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Conserved domains on  [gi|2462580500|ref|XP_054179484|]
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prefoldin subunit 4 isoform X3 [Homo sapiens]

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 ...
101-127 1.06e-10

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 cd23165:

Pssm-ID: 471851 [Multi-domain]  Cd Length: 103  Bit Score: 54.47  E-value: 1.06e-10
                          10        20
                  ....*....|....*....|....*..
gi 2462580500 101 DQQKINKFARNTSRITELKEEIEVKKE 127
Cdd:cd23165     1 DQQKINKFSRLNARLHELKEELKAKKK 27
 
Name Accession Description Interval E-value
Prefoldin_4 cd23165
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ...
101-127 1.06e-10

prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic prefoldin complex. 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 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.


Pssm-ID: 467481 [Multi-domain]  Cd Length: 103  Bit Score: 54.47  E-value: 1.06e-10
                          10        20
                  ....*....|....*....|....*..
gi 2462580500 101 DQQKINKFARNTSRITELKEEIEVKKE 127
Cdd:cd23165     1 DQQKINKFSRLNARLHELKEELKAKKK 27
 
Name Accession Description Interval E-value
Prefoldin_4 cd23165
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ...
101-127 1.06e-10

prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic prefoldin complex. 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 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.


Pssm-ID: 467481 [Multi-domain]  Cd Length: 103  Bit Score: 54.47  E-value: 1.06e-10
                          10        20
                  ....*....|....*....|....*..
gi 2462580500 101 DQQKINKFARNTSRITELKEEIEVKKE 127
Cdd:cd23165     1 DQQKINKFSRLNARLHELKEELKAKKK 27
 
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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