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Conserved domains on  [gi|17506241|ref|NP_491870|]
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Unconventional prefoldin RPB5 interactor [Caenorhabditis elegans]

Protein Classification

prefoldin subunit alpha family protein( domain architecture ID 10503232)

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
PubMed:  9630229|33137104

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 ...
 9-128 3.17e-19

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: 83.07  E-value: 3.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506241     9 CNAAKARLEVETECRRIIADNYEKVLERAKEYSK-KLEAPILAKICEVGYFCGAhVVRTNQVTMEMGANYYGECSIHTAE 87
Cdd:pfam02996   1 YKQEIESLQAELARLREAIEELEKSLETLKTLKKeDEGKEVLVPLGAGLYVKAE-VIDTDKVLVDLGAGYYVEKSLEEAI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 17506241    88 KILDRRVSEMRRQREEGLDSIRMLDDKIKFAQDNFSSVSID 128
Cdd:pfam02996  80 EILDKRIEELEKQLEKLEEELEKLKDQITTLEANLQQVQQK 120
 
Name Accession Description Interval E-value
Prefoldin pfam02996
Prefoldin subunit; This family comprises of several prefoldin subunits. The biogenesis of the ...
 9-128 3.17e-19

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: 83.07  E-value: 3.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506241     9 CNAAKARLEVETECRRIIADNYEKVLERAKEYSK-KLEAPILAKICEVGYFCGAhVVRTNQVTMEMGANYYGECSIHTAE 87
Cdd:pfam02996   1 YKQEIESLQAELARLREAIEELEKSLETLKTLKKeDEGKEVLVPLGAGLYVKAE-VIDTDKVLVDLGAGYYVEKSLEEAI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 17506241    88 KILDRRVSEMRRQREEGLDSIRMLDDKIKFAQDNFSSVSID 128
Cdd:pfam02996  80 EILDKRIEELEKQLEKLEEELEKLKDQITTLEANLQQVQQK 120
Prefoldin_URI1 cd23159
RNA polymerase II subunit 5-mediating protein homolog; URI (also called RNA polymerase II ...
 1-124 2.05e-09

RNA polymerase II subunit 5-mediating protein homolog; URI (also called RNA polymerase II fifth subunit regulatory protein or RMP) is an alpha subunit of prefoldin-like complex (PFDL). PFDL is involved in the cytoplasmic assembly of RNA polymerase II and can interact with other chaperone complexes, like R2TP to form the PAQosome. In the cytoplasm, URI acts as a chaperone protein; in the nucleus, URI acts as a transcription regulator and can interact with RPB5 (a subunit of eukaryotic RNA polymerases) and RNA polymerase II (pol II). 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: 467475  Cd Length: 124  Bit Score: 55.25  E-value: 2.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506241   1 MSELYVAECNAAKARLEVETECRRIIADnYEKVLERAKEYSKKLEAPILAKICEVGYFCGaHVVRTNQVTMEMGANYYGE 80
Cdd:cd23159   1 LQRLQEELEKALEETEEKIEQWEKYKKE-YEALKERLETLPDKLSHDVMVPFGKLAFMPG-KLVHTNEILVLLGDNYFVE 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 17506241  81 CSIHTAEKILDRRVSEMRRQREEGLDSIRMLDDKIKFAQDNFSS 124
Cdd:cd23159  79 RSAKQAIEIIERRIKFLEEKLEKLEKELKLLESRLELTSELLAE 122
 
Name Accession Description Interval E-value
Prefoldin pfam02996
Prefoldin subunit; This family comprises of several prefoldin subunits. The biogenesis of the ...
 9-128 3.17e-19

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: 83.07  E-value: 3.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506241     9 CNAAKARLEVETECRRIIADNYEKVLERAKEYSK-KLEAPILAKICEVGYFCGAhVVRTNQVTMEMGANYYGECSIHTAE 87
Cdd:pfam02996   1 YKQEIESLQAELARLREAIEELEKSLETLKTLKKeDEGKEVLVPLGAGLYVKAE-VIDTDKVLVDLGAGYYVEKSLEEAI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 17506241    88 KILDRRVSEMRRQREEGLDSIRMLDDKIKFAQDNFSSVSID 128
Cdd:pfam02996  80 EILDKRIEELEKQLEKLEEELEKLKDQITTLEANLQQVQQK 120
Prefoldin_URI1 cd23159
RNA polymerase II subunit 5-mediating protein homolog; URI (also called RNA polymerase II ...
 1-124 2.05e-09

RNA polymerase II subunit 5-mediating protein homolog; URI (also called RNA polymerase II fifth subunit regulatory protein or RMP) is an alpha subunit of prefoldin-like complex (PFDL). PFDL is involved in the cytoplasmic assembly of RNA polymerase II and can interact with other chaperone complexes, like R2TP to form the PAQosome. In the cytoplasm, URI acts as a chaperone protein; in the nucleus, URI acts as a transcription regulator and can interact with RPB5 (a subunit of eukaryotic RNA polymerases) and RNA polymerase II (pol II). 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: 467475  Cd Length: 124  Bit Score: 55.25  E-value: 2.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506241   1 MSELYVAECNAAKARLEVETECRRIIADnYEKVLERAKEYSKKLEAPILAKICEVGYFCGaHVVRTNQVTMEMGANYYGE 80
Cdd:cd23159   1 LQRLQEELEKALEETEEKIEQWEKYKKE-YEALKERLETLPDKLSHDVMVPFGKLAFMPG-KLVHTNEILVLLGDNYFVE 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 17506241  81 CSIHTAEKILDRRVSEMRRQREEGLDSIRMLDDKIKFAQDNFSS 124
Cdd:cd23159  79 RSAKQAIEIIERRIKFLEEKLEKLEKELKLLESRLELTSELLAE 122
 
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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