NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|442631632|ref|NP_001261696|]
View 

prefoldin 2, isoform B [Drosophila melanogaster]

Protein Classification

prefoldin subunit( domain architecture ID 10487305)

prefoldin subunit works as a transfer protein in conjunction with a chaperonin molecule to form a chaperone complex and correctly fold other nascent proteins

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 14-113 1.31e-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: 136.11  E-value: 1.31e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631632  14 AIVAQFQQLRNEQRNLVNSLNTLEMDLREHKTVIETLEAADPERKCFRQIGGVLCERTVKEVLPQLVENKDFIAKTIQMV 93
Cdd:cd23163    1 EVVAQYNQLRQEQQQLASKIAELEQELNEHKLVIDTLKPLDPDRKCFRLVGGVLVERTVGEVLPALEENKENLEEVIEQL 80

                         90       100
                 ....*....|....*....|
gi 442631632  94 TNDLSKKGSELNKFKEEHNI 113
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 ...
 14-113 1.31e-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: 136.11  E-value: 1.31e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631632  14 AIVAQFQQLRNEQRNLVNSLNTLEMDLREHKTVIETLEAADPERKCFRQIGGVLCERTVKEVLPQLVENKDFIAKTIQMV 93
Cdd:cd23163    1 EVVAQYNQLRQEQQQLASKIAELEQELNEHKLVIDTLKPLDPDRKCFRLVGGVLVERTVGEVLPALEENKENLEEVIEQL 80

                         90       100
                 ....*....|....*....|
gi 442631632  94 TNDLSKKGSELNKFKEEHNI 113
Cdd:cd23163   81 NEQLEEKEKELNEFREKYNI 100
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
 16-117 9.06e-23

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


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 85.74  E-value: 9.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631632   16 VAQFQQLRNEQRNLVNSLNTLEMDLREHKTVIETLEAADPERKCFRQIGGVLCERTVKEVLPQLVENKDFIAKTIQMVTN 95
Cdd:pfam01920   1 INKFQQLQQQLQLLAQQIKQLETQLKELELALEELELLDEDTKVYKLIGDVLVKQDKEEVKEQLEERKETLEKEIKTLEK 80

                          90       100
                  ....*....|....*....|..
gi 442631632   96 DLSKKGSELNKFKEEHNIKIRG 117
Cdd:pfam01920  81 QLEKLEKELEELKEELYKKFGQ 102
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
16-84 5.70e-06

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


Pssm-ID: 440992 [Multi-domain]  Cd Length: 121  Bit Score: 42.95  E-value: 5.70e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442631632  16 VAQFQQLRNEQRNLVNSLNTLEMDLREHKTVIETLEAADPERKCFRQIGGVLCERTVKEVLPQLVENKD 84
Cdd:COG1382   13 LAQLQQLQQQLQAVAAQKQQVESELKEAEKALEELEKLPDDAEVYKSVGNLLVKTDKEEVIKELEEKKE 81
gimC_beta TIGR02338
prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular ...
 13-116 2.76e-05

prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular chaperones, with a conserved toroidal architecture, that assist in the folding of nascent and/or denatured polypeptide chains. The group I chaperonin system consists of GroEL and GroES, and is found (usually) in bacteria and organelles of bacterial origin. The group II chaperonin system, called the thermosome in Archaea and TRiC or CCT in the Eukaryota, is structurally similar but only distantly related. Prefoldin, also called GimC, is a complex in Archaea and Eukaryota, that works with group II chaperonins. Members of this protein family are the archaeal clade of the beta class of prefoldin subunit. Closely related, but outside the scope of this family are the eukaryotic beta-class prefoldin subunits, Gim-1,3,4 and 6. The alpha class prefoldin subunits are more distantly related.


Pssm-ID: 131391 [Multi-domain]  Cd Length: 110  Bit Score: 40.80  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631632   13 EAIVAQFQQLRNEQRNLVNSLNTLEMDLREHKTVIETLEAADPERKCFRQIGGVLCERTVKEVLPQLVENKDfiakTIQM 92
Cdd:TIGR02338   6 QNQLAQLQQLQQQLQAVATQKQQVEAQLKEAEKALEELERLPDDTPVYKSVGNLLVKTDKEEAIQELKEKKE----TLEL 81

                          90       100
                  ....*....|....*....|....
gi 442631632   93 VTNDLSKKGSELNKFKEEHNIKIR 116
Cdd:TIGR02338  82 RVKTLQRQEERLREQLKELQEKIQ 105
 
Name Accession Description Interval E-value
Prefoldin_2 cd23163
prefoldin subunit 2; Prefoldin subunit 2 is one of the beta subunits of the eukaryotic ...
 14-113 1.31e-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: 136.11  E-value: 1.31e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631632  14 AIVAQFQQLRNEQRNLVNSLNTLEMDLREHKTVIETLEAADPERKCFRQIGGVLCERTVKEVLPQLVENKDFIAKTIQMV 93
Cdd:cd23163    1 EVVAQYNQLRQEQQQLASKIAELEQELNEHKLVIDTLKPLDPDRKCFRLVGGVLVERTVGEVLPALEENKENLEEVIEQL 80

                         90       100
                 ....*....|....*....|
gi 442631632  94 TNDLSKKGSELNKFKEEHNI 113
Cdd:cd23163   81 NEQLEEKEKELNEFREKYNI 100
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
 16-117 9.06e-23

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


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 85.74  E-value: 9.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631632   16 VAQFQQLRNEQRNLVNSLNTLEMDLREHKTVIETLEAADPERKCFRQIGGVLCERTVKEVLPQLVENKDFIAKTIQMVTN 95
Cdd:pfam01920   1 INKFQQLQQQLQLLAQQIKQLETQLKELELALEELELLDEDTKVYKLIGDVLVKQDKEEVKEQLEERKETLEKEIKTLEK 80

                          90       100
                  ....*....|....*....|..
gi 442631632   96 DLSKKGSELNKFKEEHNIKIRG 117
Cdd:pfam01920  81 QLEKLEKELEELKEELYKKFGQ 102
Prefoldin_beta cd00632
Prefoldin beta subunit; Beta subunits of prefoldin, a hexameric molecular chaperone complex, ...
 25-101 4.52e-08

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: 47.34  E-value: 4.52e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442631632  25 EQRNLVNSLNTLEMDLREHKTVIETLEAADPERKCFRQIGGVLCERTVKEVLPQLVENKDFIAKTIQMVTNDLSKKG 101
Cdd:cd00632    1 EVLALKSQKEELERKINEQKVVLDELSNLKKNRKVYRQQGNIFILASKEETLSELKKTLDHLQKEIKELEQQLKAKE 77
Prefoldin_beta_GimC cd23162
Prefoldin beta subunit, archaeal; Archaeal beta subunit of prefoldin (GimC), a hexameric ...
 16-118 4.81e-07

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: 45.16  E-value: 4.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631632  16 VAQFQQLRNEQRNLVNSLNTLEMDLREHKTVIETLEAADPERKCFRQIGGVLCERTVKEVLPQLVENKDfiakTIQMVTN 95
Cdd:cd23162    3 LAQLQQLQQQLQAVLLQKQQLEAELREIERALEELEKLPDDAEVYKSVGTILVKVDKEEVIKELKERKE----TLELRLK 78

                         90       100
                 ....*....|....*....|...
gi 442631632  96 DLSKKGSELNKFKEEHNIKIRGE 118
Cdd:cd23162   79 TLEKQEERLRKQLEELQKKIQEA 101
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
16-84 5.70e-06

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


Pssm-ID: 440992 [Multi-domain]  Cd Length: 121  Bit Score: 42.95  E-value: 5.70e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442631632  16 VAQFQQLRNEQRNLVNSLNTLEMDLREHKTVIETLEAADPERKCFRQIGGVLCERTVKEVLPQLVENKD 84
Cdd:COG1382   13 LAQLQQLQQQLQAVAAQKQQVESELKEAEKALEELEKLPDDAEVYKSVGNLLVKTDKEEVIKELEEKKE 81
gimC_beta TIGR02338
prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular ...
 13-116 2.76e-05

prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular chaperones, with a conserved toroidal architecture, that assist in the folding of nascent and/or denatured polypeptide chains. The group I chaperonin system consists of GroEL and GroES, and is found (usually) in bacteria and organelles of bacterial origin. The group II chaperonin system, called the thermosome in Archaea and TRiC or CCT in the Eukaryota, is structurally similar but only distantly related. Prefoldin, also called GimC, is a complex in Archaea and Eukaryota, that works with group II chaperonins. Members of this protein family are the archaeal clade of the beta class of prefoldin subunit. Closely related, but outside the scope of this family are the eukaryotic beta-class prefoldin subunits, Gim-1,3,4 and 6. The alpha class prefoldin subunits are more distantly related.


Pssm-ID: 131391 [Multi-domain]  Cd Length: 110  Bit Score: 40.80  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631632   13 EAIVAQFQQLRNEQRNLVNSLNTLEMDLREHKTVIETLEAADPERKCFRQIGGVLCERTVKEVLPQLVENKDfiakTIQM 92
Cdd:TIGR02338   6 QNQLAQLQQLQQQLQAVATQKQQVEAQLKEAEKALEELERLPDDTPVYKSVGNLLVKTDKEEAIQELKEKKE----TLEL 81

                          90       100
                  ....*....|....*....|....
gi 442631632   93 VTNDLSKKGSELNKFKEEHNIKIR 116
Cdd:TIGR02338  82 RVKTLQRQEERLREQLKELQEKIQ 105
Prefoldin cd00890
prefoldin; Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and ...
 25-101 2.86e-05

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: 40.01  E-value: 2.86e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442631632  25 EQRNLVNSLNTLEMDLREHKTVIETLEAADPE-RKCFRQIGGVLCERTVKEVLPQLVENKDFIAKTIQMVTNDLSKKG 101
Cdd:cd00890    1 QVQALSQQIEQLNRQINELEEALDELSNLDKDtEEVYRSVGGVFIEKSKEETKEELEEKLDELQKEIKKLEQQLEAKT 78
Prefoldin_6 cd23161
Prefoldin subunit 6; Prefoldin subunit 6 is one of the beta subunits of the eukaryotic ...
 16-110 2.18e-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: 38.23  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631632  16 VAQFQQLRNEQRNLVNSLNTLEMDLREHKTVIETLEAADPERKCFRQIGGVLCERTVKEVLpQLVENK-DFIAKTIQMVT 94
Cdd:cd23161    1 SKEFQKLQKELQKLVEARQQLEAQLNENEMVKKELDLLEDDAKVYKLIGPVLVKQDLDEAK-SNVDKRlEFITGEIKRVE 79

                         90
                 ....*....|....*.
gi 442631632  95 NDLSKKGSELNKFKEE 110
Cdd:cd23161   80 KQIKDLEKKQEKKREK 95
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH