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Conserved domains on  [gi|893695357|gb|EGE79061|]
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prefoldin subunit 2 [Blastomyces dermatitidis ATCC 18188]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Prefoldin_2 cd23163
prefoldin subunit 2; Prefoldin subunit 2 is one of the beta subunits of the eukaryotic ...
 13-112 7.56e-42

prefoldin subunit 2; Prefoldin subunit 2 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: 467479  Cd Length: 100  Bit Score: 133.03  E-value: 7.56e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893695357  13 ELQTQYQNYKTTLQQLAQKIGDIEQETEEHKLVIDTLEPLAGDRKCFRLINGVLVERTVKDVIPPLKTNSDGLKQVLDEL 92
Cdd:cd23163    1 EVVAQYNQLRQEQQQLASKIAELEQELNEHKLVIDTLKPLDPDRKCFRLVGGVLVERTVGEVLPALEENKENLEEVIEQL 80

                         90       100
                 ....*....|....*....|
gi 893695357  93 LKQYKAKQDELDGWKKKNNI 112
Cdd:cd23163   81 NEQLEEKEKELNEFREKYNI 100
 
Name Accession Description Interval E-value
Prefoldin_2 cd23163
prefoldin subunit 2; Prefoldin subunit 2 is one of the beta subunits of the eukaryotic ...
 13-112 7.56e-42

prefoldin subunit 2; Prefoldin subunit 2 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: 467479  Cd Length: 100  Bit Score: 133.03  E-value: 7.56e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893695357  13 ELQTQYQNYKTTLQQLAQKIGDIEQETEEHKLVIDTLEPLAGDRKCFRLINGVLVERTVKDVIPPLKTNSDGLKQVLDEL 92
Cdd:cd23163    1 EVVAQYNQLRQEQQQLASKIAELEQELNEHKLVIDTLKPLDPDRKCFRLVGGVLVERTVGEVLPALEENKENLEEVIEQL 80

                         90       100
                 ....*....|....*....|
gi 893695357  93 LKQYKAKQDELDGWKKKNNI 112
Cdd:cd23163   81 NEQLEEKEKELNEFREKYNI 100
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
 15-114 1.45e-15

Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 66.48  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893695357   15 QTQYQNYKTTLQQLAQKIGDIEQETEEHKLVIDTLEPLAGDRKCFRLINGVLVERTVKDVIPPLKTNSDGLKQVLDELLK 94
Cdd:pfam01920   1 INKFQQLQQQLQLLAQQIKQLETQLKELELALEELELLDEDTKVYKLIGDVLVKQDKEEVKEQLEERKETLEKEIKTLEK 80

                          90       100
                  ....*....|....*....|
gi 893695357   95 QYKAKQDELDGWKKKNNIQV 114
Cdd:pfam01920  81 QLEKLEKELEELKEELYKKF 100
 
Name Accession Description Interval E-value
Prefoldin_2 cd23163
prefoldin subunit 2; Prefoldin subunit 2 is one of the beta subunits of the eukaryotic ...
 13-112 7.56e-42

prefoldin subunit 2; Prefoldin subunit 2 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: 467479  Cd Length: 100  Bit Score: 133.03  E-value: 7.56e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893695357  13 ELQTQYQNYKTTLQQLAQKIGDIEQETEEHKLVIDTLEPLAGDRKCFRLINGVLVERTVKDVIPPLKTNSDGLKQVLDEL 92
Cdd:cd23163    1 EVVAQYNQLRQEQQQLASKIAELEQELNEHKLVIDTLKPLDPDRKCFRLVGGVLVERTVGEVLPALEENKENLEEVIEQL 80

                         90       100
                 ....*....|....*....|
gi 893695357  93 LKQYKAKQDELDGWKKKNNI 112
Cdd:cd23163   81 NEQLEEKEKELNEFREKYNI 100
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
 15-114 1.45e-15

Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 66.48  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893695357   15 QTQYQNYKTTLQQLAQKIGDIEQETEEHKLVIDTLEPLAGDRKCFRLINGVLVERTVKDVIPPLKTNSDGLKQVLDELLK 94
Cdd:pfam01920   1 INKFQQLQQQLQLLAQQIKQLETQLKELELALEELELLDEDTKVYKLIGDVLVKQDKEEVKEQLEERKETLEKEIKTLEK 80

                          90       100
                  ....*....|....*....|
gi 893695357   95 QYKAKQDELDGWKKKNNIQV 114
Cdd:pfam01920  81 QLEKLEKELEELKEELYKKF 100
Prefoldin_beta cd00632
Prefoldin beta subunit; Beta subunits of prefoldin, a hexameric molecular chaperone complex, ...
 25-100 6.87e-04

Prefoldin beta subunit; Beta subunits of prefoldin, a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin 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: 467469  Cd Length: 78  Bit Score: 35.78  E-value: 6.87e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 893695357  25 LQQLAQKIGDIEQETEEHKLVIDTLEPLAGDRKCFRLINGVLVERTVKDVIPPLKTNSDGLKQVLDELLKQYKAKQ 100
Cdd:cd00632    2 VLALKSQKEELERKINEQKVVLDELSNLKKNRKVYRQQGNIFILASKEETLSELKKTLDHLQKEIKELEQQLKAKE 77
 
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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