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Conserved domains on  [gi|530417471|ref|XP_005259419|]
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unconventional prefoldin RPB5 interactor 1 isoform X1 [Homo sapiens]

Protein Classification

prefoldin domain-containing protein( domain architecture ID 2200)

prefoldin domain-containing protein may function as a molecular chaperone 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_URI1 cd23159
RNA polymerase II subunit 5-mediating protein homolog; URI (also called RNA polymerase II ...
 14-135 1.65e-59

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: 192.38  E-value: 1.65e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417471  14 KRALAYALvvTNCQERIQHWKKVDNDYNALRERLSTLPDKLSYNIMVPFGPFAFMPGKLVHTNEVTVLLGDNWFAKCSAK 93
Cdd:cd23159    5 QEELEKAL--EETEEKIEQWEKYKKEYEALKERLETLPDKLSHDVMVPFGKLAFMPGKLVHTNEILVLLGDNYFVERSAK 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 530417471  94 QAVGLVEHRKEHVRKTIDDLKKVMKNFESRVEFTEDLQKMSD 135
Cdd:cd23159   83 QAIEIIERRIKFLEEKLEKLEKELKLLESRLELTSELLAESE 124
 
Name Accession Description Interval E-value
Prefoldin_URI1 cd23159
RNA polymerase II subunit 5-mediating protein homolog; URI (also called RNA polymerase II ...
 14-135 1.65e-59

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: 192.38  E-value: 1.65e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417471  14 KRALAYALvvTNCQERIQHWKKVDNDYNALRERLSTLPDKLSYNIMVPFGPFAFMPGKLVHTNEVTVLLGDNWFAKCSAK 93
Cdd:cd23159    5 QEELEKAL--EETEEKIEQWEKYKKEYEALKERLETLPDKLSHDVMVPFGKLAFMPGKLVHTNEILVLLGDNYFVERSAK 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 530417471  94 QAVGLVEHRKEHVRKTIDDLKKVMKNFESRVEFTEDLQKMSD 135
Cdd:cd23159   83 QAIEIIERRIKFLEEKLEKLEKELKLLESRLELTSELLAESE 124
Prefoldin pfam02996
Prefoldin subunit; This family comprises of several prefoldin subunits. The biogenesis of the ...
 27-129 1.36e-11

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: 61.50  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417471   27 QERIQHWKKVDNDYNALRERLSTLPD-KLSYNIMVPFGPFAFMPGKLVHTNEVTVLLGDNWFAKCSAKQAVGLVEHRKEH 105
Cdd:pfam02996   9 QAELARLREAIEELEKSLETLKTLKKeDEGKEVLVPLGAGLYVKAEVIDTDKVLVDLGAGYYVEKSLEEAIEILDKRIEE 88

                          90       100
                  ....*....|....*....|....
gi 530417471  106 VRKTIDDLKKVMKNFESRVEFTED 129
Cdd:pfam02996  89 LEKQLEKLEEELEKLKDQITTLEA 112
TIGR00293 TIGR00293
prefoldin, archaeal alpha subunit/eukaryotic subunit 5; Members of this protein family, rich ...
 27-147 3.84e-06

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: 46.12  E-value: 3.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417471   27 QERIQHWKKVDNDYNALRERLSTLPDKLSYNIMVPFGPFAFMPGKLVHTNEVTVLLGDNWFAKCSAKQAVGLVEHRKEHV 106
Cdd:TIGR00293  19 QAQIAALRALIAELETAIETLEDLKGAEGKETLVPVGAGSFVKAKVKDTDKVLVSIGSGYYVEKDAEEAIEFLKKRIEEL 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 530417471  107 RKTIDDLkkvmknfesrvefTEDLQKMSDAAGDIVDIREEI 147
Cdd:TIGR00293  99 EKAIEKL-------------QEALAELASRAQQLEQEAQQL 126
 
Name Accession Description Interval E-value
Prefoldin_URI1 cd23159
RNA polymerase II subunit 5-mediating protein homolog; URI (also called RNA polymerase II ...
 14-135 1.65e-59

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: 192.38  E-value: 1.65e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417471  14 KRALAYALvvTNCQERIQHWKKVDNDYNALRERLSTLPDKLSYNIMVPFGPFAFMPGKLVHTNEVTVLLGDNWFAKCSAK 93
Cdd:cd23159    5 QEELEKAL--EETEEKIEQWEKYKKEYEALKERLETLPDKLSHDVMVPFGKLAFMPGKLVHTNEILVLLGDNYFVERSAK 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 530417471  94 QAVGLVEHRKEHVRKTIDDLKKVMKNFESRVEFTEDLQKMSD 135
Cdd:cd23159   83 QAIEIIERRIKFLEEKLEKLEKELKLLESRLELTSELLAESE 124
Prefoldin_alpha cd00584
Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, ...
 38-131 8.34e-13

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: 64.94  E-value: 8.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417471  38 NDYNALRERLSTLPDKLSyNIMVPFGPFAFMPGKLVHTNEVTVLLGDNWFAKCSAKQAVGLVEHRKEHVRKTIDDLKKVM 117
Cdd:cd00584   27 AEIDEAKEALEELKKEGS-EVLVPLGGNAYVRAEVVDIDKVIVHLGLGYYAERDPDGAIEILEKKEDELDKRIEELQAEL 105

                         90
                 ....*....|....
gi 530417471 118 KNFESRVEFTEDLQ 131
Cdd:cd00584  106 AELEDEYDQLEQQA 119
Prefoldin pfam02996
Prefoldin subunit; This family comprises of several prefoldin subunits. The biogenesis of the ...
 27-129 1.36e-11

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: 61.50  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417471   27 QERIQHWKKVDNDYNALRERLSTLPD-KLSYNIMVPFGPFAFMPGKLVHTNEVTVLLGDNWFAKCSAKQAVGLVEHRKEH 105
Cdd:pfam02996   9 QAELARLREAIEELEKSLETLKTLKKeDEGKEVLVPLGAGLYVKAEVIDTDKVLVDLGAGYYVEKSLEEAIEILDKRIEE 88

                          90       100
                  ....*....|....*....|....
gi 530417471  106 VRKTIDDLKKVMKNFESRVEFTED 129
Cdd:pfam02996  89 LEKQLEKLEEELEKLKDQITTLEA 112
TIGR00293 TIGR00293
prefoldin, archaeal alpha subunit/eukaryotic subunit 5; Members of this protein family, rich ...
 27-147 3.84e-06

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: 46.12  E-value: 3.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417471   27 QERIQHWKKVDNDYNALRERLSTLPDKLSYNIMVPFGPFAFMPGKLVHTNEVTVLLGDNWFAKCSAKQAVGLVEHRKEHV 106
Cdd:TIGR00293  19 QAQIAALRALIAELETAIETLEDLKGAEGKETLVPVGAGSFVKAKVKDTDKVLVSIGSGYYVEKDAEEAIEFLKKRIEEL 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 530417471  107 RKTIDDLkkvmknfesrvefTEDLQKMSDAAGDIVDIREEI 147
Cdd:TIGR00293  99 EKAIEKL-------------QEALAELASRAQQLEQEAQQL 126
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 38-125 1.11e-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: 42.09  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417471  38 NDYNALRERLSTLPD-KLSYNIMVPFGPFAFMPGKLVHTNEVTVLLGDNWFAKCSAKQAVGLVEHRKEHVRKTIDDLKKV 116
Cdd:cd23160   31 NELNRAKETLEELKKlKEGTEILVPIGGGSFVKAKIKDTDKVLVNIGAGVVVEKTIDEAIEILEKRIKELEKALEKLQEQ 110


                 ....*....
gi 530417471 117 MKNFESRVE 125
Cdd:cd23160  111 LQQIAQRLE 119
Prefoldin_5 cd23157
Prefoldin subunit 5; Prefoldin subunit 5 is one of the alpha subunits of the eukaryotic ...
 23-118 2.17e-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: 38.23  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417471  23 VTNCQERIQHWKKVDNDYNALRERLSTL-PDKLSYNIMVPFGPFAFMPGKLVHTNEVTVLLGDNWFAKCSAKQAVGLVEH 101
Cdd:cd23157   13 LEHLTSSLQQLKTAQAKFKESKEALEQLkKENEGKEILVPLTSSLYVPGKLSDVDKVLVDIGTGYYVEKSVEDAKDYFKR 92

                         90
                 ....*....|....*..
gi 530417471 102 RKEHVRKTIDDLKKVMK 118
Cdd:cd23157   93 KIEFLNEQIEKLQKILQ 109
 
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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