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Conserved domains on  [gi|31981577|ref|NP_035200|]
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prefoldin subunit 2 isoform 1 [Mus musculus]

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 ...
25-124 1.62e-53

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: 164.23  E-value: 1.62e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981577  25 QVIAGFNRLRQEQRGLASKAAELEMELNEHSLVIDTLKEVDETRKCYRMVGGVLVERTVKEVLPALEGNKEQIQKIIETL 104
Cdd:cd23163   1 EVVAQYNQLRQEQQQLASKIAELEQELNEHKLVIDTLKPLDPDRKCFRLVGGVLVERTVGEVLPALEENKENLEEVIEQL 80
                        90       100
                ....*....|....*....|
gi 31981577 105 SQQLQAKGKELNEFREKHNI 124
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 ...
25-124 1.62e-53

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: 164.23  E-value: 1.62e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981577  25 QVIAGFNRLRQEQRGLASKAAELEMELNEHSLVIDTLKEVDETRKCYRMVGGVLVERTVKEVLPALEGNKEQIQKIIETL 104
Cdd:cd23163   1 EVVAQYNQLRQEQQQLASKIAELEQELNEHKLVIDTLKPLDPDRKCFRLVGGVLVERTVGEVLPALEENKENLEEVIEQL 80
                        90       100
                ....*....|....*....|
gi 31981577 105 SQQLQAKGKELNEFREKHNI 124
Cdd:cd23163  81 NEQLEEKEKELNEFREKYNI 100
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
27-128 9.36e-26

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


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 93.83  E-value: 9.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981577    27 IAGFNRLRQEQRGLASKAAELEMELNEHSLVIDTLKEVDETRKCYRMVGGVLVERTVKEVLPALEGNKEQIQKIIETLSQ 106
Cdd:pfam01920   1 INKFQQLQQQLQLLAQQIKQLETQLKELELALEELELLDEDTKVYKLIGDVLVKQDKEEVKEQLEERKETLEKEIKTLEK 80
                          90       100
                  ....*....|....*....|..
gi 31981577   107 QLQAKGKELNEFREKHNIRLMG 128
Cdd:pfam01920  81 QLEKLEKELEELKEELYKKFGQ 102
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
23-128 8.48e-08

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


Pssm-ID: 440992 [Multi-domain]  Cd Length: 121  Bit Score: 47.96  E-value: 8.48e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981577  23 AEQVIAGFNRLRQEQRGLASKAAELEMELNEHSLVIDTLKEVDETRKCYRMVGGVLVERTVKEVLPALEGNKEQIQKIIE 102
Cdd:COG1382   9 VQNQLAQLQQLQQQLQAVAAQKQQVESELKEAEKALEELEKLPDDAEVYKSVGNLLVKTDKEEVIKELEEKKETLELRLK 88
                        90       100
                ....*....|....*....|....*.
gi 31981577 103 TLSQQLQAKGKELNEFREKHNIRLMG 128
Cdd:COG1382  89 TLEKQEERLQKQLEELQEKLQEALSG 114
PRK09343 PRK09343
prefoldin subunit beta; Provisional
24-126 3.56e-03

prefoldin subunit beta; Provisional


Pssm-ID: 181787 [Multi-domain]  Cd Length: 121  Bit Score: 35.43  E-value: 3.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981577   24 EQVIAGFNRLRQEQRGLASKAAELEMELNEHSLVIDTLKEVDETRKCYRMVGGVLVERTVKEVLPALEGNKEQIQKIIET 103
Cdd:PRK09343  10 QAQLAQLQQLQQQLERLLQQKSQIDLELREINKALEELEKLPDDTPIYKIVGNLLVKVDKTKVEKELKERKELLELRSRT 89
                         90       100
                 ....*....|....*....|...
gi 31981577  104 LSQQLQAKGKELNEFREKHNIRL 126
Cdd:PRK09343  90 LEKQEKKLREKLKELQAKINEML 112
 
Name Accession Description Interval E-value
Prefoldin_2 cd23163
prefoldin subunit 2; Prefoldin subunit 2 is one of the beta subunits of the eukaryotic ...
25-124 1.62e-53

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: 164.23  E-value: 1.62e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981577  25 QVIAGFNRLRQEQRGLASKAAELEMELNEHSLVIDTLKEVDETRKCYRMVGGVLVERTVKEVLPALEGNKEQIQKIIETL 104
Cdd:cd23163   1 EVVAQYNQLRQEQQQLASKIAELEQELNEHKLVIDTLKPLDPDRKCFRLVGGVLVERTVGEVLPALEENKENLEEVIEQL 80
                        90       100
                ....*....|....*....|
gi 31981577 105 SQQLQAKGKELNEFREKHNI 124
Cdd:cd23163  81 NEQLEEKEKELNEFREKYNI 100
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
27-128 9.36e-26

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


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 93.83  E-value: 9.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981577    27 IAGFNRLRQEQRGLASKAAELEMELNEHSLVIDTLKEVDETRKCYRMVGGVLVERTVKEVLPALEGNKEQIQKIIETLSQ 106
Cdd:pfam01920   1 INKFQQLQQQLQLLAQQIKQLETQLKELELALEELELLDEDTKVYKLIGDVLVKQDKEEVKEQLEERKETLEKEIKTLEK 80
                          90       100
                  ....*....|....*....|..
gi 31981577   107 QLQAKGKELNEFREKHNIRLMG 128
Cdd:pfam01920  81 QLEKLEKELEELKEELYKKFGQ 102
Prefoldin_beta cd00632
Prefoldin beta subunit; Beta subunits of prefoldin, a hexameric molecular chaperone complex, ...
36-113 1.79e-17

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: 71.99  E-value: 1.79e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31981577  36 EQRGLASKAAELEMELNEHSLVIDTLKEVDETRKCYRMVGGVLVERTVKEVLPALEGNKEQIQKIIETLSQQLQAKGK 113
Cdd:cd00632   1 EVLALKSQKEELERKINEQKVVLDELSNLKKNRKVYRQQGNIFILASKEETLSELKKTLDHLQKEIKELEQQLKAKEK 78
Prefoldin cd00890
prefoldin; Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and ...
36-113 3.95e-14

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: 63.51  E-value: 3.95e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31981577  36 EQRGLASKAAELEMELNEHSLVIDTLKEVD-ETRKCYRMVGGVLVERTVKEVLPALEGNKEQIQKIIETLSQQLQAKGK 113
Cdd:cd00890   1 QVQALSQQIEQLNRQINELEEALDELSNLDkDTEEVYRSVGGVFIEKSKEETKEELEEKLDELQKEIKKLEQQLEAKTK 79
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
23-128 8.48e-08

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


Pssm-ID: 440992 [Multi-domain]  Cd Length: 121  Bit Score: 47.96  E-value: 8.48e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981577  23 AEQVIAGFNRLRQEQRGLASKAAELEMELNEHSLVIDTLKEVDETRKCYRMVGGVLVERTVKEVLPALEGNKEQIQKIIE 102
Cdd:COG1382   9 VQNQLAQLQQLQQQLQAVAAQKQQVESELKEAEKALEELEKLPDDAEVYKSVGNLLVKTDKEEVIKELEEKKETLELRLK 88
                        90       100
                ....*....|....*....|....*.
gi 31981577 103 TLSQQLQAKGKELNEFREKHNIRLMG 128
Cdd:COG1382  89 TLEKQEERLQKQLEELQEKLQEALSG 114
Prefoldin_beta_GimC cd23162
Prefoldin beta subunit, archaeal; Archaeal beta subunit of prefoldin (GimC), a hexameric ...
27-121 2.92e-06

Prefoldin beta subunit, archaeal; Archaeal beta subunit of prefoldin (GimC), 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: 467478 [Multi-domain]  Cd Length: 102  Bit Score: 43.24  E-value: 2.92e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981577  27 IAGFNRLRQEQRGLASKAAELEMELNEHSLVIDTLKEVDETRKCYRMVGGVLVERTVKEVLPALEGNKEQIQKIIETLSQ 106
Cdd:cd23162   3 LAQLQQLQQQLQAVLLQKQQLEAELREIERALEELEKLPDDAEVYKSVGTILVKVDKEEVIKELKERKETLELRLKTLEK 82
                        90
                ....*....|....*
gi 31981577 107 QLQAKGKELNEFREK 121
Cdd:cd23162  83 QEERLRKQLEELQKK 97
Prefoldin_6 cd23161
Prefoldin subunit 6; Prefoldin subunit 6 is one of the beta subunits of the eukaryotic ...
30-121 6.41e-04

Prefoldin subunit 6; Prefoldin subunit 6 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: 467477 [Multi-domain]  Cd Length: 101  Bit Score: 37.08  E-value: 6.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981577  30 FNRLRQEQRGLASKAAELEMELNEHSLVIDTLKEVDETRKCYRMVGGVLVERTVKEVLPALEGNKEQIQKIIETLSQQLQ 109
Cdd:cd23161   4 FQKLQKELQKLVEARQQLEAQLNENEMVKKELDLLEDDAKVYKLIGPVLVKQDLDEAKSNVDKRLEFITGEIKRVEKQIK 83
                        90
                ....*....|..
gi 31981577 110 AKGKELNEFREK 121
Cdd:cd23161  84 DLEKKQEKKREK 95
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
24-121 1.88e-03

Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), 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: 467476 [Multi-domain]  Cd Length: 127  Bit Score: 36.31  E-value: 1.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981577  24 EQVIAGFNRLRQEQRGLASKAAELEMELNEHSLVIDTLKE-----------------------VDETRKCYRMVG-GVLV 79
Cdd:cd23160   3 QRLLAELQQLEQQAEALQQQIELLQASINELNRAKETLEElkklkegteilvpigggsfvkakIKDTDKVLVNIGaGVVV 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 31981577  80 ERTVKEVLPALEGNKEQIQKIIETLSQQLQAKGKELNEFREK 121
Cdd:cd23160  83 EKTIDEAIEILEKRIKELEKALEKLQEQLQQIAQRLEELEAE 124
PRK09343 PRK09343
prefoldin subunit beta; Provisional
24-126 3.56e-03

prefoldin subunit beta; Provisional


Pssm-ID: 181787 [Multi-domain]  Cd Length: 121  Bit Score: 35.43  E-value: 3.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981577   24 EQVIAGFNRLRQEQRGLASKAAELEMELNEHSLVIDTLKEVDETRKCYRMVGGVLVERTVKEVLPALEGNKEQIQKIIET 103
Cdd:PRK09343  10 QAQLAQLQQLQQQLERLLQQKSQIDLELREINKALEELEKLPDDTPIYKIVGNLLVKVDKTKVEKELKERKELLELRSRT 89
                         90       100
                 ....*....|....*....|...
gi 31981577  104 LSQQLQAKGKELNEFREKHNIRL 126
Cdd:PRK09343  90 LEKQEKKLREKLKELQAKINEML 112
 
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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