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Conserved domains on  [gi|15228766|ref|NP_188887|]
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prefoldin 2 [Arabidopsis thaliana]

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 ...
 18-117 7.27e-43

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: 136.88  E-value: 7.27e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228766  18 AVLNMYEGKRSELSQIYSNITDLEMQVSEHSLVINAIQPLDQSRKCFRMIGGVLVERTIKEVLPAVQRNKDGLEEVVRKL 97
Cdd:cd23163   1 EVVAQYNQLRQEQQQLASKIAELEQELNEHKLVIDTLKPLDPDRKCFRLVGGVLVERTVGEVLPALEENKENLEEVIEQL 80

                        90       100
                ....*....|....*....|
gi 15228766  98 YETLEKKKKDLTEFEAKYKI 117
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 ...
 18-117 7.27e-43

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: 136.88  E-value: 7.27e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228766  18 AVLNMYEGKRSELSQIYSNITDLEMQVSEHSLVINAIQPLDQSRKCFRMIGGVLVERTIKEVLPAVQRNKDGLEEVVRKL 97
Cdd:cd23163   1 EVVAQYNQLRQEQQQLASKIAELEQELNEHKLVIDTLKPLDPDRKCFRLVGGVLVERTVGEVLPALEENKENLEEVIEQL 80

                        90       100
                ....*....|....*....|
gi 15228766  98 YETLEKKKKDLTEFEAKYKI 117
Cdd:cd23163  81 NEQLEEKEKELNEFREKYNI 100
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
 20-121 2.82e-19

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


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 77.26  E-value: 2.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228766    20 LNMYEGKRSELSQIYSNITDLEMQVSEHSLVINAIQPLDQSRKCFRMIGGVLVERTIKEVLPAVQRNKDGLEEVVRKLYE 99
Cdd:pfam01920   1 INKFQQLQQQLQLLAQQIKQLETQLKELELALEELELLDEDTKVYKLIGDVLVKQDKEEVKEQLEERKETLEKEIKTLEK 80

                          90       100
                  ....*....|....*....|..
gi 15228766   100 TLEKKKKDLTEFEAKYKIRITK 121
Cdd:pfam01920  81 QLEKLEKELEELKEELYKKFGQ 102
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
13-110 2.37e-03

Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440992 [Multi-domain]  Cd Length: 121  Bit Score: 35.64  E-value: 2.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228766  13 PPNEQAVLNMYEGKRSELSQIYSNITDLEMQVSEHSLVINAIQPLDQSRKCFRMIGGVLVERTIKEVLPAVQRNKDGLE- 91
Cdd:COG1382   6 PPEVQNQLAQLQQLQQQLQAVAAQKQQVESELKEAEKALEELEKLPDDAEVYKSVGNLLVKTDKEEVIKELEEKKETLEl 85

                        90       100
                ....*....|....*....|.
gi 15228766  92 --EVVRKLYETLEKKKKDLTE 110
Cdd:COG1382  86 rlKTLEKQEERLQKQLEELQE 106
 
Name Accession Description Interval E-value
Prefoldin_2 cd23163
prefoldin subunit 2; Prefoldin subunit 2 is one of the beta subunits of the eukaryotic ...
 18-117 7.27e-43

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: 136.88  E-value: 7.27e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228766  18 AVLNMYEGKRSELSQIYSNITDLEMQVSEHSLVINAIQPLDQSRKCFRMIGGVLVERTIKEVLPAVQRNKDGLEEVVRKL 97
Cdd:cd23163   1 EVVAQYNQLRQEQQQLASKIAELEQELNEHKLVIDTLKPLDPDRKCFRLVGGVLVERTVGEVLPALEENKENLEEVIEQL 80

                        90       100
                ....*....|....*....|
gi 15228766  98 YETLEKKKKDLTEFEAKYKI 117
Cdd:cd23163  81 NEQLEEKEKELNEFREKYNI 100
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
 20-121 2.82e-19

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


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 77.26  E-value: 2.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228766    20 LNMYEGKRSELSQIYSNITDLEMQVSEHSLVINAIQPLDQSRKCFRMIGGVLVERTIKEVLPAVQRNKDGLEEVVRKLYE 99
Cdd:pfam01920   1 INKFQQLQQQLQLLAQQIKQLETQLKELELALEELELLDEDTKVYKLIGDVLVKQDKEEVKEQLEERKETLEKEIKTLEK 80

                          90       100
                  ....*....|....*....|..
gi 15228766   100 TLEKKKKDLTEFEAKYKIRITK 121
Cdd:pfam01920  81 QLEKLEKELEELKEELYKKFGQ 102
Prefoldin_beta cd00632
Prefoldin beta subunit; Beta subunits of prefoldin, a hexameric molecular chaperone complex, ...
 29-108 2.88e-09

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: 50.81  E-value: 2.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228766  29 ELSQIYSNITDLEMQVSEHSLVINAIQPLDQSRKCFRMIGGVLVERTIKEVLPAVQRNKDGLEEVvrklYETLEKKKKDL 108
Cdd:cd00632   1 EVLALKSQKEELERKINEQKVVLDELSNLKKNRKVYRQQGNIFILASKEETLSELKKTLDHLQKE----IKELEQQLKAK 76
Prefoldin cd00890
prefoldin; Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and ...
 35-106 1.77e-06

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.


Pssm-ID: 467470  Cd Length: 79  Bit Score: 43.48  E-value: 1.77e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228766  35 SNITDLEMQVSEHSLVINAIQPLDQ-SRKCFRMIGGVLVERTIKEVLPAVQRNKDGLEEVVRKLYETLEKKKK 106
Cdd:cd00890   7 QQIEQLNRQINELEEALDELSNLDKdTEEVYRSVGGVFIEKSKEETKEELEEKLDELQKEIKKLEQQLEAKTK 79
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
13-110 2.37e-03

Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440992 [Multi-domain]  Cd Length: 121  Bit Score: 35.64  E-value: 2.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228766  13 PPNEQAVLNMYEGKRSELSQIYSNITDLEMQVSEHSLVINAIQPLDQSRKCFRMIGGVLVERTIKEVLPAVQRNKDGLE- 91
Cdd:COG1382   6 PPEVQNQLAQLQQLQQQLQAVAAQKQQVESELKEAEKALEELEKLPDDAEVYKSVGNLLVKTDKEEVIKELEEKKETLEl 85

                        90       100
                ....*....|....*....|.
gi 15228766  92 --EVVRKLYETLEKKKKDLTE 110
Cdd:COG1382  86 rlKTLEKQEERLQKQLEELQE 106
 
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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