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Conserved domains on  [gi|1780592907|emb|VYS57458|]
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unnamed protein product [Arabidopsis thaliana]

Protein Classification

prefoldin domain-containing protein( domain architecture ID 2200)

prefoldin domain-containing protein may function as a molecular chaperone that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Prefoldin super family cl09111
prefoldin; Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and ...
14-143 2.31e-13

prefoldin; Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits; the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes, there are two or more paralogous genes encoding each subunit, adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


The actual alignment was detected with superfamily member cd22860:

Pssm-ID: 471851  Cd Length: 103  Bit Score: 62.53  E-value: 2.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780592907  14 KIEAEADEFLLARNQMVENDKERNANREALTALRKrarttktsvmspfdsmmkdihgsstkplvqevcstcgSHDSSEPT 93
Cdd:cd22860     7 EVEELAEEILTDKQELVDLDRRRNKNREALRALKK-------------------------------------SKKEESKV 49
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1780592907  94 WMMLpgADLFAAIPFHAVHTMLEKDEEKMEFESKKLQSLVKEKALFISEL 143
Cdd:cd22860    50 WICL--GDMFIKLPKEKAKKMLEKDQKELDKEINKLRSELKEKVNKLRDL 97
 
Name Accession Description Interval E-value
PDRG1 cd22860
p53 and DNA damage-regulated protein 1; p53 and DNA damage-regulated protein 1 (PDRG1) is a ...
14-143 2.31e-13

p53 and DNA damage-regulated protein 1; p53 and DNA damage-regulated protein 1 (PDRG1) is a beta-type subunit of the prefoldin-like complex that is part of the PAQosome (Particle for Arrangement of Quaternary structure) complex. The PAQosome is a cochaperone that assists the chaperone HSP90 in assembly of large protein complexes. PDRG1 acts as a tumor marker in multiple cancer types, including testicular cancer, lung cancer, colorectal cancer, liver cancer, etc. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related.


Pssm-ID: 467471  Cd Length: 103  Bit Score: 62.53  E-value: 2.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780592907  14 KIEAEADEFLLARNQMVENDKERNANREALTALRKrarttktsvmspfdsmmkdihgsstkplvqevcstcgSHDSSEPT 93
Cdd:cd22860     7 EVEELAEEILTDKQELVDLDRRRNKNREALRALKK-------------------------------------SKKEESKV 49
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1780592907  94 WMMLpgADLFAAIPFHAVHTMLEKDEEKMEFESKKLQSLVKEKALFISEL 143
Cdd:cd22860    50 WICL--GDMFIKLPKEKAKKMLEKDQKELDKEINKLRSELKEKVNKLRDL 97
 
Name Accession Description Interval E-value
PDRG1 cd22860
p53 and DNA damage-regulated protein 1; p53 and DNA damage-regulated protein 1 (PDRG1) is a ...
14-143 2.31e-13

p53 and DNA damage-regulated protein 1; p53 and DNA damage-regulated protein 1 (PDRG1) is a beta-type subunit of the prefoldin-like complex that is part of the PAQosome (Particle for Arrangement of Quaternary structure) complex. The PAQosome is a cochaperone that assists the chaperone HSP90 in assembly of large protein complexes. PDRG1 acts as a tumor marker in multiple cancer types, including testicular cancer, lung cancer, colorectal cancer, liver cancer, etc. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related.


Pssm-ID: 467471  Cd Length: 103  Bit Score: 62.53  E-value: 2.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780592907  14 KIEAEADEFLLARNQMVENDKERNANREALTALRKrarttktsvmspfdsmmkdihgsstkplvqevcstcgSHDSSEPT 93
Cdd:cd22860     7 EVEELAEEILTDKQELVDLDRRRNKNREALRALKK-------------------------------------SKKEESKV 49
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1780592907  94 WMMLpgADLFAAIPFHAVHTMLEKDEEKMEFESKKLQSLVKEKALFISEL 143
Cdd:cd22860    50 WICL--GDMFIKLPKEKAKKMLEKDQKELDKEINKLRSELKEKVNKLRDL 97
 
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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