLLSSSSFYKSAMKAIQQHQIQLILSCNSVSESFKTLCYEEGIAVIAGIPREELLHLVSLCG 339
Cdd:TIGR02346 243 TeTKGTVL-IHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVG 321

                  ....*..
gi 1238882469 340 IQPIICL 346
Cdd:TIGR02346 322 ATPLPRL 328
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
25-98 8.90e-08

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: 54.96  E-value: 8.90e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238882469  25 GPYGRSSLCVSAVGQIEITSSGISILETARVNHPVATVITRAVKNHHELVGDGTKTFILLLKAIFNELSKYITE 98
Cdd:cd03342    33 GPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGELLKQAERYIQE 106
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
16-104 3.11e-03

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 40.78  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469  16 IGSLVEKSYGPYGRSSLCVSA-----VGQIEITSSGISILETARVNHPVATVITRAVKNHHELVGDGTKTFILLLKAIFN 90
Cdd:PTZ00212   34 VADLVKTTLGPKGMDKILQPMsegprSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGDGTTSVVVLAGELLR 113
                          90
                  ....*....|....
gi 1238882469  91 ELSKYITESSYiPQ 104
Cdd:PTZ00212  114 EAEKLLDQKIH-PQ 126
 
Name Accession Description Interval E-value
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
16-402 3.35e-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: 91.11  E-value: 3.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469  16 IGSLVEKSYGPYGRSSLCVSAVGQIEITSSGISILETARVNHPVATVITRAVKNHHELVGDGTKTFILLLKAIFNELSKY 95
Cdd:pfam00118   1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469  96 ItessyipqKQG--TMEIRTKLRLELSnllyfmlpeyfgqlRANKMIQNIFFHENNLPLVKScVQNLLKTFLTGKfgqlV 173
Cdd:pfam00118  81 L--------AAGvhPTTIIEGYEKALE--------------KALEILDSIISIPVEDVDRED-LLKVARTSLSSK----I 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469 174 THQLVELCYNLIFFSVSDISKFNEVVqylikNFHllccRINVLPIQL-----SRIVEGFVLTRDFTVPwkDYTSKEEEFN 248
Cdd:pfam00118 134 ISRESDFLAKLVVDAVLAIPKNDGSF-----DLG----NIGVVKILGgsledSELVDGVVLDKGPLHP--DMPKRLENAK 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469 249 FIVILSSQDNQSICNGAILKITQPQDIEMFLLSSSSFYKSAMKAIQQHQIQLILSCNSVSESFKTLCYEEGIAVIAGIPR 328
Cdd:pfam00118 203 VLLLNCSLEYEKTETKATVVLSDAEQLERFLKAEEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKK 282
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238882469 329 EELLHLVSLCGIQPIICLqETLNASKIGKAQFARPITLEAKWYIQI-GIKLSNLDTLLvphylvLCGPTEGICKQ 402
Cdd:pfam00118 283 RDLERLAKATGARAVSSL-DDLTPDDLGTAGKVEEEKIGDEKYTFIeGCKSPKAATIL------LRGATDHVLDE 350
chap_CCT_theta TIGR02346
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
23-346 7.95e-08

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: 55.49  E-value: 7.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469  23 SYGPYGRSSLCVSAVGQIEITSSGISILETARVNHPVATVITRAVKNHHELVGDGTKTFILLLKAIFNELSKYITESSYI 102
Cdd:TIGR02346  37 SLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGELLNKAEELIRMGLHP 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469 103 PQ-KQGTMEIRTKLRLELSNLLYFMLPEYFGQLRANKMIqniffhennlplvKSCVqnLLKTFLTGKF-GQLVTHQLVEL 180
Cdd:TIGR02346 117 SEiIKGYEMALKKAMEILEELVVWEVKDLRDKDELIKAL-------------KASI--SSKQYGNEDFlAQLVAQACSTV 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469 181 CynliffsVSDISKFNevvqylIKNFHLlcCRINVLPIQLSRIVEGFVLTRDftvPWKDYTSKEEEfNFIVILSSQDNQS 260
Cdd:TIGR02346 182 L-------PKNPQNFN------VDNIRV--CKILGGSLSNSEVLKGMVFNRE---AEGSVKSVKNA-KVAVFSCPLDTAT 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469 261 I-CNGAILkITQPQDIEMFLLSSSSFYKSAMKAIQQHQIQLILSCNSVSESFKTLCYEEGIAVIAGIPREELLHLVSLCG 339
Cdd:TIGR02346 243 TeTKGTVL-IHNAEELLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVG 321

                  ....*..
gi 1238882469 340 IQPIICL 346
Cdd:TIGR02346 322 ATPLPRL 328
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
25-98 8.90e-08

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: 54.96  E-value: 8.90e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238882469  25 GPYGRSSLCVSAVGQIEITSSGISILETARVNHPVATVITRAVKNHHELVGDGTKTFILLLKAIFNELSKYITE 98
Cdd:cd03342    33 GPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTASMIARAATAQDDITGDGTTSNVLLIGELLKQAERYIQE 106
chap_CCT_zeta TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
18-98 4.16e-07

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: 53.20  E-value: 4.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469  18 SLVEKSYGPYGRSSLCVSAVGQIEITSSGISILETARVNHPVATVITRAVKNHHELVGDGTKTFILLLKAIFNELSKYIT 97
Cdd:TIGR02347  30 DVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDITGDGTTSTVLLIGELLKQAERYIL 109

                  .
gi 1238882469  98 E 98
Cdd:TIGR02347 110 E 110
chap_CCT_epsi TIGR02343
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
16-236 7.47e-07

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: 52.11  E-value: 7.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469  16 IGSLVEKSYGPYGRSSLCVSAVGQIEITSSGISILETARVNHPVATVITRAVKNHHELVGDGTKTFILLLKAIFNELSKY 95
Cdd:TIGR02343  39 VASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEQAEEL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469  96 ItessyipqKQGTMEIRTK------LRLELSNLlyfmlpeyfgqlraNKMIQNIFFHENNL-PLVKSCvqnllKTFLTGK 168
Cdd:TIGR02343 119 L--------DKGIHPIKIAdgfeeaARIAVEHL--------------EEISDEISADNNNRePLIQAA-----KTSLGSK 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238882469 169 FGQLVTHQLVELCYNLIfFSVSDISKfNEVvqylikNFHLLCCRINV-LPIQLSRIVEGFVLTRDFTVP 236
Cdd:TIGR02343 172 IVSKCHRRFAEIAVDAV-LNVADMER-RDV------DFDLIKVEGKVgGSLEDTKLIKGIIIDKDFSHP 232
chap_CCT_alpha TIGR02340
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
16-94 1.19e-06

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: 51.64  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469  16 IGSLVEKSYGPYGRSSLCVSAVGQIEITSSGISILETARVNHPVATVITRAVKNHHELVGDGTKTFILLLKAIF---NEL 92
Cdd:TIGR02340  24 IANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDGTTSVVIIAAELLkraDEL 103

                  ..
gi 1238882469  93 SK 94
Cdd:TIGR02340 104 VK 105
TCP1_theta cd03341
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
16-84 1.21e-06

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: 51.45  E-value: 1.21e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238882469  16 IGSLVEKSYGPYGRSSLCVSAVGQIEITSSGISILETARVNHPVATVITRAVKNHHELVGDGTKTFILL 84
Cdd:cd03341    20 LSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVL 88
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
20-84 2.94e-06

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: 50.34  E-value: 2.94e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238882469  20 VEKSYGPYGRSSLCVSAVGQIEITSSGISILETARVNHPVATVITRAVKNHHELVGDGTKTFILL 84
Cdd:cd03343    31 VRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKTQDEEVGDGTTTAVVL 95
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
16-98 4.92e-06

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: 49.59  E-value: 4.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469  16 IGSLVEKSYGPYGRSSLCVSAVGQIEITSSGISILETARVNHPVATVITRAVKNHHELVGDGTKTFILLLKAIFNELSKY 95
Cdd:cd03340    28 IADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVVVLAGEFLKEAKPF 107

                  ...
gi 1238882469  96 ITE 98
Cdd:cd03340   108 IED 110
chap_CCT_eta TIGR02345
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ...
16-98 5.27e-06

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: 49.37  E-value: 5.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469  16 IGSLVEKSYGPYGRSSLCVSAVGQIEITSSGISILETARVNHPVATVITRAVKNHHELVGDGTKTFILLLKAIFNELSKY 95
Cdd:TIGR02345  30 IAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAKSQDAEVGDGTTSVTILAGELLKEAKPF 109

                  ...
gi 1238882469  96 ITE 98
Cdd:TIGR02345 110 IEE 112
TCP1_epsilon cd03339
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
16-96 5.39e-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: 43.06  E-value: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469  16 IGSLVEKSYGPYGRSSLCVSAVGQIEITSSGISILETARVNHPVATVITRAVKNHHELVGDGTKTFILLLKAIFNELSKY 95
Cdd:cd03339    35 VANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVELSKSQDDEIGDGTTGVVVLAGALLEQAEKL 114

                  .
gi 1238882469  96 I 96
Cdd:cd03339   115 L 115
chap_CCT_delta TIGR02342
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ...
20-96 1.32e-03

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: 41.69  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469  20 VEKSYGPYGRSSLCVSAVGQIEITSSGISILETARVNHPVATVITRAVKNHHELVGDGTKTFIL----LLKAIFNELSKY 95
Cdd:TIGR02342  25 IRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGTTSVVIlagaLLGACERLLNKG 104

                  .
gi 1238882469  96 I 96
Cdd:TIGR02342 105 I 105
chap_CCT_gamma TIGR02344
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
16-84 2.54e-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: 40.88  E-value: 2.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238882469  16 IGSLVEKSYGPYGRSSLCVSAVGQIEITSSGISILETARVNHPVATVITRAVKNHHELVGDGTKTFILL 84
Cdd:TIGR02344  28 VADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSRTQDEEVGDGTTSVIIL 96
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
16-104 3.11e-03

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 40.78  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882469  16 IGSLVEKSYGPYGRSSLCVSA-----VGQIEITSSGISILETARVNHPVATVITRAVKNHHELVGDGTKTFILLLKAIFN 90
Cdd:PTZ00212   34 VADLVKTTLGPKGMDKILQPMsegprSGNVTVTNDGATILKSVWLDNPAAKILVDISKTQDEEVGDGTTSVVVLAGELLR 113
                          90
                  ....*....|....
gi 1238882469  91 ELSKYITESSYiPQ 104
Cdd:PTZ00212  114 EAEKLLDQKIH-PQ 126
 
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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