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Conserved domains on  [gi|1331792263|gb|PNI51859|]
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BBS12 isoform 3, partial [Pan troglodytes]

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 ...
 23-125 2.95e-04

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: 40.65  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331792263  23 AETGRTFLGPLKSSKFIIDEecHESVLISST-VRLLESLDLTSAVGQLLNEAVQAQNNTYRTGISTLLFLVGAWSSAVEE 101
Cdd:pfam00118   2 ADIVRTSLGPKGMDKMLVNS--GGDVTVTNDgATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEK 79

                          90       100
                  ....*....|....*....|....
gi 1331792263 102 CLHLGVPISIIVSVMSEGLNFCSE 125
Cdd:pfam00118  80 LLAAGVHPTTIIEGYEKALEKALE 103
 
Name Accession Description Interval E-value
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 23-125 2.95e-04

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: 40.65  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331792263  23 AETGRTFLGPLKSSKFIIDEecHESVLISST-VRLLESLDLTSAVGQLLNEAVQAQNNTYRTGISTLLFLVGAWSSAVEE 101
Cdd:pfam00118   2 ADIVRTSLGPKGMDKMLVNS--GGDVTVTNDgATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEK 79

                          90       100
                  ....*....|....*....|....
gi 1331792263 102 CLHLGVPISIIVSVMSEGLNFCSE 125
Cdd:pfam00118  80 LLAAGVHPTTIIEGYEKALEKALE 103
TCP1_theta cd03341
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
 22-130 2.02e-03

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: 37.97  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331792263  22 FAETGRTFLGPLKSSKFIIDEEcHESVLISSTVRLLESLDLTSAVGQLLNEAVQAQNNTYRTGISTLLFLVGAWSSAVEE 101
Cdd:cd03341    20 LSQITRTSYGPNGMNKMVINHL-EKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGELLEKAEE 98

                          90       100
                  ....*....|....*....|....*....
gi 1331792263 102 CLHLGVPISIIVSVMSEGLNFCSEEVVSL 130
Cdd:cd03341    99 LLRMGLHPSEIIEGYEKALKKALEILEEL 127
 
Name Accession Description Interval E-value
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
 23-125 2.95e-04

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: 40.65  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331792263  23 AETGRTFLGPLKSSKFIIDEecHESVLISST-VRLLESLDLTSAVGQLLNEAVQAQNNTYRTGISTLLFLVGAWSSAVEE 101
Cdd:pfam00118   2 ADIVRTSLGPKGMDKMLVNS--GGDVTVTNDgATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEK 79

                          90       100
                  ....*....|....*....|....
gi 1331792263 102 CLHLGVPISIIVSVMSEGLNFCSE 125
Cdd:pfam00118  80 LLAAGVHPTTIIEGYEKALEKALE 103
TCP1_theta cd03341
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
 22-130 2.02e-03

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: 37.97  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331792263  22 FAETGRTFLGPLKSSKFIIDEEcHESVLISSTVRLLESLDLTSAVGQLLNEAVQAQNNTYRTGISTLLFLVGAWSSAVEE 101
Cdd:cd03341    20 LSQITRTSYGPNGMNKMVINHL-EKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGELLEKAEE 98

                          90       100
                  ....*....|....*....|....*....
gi 1331792263 102 CLHLGVPISIIVSVMSEGLNFCSEEVVSL 130
Cdd:cd03341    99 LLRMGLHPSEIIEGYEKALKKALEILEEL 127
 
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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