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Conserved domains on  [gi|4507873|ref|NP_003363|]
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prefoldin subunit 3 isoform 1 [Homo sapiens]

Protein Classification

prefoldin subunit alpha family protein( domain architecture ID 19227067)

prefoldin subunit alpha is an alpha subunit of prefoldin, a hexameric co-chaperone prefoldin complex that binds and stabilizes newly synthesized polypeptides, allowing them to fold correctly

Gene Ontology:  GO:0016272|GO:0006457|GO:0051082|GO:0016272|GO:0006457|GO:0051082
PubMed:  11106732|33137104|9630229|9630229|33137104

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Prefoldin_3 cd23156
Prefoldin subunit 3; Prefoldin subunit 3 is one of the alpha subunits of the eukaryotic ...
 52-180 3.77e-76

Prefoldin subunit 3; Prefoldin subunit 3 is one of the alpha 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: 467472  Cd Length: 129  Bit Score: 224.27  E-value: 3.77e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507873   52 KLDEQYQKYKFMELNLAQKKRRLKGQIPEIKQTLEILKYMQKKKESTNSMETRFLLADNLYCKASVPPTDKVCLWLGANV 131
Cdd:cd23156   1 KLQELYSKYKFMEASLLQKKARLKEKIPDIKKTLEAVKFLKKKKEEGEELETHFELADTVYAKATVPPTDKVCLWLGANV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 4507873  132 MLEYDIDEAQALLEKNLSTATKNLDSLEEDLDFLRDQFTTTEVNMARVY 180
Cdd:cd23156  81 MLEYPLDEAEELLEKNLATAKKSLKELEEDLEFLRDQITTTEVNIARVY 129
 
Name Accession Description Interval E-value
Prefoldin_3 cd23156
Prefoldin subunit 3; Prefoldin subunit 3 is one of the alpha subunits of the eukaryotic ...
 52-180 3.77e-76

Prefoldin subunit 3; Prefoldin subunit 3 is one of the alpha 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: 467472  Cd Length: 129  Bit Score: 224.27  E-value: 3.77e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507873   52 KLDEQYQKYKFMELNLAQKKRRLKGQIPEIKQTLEILKYMQKKKESTNSMETRFLLADNLYCKASVPPTDKVCLWLGANV 131
Cdd:cd23156   1 KLQELYSKYKFMEASLLQKKARLKEKIPDIKKTLEAVKFLKKKKEEGEELETHFELADTVYAKATVPPTDKVCLWLGANV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 4507873  132 MLEYDIDEAQALLEKNLSTATKNLDSLEEDLDFLRDQFTTTEVNMARVY 180
Cdd:cd23156  81 MLEYPLDEAEELLEKNLATAKKSLKELEEDLEFLRDQITTTEVNIARVY 129
Prefoldin pfam02996
Prefoldin subunit; This family comprises of several prefoldin subunits. The biogenesis of the ...
 60-182 6.18e-35

Prefoldin subunit; This family comprises of several prefoldin subunits. The biogenesis of the cytoskeletal proteins actin and tubulin involves interaction of nascent chains of each of the two proteins with the oligomeric protein prefoldin (PFD) and their subsequent transfer to the cytosolic chaperonin CCT (chaperonin containing TCP-1). Electron microscopy shows that eukaryotic PFD, which has a similar structure to its archaeal counterpart, interacts with unfolded actin along the tips of its projecting arms. In its PFD-bound state, actin seems to acquire a conformation similar to that adopted when it is bound to CCT.


Pssm-ID: 427096 [Multi-domain]  Cd Length: 120  Bit Score: 119.28  E-value: 6.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507873     60 YKFMELNLAQKKRRLKGQIPEIKQTLEILKYMQKKKEStnsMETRFLLADNLYCKASVPPTDKVCLWLGANVMLEYDIDE 139
Cdd:pfam02996   1 YKQEIESLQAELARLREAIEELEKSLETLKTLKKEDEG---KEVLVPLGAGLYVKAEVIDTDKVLVDLGAGYYVEKSLEE 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 4507873    140 AQALLEKNLSTATKNLDSLEEDLDFLRDQFTTTEVNMARVYNW 182
Cdd:pfam02996  78 AIEILDKRIEELEKQLEKLEEELEKLKDQITTLEANLQQVQQK 120
GIM5 COG1730
Prefoldin subunit 5 [Posttranslational modification, protein turnover, chaperones];
50-168 5.57e-07

Prefoldin subunit 5 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441336 [Multi-domain]  Cd Length: 145  Bit Score: 47.21  E-value: 5.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507873   50 LKKLDEQYQKYK-FMELnLAQKKRRLKGQIPEIKQTLEILKYMQKKKEStnsmETRFLLADNLYCKASVPPTDKVCLWLG 128
Cdd:COG1730  10 LQQLLQQLQELEaQIEA-LQQQIELLQASIEELDAAIETLEALKSGEGS----EVLVPLGGGAFVKAKVKDKDKVIVSLG 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 4507873  129 ANVMLEYDIDEAQALLEKNLSTATKNLDSLEEDLDFLRDQ 168
Cdd:COG1730  85 AGVAVEKDLDEAIEYLEKRIKELEKALEKLEEELQELEEE 124
TIGR00293 TIGR00293
prefoldin, archaeal alpha subunit/eukaryotic subunit 5; Members of this protein family, rich ...
 50-168 2.88e-04

prefoldin, archaeal alpha subunit/eukaryotic subunit 5; Members of this protein family, rich in coiled coil regions, are molecular chaperones in the class of the prefoldin (GimC) alpha subunit. Prefoldin is a hexamer of two alpha and four beta subunits. This protein appears universal in the archaea but is restricted to Aquifex aeolicus among bacteria so far. Eukaryotes have several related proteins; only prefoldin subunit 5, which appeared the most similar to archaeal prefoldin alpha, is included in this model. This model finds a set of small proteins from the Archaea and from Aquifex aeolicus that may represent two orthologous groups. The proteins are predicted to be mostly coiled coil, and the model may have a significant number of hits to proteins that contain coiled coil regions. [Protein fate, Protein folding and stabilization]


Pssm-ID: 129394 [Multi-domain]  Cd Length: 126  Bit Score: 39.18  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507873     50 LKKLDEQYQKYKfMELN-LAQKKRRLKGQIPEIKQTLEILKYMQKKKestnSMETRFLLADNLYCKASVPPTDKVCLWLG 128
Cdd:TIGR00293   1 LQQLAAELQILQ-QQVEsLQAQIAALRALIAELETAIETLEDLKGAE----GKETLVPVGAGSFVKAKVKDTDKVLVSIG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 4507873    129 ANVMLEYDIDEAQALLEKNLSTATKNLDSLEEDLDFLRDQ 168
Cdd:TIGR00293  76 SGYYVEKDAEEAIEFLKKRIEELEKAIEKLQEALAELASR 115
 
Name Accession Description Interval E-value
Prefoldin_3 cd23156
Prefoldin subunit 3; Prefoldin subunit 3 is one of the alpha subunits of the eukaryotic ...
 52-180 3.77e-76

Prefoldin subunit 3; Prefoldin subunit 3 is one of the alpha 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: 467472  Cd Length: 129  Bit Score: 224.27  E-value: 3.77e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507873   52 KLDEQYQKYKFMELNLAQKKRRLKGQIPEIKQTLEILKYMQKKKESTNSMETRFLLADNLYCKASVPPTDKVCLWLGANV 131
Cdd:cd23156   1 KLQELYSKYKFMEASLLQKKARLKEKIPDIKKTLEAVKFLKKKKEEGEELETHFELADTVYAKATVPPTDKVCLWLGANV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 4507873  132 MLEYDIDEAQALLEKNLSTATKNLDSLEEDLDFLRDQFTTTEVNMARVY 180
Cdd:cd23156  81 MLEYPLDEAEELLEKNLATAKKSLKELEEDLEFLRDQITTTEVNIARVY 129
Prefoldin pfam02996
Prefoldin subunit; This family comprises of several prefoldin subunits. The biogenesis of the ...
 60-182 6.18e-35

Prefoldin subunit; This family comprises of several prefoldin subunits. The biogenesis of the cytoskeletal proteins actin and tubulin involves interaction of nascent chains of each of the two proteins with the oligomeric protein prefoldin (PFD) and their subsequent transfer to the cytosolic chaperonin CCT (chaperonin containing TCP-1). Electron microscopy shows that eukaryotic PFD, which has a similar structure to its archaeal counterpart, interacts with unfolded actin along the tips of its projecting arms. In its PFD-bound state, actin seems to acquire a conformation similar to that adopted when it is bound to CCT.


Pssm-ID: 427096 [Multi-domain]  Cd Length: 120  Bit Score: 119.28  E-value: 6.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507873     60 YKFMELNLAQKKRRLKGQIPEIKQTLEILKYMQKKKEStnsMETRFLLADNLYCKASVPPTDKVCLWLGANVMLEYDIDE 139
Cdd:pfam02996   1 YKQEIESLQAELARLREAIEELEKSLETLKTLKKEDEG---KEVLVPLGAGLYVKAEVIDTDKVLVDLGAGYYVEKSLEE 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 4507873    140 AQALLEKNLSTATKNLDSLEEDLDFLRDQFTTTEVNMARVYNW 182
Cdd:pfam02996  78 AIEILDKRIEELEKQLEKLEEELEKLKDQITTLEANLQQVQQK 120
Prefoldin_alpha cd00584
Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, ...
 53-178 3.10e-32

Prefoldin alpha subunit; Alpha 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: 467468 [Multi-domain]  Cd Length: 121  Bit Score: 112.71  E-value: 3.10e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507873   53 LDEQYQKYKFMELNLAQKKRRLKGQIPEIKQTLEILKYMQKKKestnsMETRFLLADNLYCKASVPPTDKVCLWLGANVM 132
Cdd:cd00584   1 LAEQLQELREQIEALQEEIEQLEEEQAEIDEAKEALEELKKEG-----SEVLVPLGGNAYVRAEVVDIDKVIVHLGLGYY 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 4507873  133 LEYDIDEAQALLEKNLSTATKNLDSLEEDLDFLRDQFTTTEVNMAR 178
Cdd:cd00584  76 AERDPDGAIEILEKKEDELDKRIEELQAELAELEDEYDQLEQQAQQ 121
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 50-168 8.26e-08

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: 49.02  E-value: 8.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507873   50 LKKLDEQYQKYK-FMElNLAQKKRRLKGQIPEIKQTLEILKYMQKKKESTnsmETRFLLADNLYCKASVPPTDKVCLWLG 128
Cdd:cd23160   2 LQRLLAELQQLEqQAE-ALQQQIELLQASINELNRAKETLEELKKLKEGT---EILVPIGGGSFVKAKIKDTDKVLVNIG 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 4507873  129 ANVMLEYDIDEAQALLEKNLSTATKNLDSLEEDLDFLRDQ 168
Cdd:cd23160  78 AGVVVEKTIDEAIEILEKRIKELEKALEKLQEQLQQIAQR 117
GIM5 COG1730
Prefoldin subunit 5 [Posttranslational modification, protein turnover, chaperones];
50-168 5.57e-07

Prefoldin subunit 5 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441336 [Multi-domain]  Cd Length: 145  Bit Score: 47.21  E-value: 5.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507873   50 LKKLDEQYQKYK-FMELnLAQKKRRLKGQIPEIKQTLEILKYMQKKKEStnsmETRFLLADNLYCKASVPPTDKVCLWLG 128
Cdd:COG1730  10 LQQLLQQLQELEaQIEA-LQQQIELLQASIEELDAAIETLEALKSGEGS----EVLVPLGGGAFVKAKVKDKDKVIVSLG 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 4507873  129 ANVMLEYDIDEAQALLEKNLSTATKNLDSLEEDLDFLRDQ 168
Cdd:COG1730  85 AGVAVEKDLDEAIEYLEKRIKELEKALEKLEEELQELEEE 124
Prefoldin_UXT cd23158
protein UXT; UXT is an alpha subunit of the prefoldin-like complex (PFDL). PFDL is involved in ...
 64-168 9.88e-07

protein UXT; UXT is an alpha subunit of the prefoldin-like complex (PFDL). PFDL is involved in the cytoplasmic assembly of RNA polymerase I and can interact with other chaperone complexes, like R2TP, to form the PAQosome. UXT has an important role in the activation of the NF-kappaB pathway. UXT is also a component of the centrosome and is associated with gamma-tubulin. 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.


Pssm-ID: 467474  Cd Length: 128  Bit Score: 45.95  E-value: 9.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507873   64 ELNLAQKKR-RLKGQIPEIKQTLEILKYMQKKKESTnSMETRFLLADNLYCKASVPPTDKVCLWLGANVMLEYDIDEAQA 142
Cdd:cd23158  12 DLKKVLEERdKLYEEISEYEQLKNTIETLQENDGLK-PLKTLVDLGCNFYVQAKVPDTSKIFVDVGLGFYVEMTLDEALK 90

                        90       100
                ....*....|....*....|....*.
gi 4507873  143 LLEknlstatKNLDSLEEDLDFLRDQ 168
Cdd:cd23158  91 FID-------KKEKLLEKKADKLTKK 109
TIGR00293 TIGR00293
prefoldin, archaeal alpha subunit/eukaryotic subunit 5; Members of this protein family, rich ...
 50-168 2.88e-04

prefoldin, archaeal alpha subunit/eukaryotic subunit 5; Members of this protein family, rich in coiled coil regions, are molecular chaperones in the class of the prefoldin (GimC) alpha subunit. Prefoldin is a hexamer of two alpha and four beta subunits. This protein appears universal in the archaea but is restricted to Aquifex aeolicus among bacteria so far. Eukaryotes have several related proteins; only prefoldin subunit 5, which appeared the most similar to archaeal prefoldin alpha, is included in this model. This model finds a set of small proteins from the Archaea and from Aquifex aeolicus that may represent two orthologous groups. The proteins are predicted to be mostly coiled coil, and the model may have a significant number of hits to proteins that contain coiled coil regions. [Protein fate, Protein folding and stabilization]


Pssm-ID: 129394 [Multi-domain]  Cd Length: 126  Bit Score: 39.18  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507873     50 LKKLDEQYQKYKfMELN-LAQKKRRLKGQIPEIKQTLEILKYMQKKKestnSMETRFLLADNLYCKASVPPTDKVCLWLG 128
Cdd:TIGR00293   1 LQQLAAELQILQ-QQVEsLQAQIAALRALIAELETAIETLEDLKGAE----GKETLVPVGAGSFVKAKVKDTDKVLVSIG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 4507873    129 ANVMLEYDIDEAQALLEKNLSTATKNLDSLEEDLDFLRDQ 168
Cdd:TIGR00293  76 SGYYVEKDAEEAIEFLKKRIEELEKAIEKLQEALAELASR 115
 
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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