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Conserved domains on  [gi|1932796905|emb|CAD6626381|]
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HLJ1_G0050110.mRNA.1.CDS.1 [Saccharomyces cerevisiae]

Protein Classification

prefoldin subunit alpha family protein; prefoldin subunit 5( domain architecture ID 11139890)

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| prefoldin subunit 5 (PFDN5) is an alpha subunit of prefoldin, a hexameric co-chaperone prefoldin complex that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Prefoldin pfam02996
Prefoldin subunit; This family comprises of several prefoldin subunits. The biogenesis of the ...
 8-126 1.17e-15

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: 73.83  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932796905   8 VESTLKNLQDKRNFLSEQREHYIDIRSRLVRFINDNDDGEEERE-GQGMVFGDIIISTSKIYLSLGYEYYVEKTKEEAIT 86
Cdd:pfam02996   1 YKQEIESLQAELARLREAIEELEKSLETLKTLKKEDEGKEVLVPlGAGLYVKAEVIDTDKVLVDLGAGYYVEKSLEEAIE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1932796905  87 FVDDKLKLMEDAIEQFNLKIEEAKKTLDNLNHMEDENGIE 126
Cdd:pfam02996  81 ILDKRIEELEKQLEKLEEELEKLKDQITTLEANLQQVQQK 120
DUF3835 pfam12927
Domain of unknown function (DUF3835); This is a C-terminal domain conserved in fungi.
 709-783 2.86e-14

Domain of unknown function (DUF3835); This is a C-terminal domain conserved in fungi.


:

Pssm-ID: 463753  Cd Length: 73  Bit Score: 68.38  E-value: 2.86e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1932796905 709 DIIEHKFPESYTNDEDEvALHPDRLQEEVAIEYRRLKEATASKwQSSSPAAHTEGELEPIDKFGNPVKTSRFRSQ 783
Cdd:pfam12927   1 TVVERDIPEAAAPPDPD-ELDEELLRREVATEYHRLRNRMIQQ-QGGFLKSDEELEIEPIDEDGNPKKVSRFKAA 73
 
Name Accession Description Interval E-value
Prefoldin pfam02996
Prefoldin subunit; This family comprises of several prefoldin subunits. The biogenesis of the ...
 8-126 1.17e-15

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: 73.83  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932796905   8 VESTLKNLQDKRNFLSEQREHYIDIRSRLVRFINDNDDGEEERE-GQGMVFGDIIISTSKIYLSLGYEYYVEKTKEEAIT 86
Cdd:pfam02996   1 YKQEIESLQAELARLREAIEELEKSLETLKTLKKEDEGKEVLVPlGAGLYVKAEVIDTDKVLVDLGAGYYVEKSLEEAIE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1932796905  87 FVDDKLKLMEDAIEQFNLKIEEAKKTLDNLNHMEDENGIE 126
Cdd:pfam02996  81 ILDKRIEELEKQLEKLEEELEKLKDQITTLEANLQQVQQK 120
DUF3835 pfam12927
Domain of unknown function (DUF3835); This is a C-terminal domain conserved in fungi.
 709-783 2.86e-14

Domain of unknown function (DUF3835); This is a C-terminal domain conserved in fungi.


Pssm-ID: 463753  Cd Length: 73  Bit Score: 68.38  E-value: 2.86e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1932796905 709 DIIEHKFPESYTNDEDEvALHPDRLQEEVAIEYRRLKEATASKwQSSSPAAHTEGELEPIDKFGNPVKTSRFRSQ 783
Cdd:pfam12927   1 TVVERDIPEAAAPPDPD-ELDEELLRREVATEYHRLRNRMIQQ-QGGFLKSDEELEIEPIDEDGNPKKVSRFKAA 73
Prefoldin_UXT cd23158
protein UXT; UXT is an alpha subunit of the prefoldin-like complex (PFDL). PFDL is involved in ...
 12-110 7.32e-09

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: 54.42  E-value: 7.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932796905  12 LKNLQDKRNFLSEQREHYIDIRSrLVRFINDNDDGEEERegqGMVfgDI---------IISTSKIYLSLGYEYYVEKTKE 82
Cdd:cd23158    13 LKKVLEERDKLYEEISEYEQLKN-TIETLQENDGLKPLK---TLV--DLgcnfyvqakVPDTSKIFVDVGLGFYVEMTLD 86

                          90       100
                  ....*....|....*....|....*...
gi 1932796905  83 EAITFVDDKLKLMEDAIEQFNLKIEEAK 110
Cdd:cd23158    87 EALKFIDKKEKLLEKKADKLTKKAAKIK 114
GIM5 COG1730
Prefoldin subunit 5 [Posttranslational modification, protein turnover, chaperones];
61-116 2.97e-04

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


Pssm-ID: 441336 [Multi-domain]  Cd Length: 145  Bit Score: 41.81  E-value: 2.97e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1932796905  61 IISTSKIYLSLGYEYYVEKTKEEAITFVDDKLKLMEDAIEQFNLKIEEAKKTLDNL 116
Cdd:COG1730    73 VKDKDKVIVSLGAGVAVEKDLDEAIEYLEKRIKELEKALEKLEEELQELEEEYEEL 128
TIGR00293 TIGR00293
prefoldin, archaeal alpha subunit/eukaryotic subunit 5; Members of this protein family, rich ...
 64-116 5.04e-03

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: 37.64  E-value: 5.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1932796905  64 TSKIYLSLGYEYYVEKTKEEAITFVDDKLKLMEDAIEQFNLKIEEAKKTLDNL 116
Cdd:TIGR00293  67 TDKVLVSIGSGYYVEKDAEEAIEFLKKRIEELEKAIEKLQEALAELASRAQQL 119
 
Name Accession Description Interval E-value
Prefoldin pfam02996
Prefoldin subunit; This family comprises of several prefoldin subunits. The biogenesis of the ...
 8-126 1.17e-15

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: 73.83  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932796905   8 VESTLKNLQDKRNFLSEQREHYIDIRSRLVRFINDNDDGEEERE-GQGMVFGDIIISTSKIYLSLGYEYYVEKTKEEAIT 86
Cdd:pfam02996   1 YKQEIESLQAELARLREAIEELEKSLETLKTLKKEDEGKEVLVPlGAGLYVKAEVIDTDKVLVDLGAGYYVEKSLEEAIE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1932796905  87 FVDDKLKLMEDAIEQFNLKIEEAKKTLDNLNHMEDENGIE 126
Cdd:pfam02996  81 ILDKRIEELEKQLEKLEEELEKLKDQITTLEANLQQVQQK 120
DUF3835 pfam12927
Domain of unknown function (DUF3835); This is a C-terminal domain conserved in fungi.
 709-783 2.86e-14

Domain of unknown function (DUF3835); This is a C-terminal domain conserved in fungi.


Pssm-ID: 463753  Cd Length: 73  Bit Score: 68.38  E-value: 2.86e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1932796905 709 DIIEHKFPESYTNDEDEvALHPDRLQEEVAIEYRRLKEATASKwQSSSPAAHTEGELEPIDKFGNPVKTSRFRSQ 783
Cdd:pfam12927   1 TVVERDIPEAAAPPDPD-ELDEELLRREVATEYHRLRNRMIQQ-QGGFLKSDEELEIEPIDEDGNPKKVSRFKAA 73
Prefoldin_UXT cd23158
protein UXT; UXT is an alpha subunit of the prefoldin-like complex (PFDL). PFDL is involved in ...
 12-110 7.32e-09

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: 54.42  E-value: 7.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932796905  12 LKNLQDKRNFLSEQREHYIDIRSrLVRFINDNDDGEEERegqGMVfgDI---------IISTSKIYLSLGYEYYVEKTKE 82
Cdd:cd23158    13 LKKVLEERDKLYEEISEYEQLKN-TIETLQENDGLKPLK---TLV--DLgcnfyvqakVPDTSKIFVDVGLGFYVEMTLD 86

                          90       100
                  ....*....|....*....|....*...
gi 1932796905  83 EAITFVDDKLKLMEDAIEQFNLKIEEAK 110
Cdd:cd23158    87 EALKFIDKKEKLLEKKADKLTKKAAKIK 114
GIM5 COG1730
Prefoldin subunit 5 [Posttranslational modification, protein turnover, chaperones];
61-116 2.97e-04

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


Pssm-ID: 441336 [Multi-domain]  Cd Length: 145  Bit Score: 41.81  E-value: 2.97e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1932796905  61 IISTSKIYLSLGYEYYVEKTKEEAITFVDDKLKLMEDAIEQFNLKIEEAKKTLDNL 116
Cdd:COG1730    73 VKDKDKVIVSLGAGVAVEKDLDEAIEYLEKRIKELEKALEKLEEELQELEEEYEEL 128
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 61-116 7.79e-04

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: 40.16  E-value: 7.79e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1932796905  61 IISTSKIYLSLGYEYYVEKTKEEAITFVDDKLKLMEDAIEQFNLKIEEAKKTLDNL 116
Cdd:cd23160    66 IKDTDKVLVNIGAGVVVEKTIDEAIEILEKRIKELEKALEKLQEQLQQIAQRLEEL 121
Prefoldin_5 cd23157
Prefoldin subunit 5; Prefoldin subunit 5 is one of the alpha subunits of the eukaryotic ...
 61-119 1.16e-03

Prefoldin subunit 5; Prefoldin subunit 5 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: 467473  Cd Length: 124  Bit Score: 39.39  E-value: 1.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1932796905  61 IISTSKIYLSLGYEYYVEKTKEEAITFVDDKLKLMEDAIEQFNLKIEEAKKTLDNLNHM 119
Cdd:cd23157    63 LSDVDKVLVDIGTGYYVEKSVEDAKDYFKRKIEFLNEQIEKLQKILQEKQQNLQAVVEV 121
TIGR00293 TIGR00293
prefoldin, archaeal alpha subunit/eukaryotic subunit 5; Members of this protein family, rich ...
 64-116 5.04e-03

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: 37.64  E-value: 5.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1932796905  64 TSKIYLSLGYEYYVEKTKEEAITFVDDKLKLMEDAIEQFNLKIEEAKKTLDNL 116
Cdd:TIGR00293  67 TDKVLVSIGSGYYVEKDAEEAIEFLKKRIEELEKAIEKLQEALAELASRAQQL 119
 
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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