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Conserved domains on  [gi|20130365|ref|NP_611933|]
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unconventional prefoldin RPB5 interactor [Drosophila melanogaster]

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_URI1 cd23159
RNA polymerase II subunit 5-mediating protein homolog; URI (also called RNA polymerase II ...
 1-113 2.25e-37

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: 135.76  E-value: 2.25e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130365   1 MDRREDALLQALQTNASETERWEAFKRDNESTIRNLDKFAKNLSVEVMVPIGRKALMPGELIHTNELLVGHYEGYFSACS 80
Cdd:cd23159   1 LQRLQEELEKALEETEEKIEQWEKYKKEYEALKERLETLPDKLSHDVMVPFGKLAFMPGKLVHTNEILVLLGDNYFVERS 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 20130365  81 SHKAKEICQYRLKLAEEQLKKLAVENDLWQKKL 113
Cdd:cd23159  81 AKQAIEIIERRIKFLEEKLEKLEKELKLLESRL 113
PTZ00121 super family cl31754
MAEBL; Provisional
 144-271 2.57e-03

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130365   144 AEHRKRMRQQKQKERLEREAEPVKKDNEVLRKLEEREMMEELGLDPDNIDEDQLHDMLNQEPLKSTNESSPKSLTQEEED 223
Cdd:PTZ00121 1226 AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD 1305

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 20130365   224 ELWKKleAEEQNEADELSSEAEESLKTTDNLVRQLMSGETETPSSKKR 271
Cdd:PTZ00121 1306 EAKKK--AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE 1351
 
Name Accession Description Interval E-value
Prefoldin_URI1 cd23159
RNA polymerase II subunit 5-mediating protein homolog; URI (also called RNA polymerase II ...
 1-113 2.25e-37

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: 135.76  E-value: 2.25e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130365   1 MDRREDALLQALQTNASETERWEAFKRDNESTIRNLDKFAKNLSVEVMVPIGRKALMPGELIHTNELLVGHYEGYFSACS 80
Cdd:cd23159   1 LQRLQEELEKALEETEEKIEQWEKYKKEYEALKERLETLPDKLSHDVMVPFGKLAFMPGKLVHTNEILVLLGDNYFVERS 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 20130365  81 SHKAKEICQYRLKLAEEQLKKLAVENDLWQKKL 113
Cdd:cd23159  81 AKQAIEIIERRIKFLEEKLEKLEKELKLLESRL 113
Prefoldin pfam02996
Prefoldin subunit; This family comprises of several prefoldin subunits. The biogenesis of the ...
 8-126 9.34e-23

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: 93.86  E-value: 9.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130365     8 LLQALQTNASETERWEAFKRDNESTIRNLDKFAK-NLSVEVMVPIGRKALMPGELIHTNELLVGHYEGYFSACSSHKAKE 86
Cdd:pfam02996   1 YKQEIESLQAELARLREAIEELEKSLETLKTLKKeDEGKEVLVPLGAGLYVKAEVIDTDKVLVDLGAGYYVEKSLEEAIE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 20130365    87 ICQYRLKLAEEQLKKLAVENDLWQKKLHTPFAEGAVPSGD 126
Cdd:pfam02996  81 ILDKRIEELEKQLEKLEEELEKLKDQITTLEANLQQVQQK 120
TIGR00293 TIGR00293
prefoldin, archaeal alpha subunit/eukaryotic subunit 5; Members of this protein family, rich ...
 6-102 3.38e-05

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: 43.81  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130365     6 DALLQALQtnaSETERWEAFKRDNESTIRNLDKFAKNLSVEVMVPIGRKALMPGELIHTNELLVGHYEGYFSACSSHKAK 85
Cdd:TIGR00293  12 QQQVESLQ---AQIAALRALIAELETAIETLEDLKGAEGKETLVPVGAGSFVKAKVKDTDKVLVSIGSGYYVEKDAEEAI 88

                          90
                  ....*....|....*..
gi 20130365    86 EICQYRLKLAEEQLKKL 102
Cdd:TIGR00293  89 EFLKKRIEELEKAIEKL 105
PTZ00121 PTZ00121
MAEBL; Provisional
 144-271 2.57e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130365   144 AEHRKRMRQQKQKERLEREAEPVKKDNEVLRKLEEREMMEELGLDPDNIDEDQLHDMLNQEPLKSTNESSPKSLTQEEED 223
Cdd:PTZ00121 1226 AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD 1305

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 20130365   224 ELWKKleAEEQNEADELSSEAEESLKTTDNLVRQLMSGETETPSSKKR 271
Cdd:PTZ00121 1306 EAKKK--AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE 1351
 
Name Accession Description Interval E-value
Prefoldin_URI1 cd23159
RNA polymerase II subunit 5-mediating protein homolog; URI (also called RNA polymerase II ...
 1-113 2.25e-37

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: 135.76  E-value: 2.25e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130365   1 MDRREDALLQALQTNASETERWEAFKRDNESTIRNLDKFAKNLSVEVMVPIGRKALMPGELIHTNELLVGHYEGYFSACS 80
Cdd:cd23159   1 LQRLQEELEKALEETEEKIEQWEKYKKEYEALKERLETLPDKLSHDVMVPFGKLAFMPGKLVHTNEILVLLGDNYFVERS 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 20130365  81 SHKAKEICQYRLKLAEEQLKKLAVENDLWQKKL 113
Cdd:cd23159  81 AKQAIEIIERRIKFLEEKLEKLEKELKLLESRL 113
Prefoldin pfam02996
Prefoldin subunit; This family comprises of several prefoldin subunits. The biogenesis of the ...
 8-126 9.34e-23

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: 93.86  E-value: 9.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130365     8 LLQALQTNASETERWEAFKRDNESTIRNLDKFAK-NLSVEVMVPIGRKALMPGELIHTNELLVGHYEGYFSACSSHKAKE 86
Cdd:pfam02996   1 YKQEIESLQAELARLREAIEELEKSLETLKTLKKeDEGKEVLVPLGAGLYVKAEVIDTDKVLVDLGAGYYVEKSLEEAIE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 20130365    87 ICQYRLKLAEEQLKKLAVENDLWQKKLHTPFAEGAVPSGD 126
Cdd:pfam02996  81 ILDKRIEELEKQLEKLEEELEKLKDQITTLEANLQQVQQK 120
TIGR00293 TIGR00293
prefoldin, archaeal alpha subunit/eukaryotic subunit 5; Members of this protein family, rich ...
 6-102 3.38e-05

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: 43.81  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130365     6 DALLQALQtnaSETERWEAFKRDNESTIRNLDKFAKNLSVEVMVPIGRKALMPGELIHTNELLVGHYEGYFSACSSHKAK 85
Cdd:TIGR00293  12 QQQVESLQ---AQIAALRALIAELETAIETLEDLKGAEGKETLVPVGAGSFVKAKVKDTDKVLVSIGSGYYVEKDAEEAI 88

                          90
                  ....*....|....*..
gi 20130365    86 EICQYRLKLAEEQLKKL 102
Cdd:TIGR00293  89 EFLKKRIEELEKAIEKL 105
Prefoldin_alpha cd00584
Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, ...
 9-102 9.42e-05

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: 42.60  E-value: 9.42e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130365   9 LQALQTnasETERWEAFKRDNESTIRNLDKFAKNLSvEVMVPIGRKALMPGELIHTNELLVGHYEGYFSACSSHKAKEIC 88
Cdd:cd00584  12 IEALQE---EIEQLEEEQAEIDEAKEALEELKKEGS-EVLVPLGGNAYVRAEVVDIDKVIVHLGLGYYAERDPDGAIEIL 87

                        90
                ....*....|....
gi 20130365  89 QYRLKLAEEQLKKL 102
Cdd:cd00584  88 EKKEDELDKRIEEL 101
PTZ00121 PTZ00121
MAEBL; Provisional
 144-271 2.57e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130365   144 AEHRKRMRQQKQKERLEREAEPVKKDNEVLRKLEEREMMEELGLDPDNIDEDQLHDMLNQEPLKSTNESSPKSLTQEEED 223
Cdd:PTZ00121 1226 AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD 1305

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 20130365   224 ELWKKleAEEQNEADELSSEAEESLKTTDNLVRQLMSGETETPSSKKR 271
Cdd:PTZ00121 1306 EAKKK--AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE 1351
PTZ00121 PTZ00121
MAEBL; Provisional
 122-254 9.08e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 9.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130365   122 VPSGDQVEIVEDFNEESHNKWLAEHRKRMRQQKQKERLEREAEPVKKDNEVLRKLEEREMMEElglDPDNIDEDQLHDML 201
Cdd:PTZ00121 1283 LKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA---EAAKAEAEAAADEA 1359

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 20130365   202 NQEPLKSTNESSPKSLTQEEEDELWKKleAEEQNEADELSSEAEESLKTTDNL 254
Cdd:PTZ00121 1360 EAAEEKAEAAEKKKEEAKKKADAAKKK--AEEKKKADEAKKKAEEDKKKADEL 1410
 
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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