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Conserved domains on  [gi|1965563523|ref|XP_039072717|]
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protein UXT isoform X2 [Hyaena hyaena]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Prefoldin_UXT cd23158
protein UXT; UXT is an alpha subunit of the prefoldin-like complex (PFDL). PFDL is involved in ...
 20-146 4.03e-59

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: 179.61  E-value: 4.03e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965563523  20 YEAFICDVLQRDLRKVLDHRDKVYDQLAKYLQLRNVIERLQEA-KPSELYMQVDLGCNFFVDTVVPDTSRIYVALGYGFF 98
Cdd:cd23158     1 YEAFLNEVLKPDLKKVLEERDKLYEEISEYEQLKNTIETLQENdGLKPLKTLVDLGCNFYVQAKVPDTSKIFVDVGLGFY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1965563523  99 LELTLTEALKFIDRKSSLLTELSDSLTKDSMNIKAHIHMLLEGLRELQ 146
Cdd:cd23158    81 VEMTLDEALKFIDKKEKLLEKKADKLTKKAAKIKAHIKLVLEAIRELQ 128
 
Name Accession Description Interval E-value
Prefoldin_UXT cd23158
protein UXT; UXT is an alpha subunit of the prefoldin-like complex (PFDL). PFDL is involved in ...
 20-146 4.03e-59

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: 179.61  E-value: 4.03e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965563523  20 YEAFICDVLQRDLRKVLDHRDKVYDQLAKYLQLRNVIERLQEA-KPSELYMQVDLGCNFFVDTVVPDTSRIYVALGYGFF 98
Cdd:cd23158     1 YEAFLNEVLKPDLKKVLEERDKLYEEISEYEQLKNTIETLQENdGLKPLKTLVDLGCNFYVQAKVPDTSKIFVDVGLGFY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1965563523  99 LELTLTEALKFIDRKSSLLTELSDSLTKDSMNIKAHIHMLLEGLRELQ 146
Cdd:cd23158    81 VEMTLDEALKFIDKKEKLLEKKADKLTKKAAKIKAHIKLVLEAIRELQ 128
Prefoldin pfam02996
Prefoldin subunit; This family comprises of several prefoldin subunits. The biogenesis of the ...
 28-146 7.24e-14

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: 63.81  E-value: 7.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965563523  28 LQRDLRKVLDHRDKVYDQLAKYLQLRNVIERLQEAKPSELyMQVDLGCNFFVDTVVPDTSRIYVALGYGFFLELTLTEAL 107
Cdd:pfam02996   1 YKQEIESLQAELARLREAIEELEKSLETLKTLKKEDEGKE-VLVPLGAGLYVKAEVIDTDKVLVDLGAGYYVEKSLEEAI 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1965563523 108 KFIDRKSSLLTELSDSLTKDSMNIKAHIHMLLEGLRELQ 146
Cdd:pfam02996  80 EILDKRIEELEKQLEKLEEELEKLKDQITTLEANLQQVQ 118
 
Name Accession Description Interval E-value
Prefoldin_UXT cd23158
protein UXT; UXT is an alpha subunit of the prefoldin-like complex (PFDL). PFDL is involved in ...
 20-146 4.03e-59

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: 179.61  E-value: 4.03e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965563523  20 YEAFICDVLQRDLRKVLDHRDKVYDQLAKYLQLRNVIERLQEA-KPSELYMQVDLGCNFFVDTVVPDTSRIYVALGYGFF 98
Cdd:cd23158     1 YEAFLNEVLKPDLKKVLEERDKLYEEISEYEQLKNTIETLQENdGLKPLKTLVDLGCNFYVQAKVPDTSKIFVDVGLGFY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1965563523  99 LELTLTEALKFIDRKSSLLTELSDSLTKDSMNIKAHIHMLLEGLRELQ 146
Cdd:cd23158    81 VEMTLDEALKFIDKKEKLLEKKADKLTKKAAKIKAHIKLVLEAIRELQ 128
Prefoldin_alpha cd00584
Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, ...
 26-144 9.39e-20

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: 79.19  E-value: 9.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965563523  26 DVLQRDLRKVLDHRDKVYDQLAKYLQLRNVIERLQEAKPSelyMQVDLGCNFFVDTVVPDTSRIYVALGYGFFLELTLTE 105
Cdd:cd00584     6 QELREQIEALQEEIEQLEEEQAEIDEAKEALEELKKEGSE---VLVPLGGNAYVRAEVVDIDKVIVHLGLGYYAERDPDG 82

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1965563523 106 ALKFIDRKSSLLTELSDSLTKDSMNIKAHIHMLLEGLRE 144
Cdd:cd00584    83 AIEILEKKEDELDKRIEELQAELAELEDEYDQLEQQAQQ 121
Prefoldin pfam02996
Prefoldin subunit; This family comprises of several prefoldin subunits. The biogenesis of the ...
 28-146 7.24e-14

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: 63.81  E-value: 7.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965563523  28 LQRDLRKVLDHRDKVYDQLAKYLQLRNVIERLQEAKPSELyMQVDLGCNFFVDTVVPDTSRIYVALGYGFFLELTLTEAL 107
Cdd:pfam02996   1 YKQEIESLQAELARLREAIEELEKSLETLKTLKKEDEGKE-VLVPLGAGLYVKAEVIDTDKVLVDLGAGYYVEKSLEEAI 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1965563523 108 KFIDRKSSLLTELSDSLTKDSMNIKAHIHMLLEGLRELQ 146
Cdd:pfam02996  80 EILDKRIEELEKQLEKLEEELEKLKDQITTLEANLQQVQ 118
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 45-144 6.36e-05

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: 6.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965563523  45 QLAKYLQLRNVIERLQEAKP-SELYMQVdlGCNFFVDTVVPDTSRIYVALGYGFFLELTLTEALKFIDRKSSLLTELSDS 123
Cdd:cd23160    29 SINELNRAKETLEELKKLKEgTEILVPI--GGGSFVKAKIKDTDKVLVNIGAGVVVEKTIDEAIEILEKRIKELEKALEK 106

                          90       100
                  ....*....|....*....|.
gi 1965563523 124 LTKDSMNIKAHIHMLLEGLRE 144
Cdd:cd23160   107 LQEQLQQIAQRLEELEAELQE 127
Prefoldin_5 cd23157
Prefoldin subunit 5; Prefoldin subunit 5 is one of the alpha subunits of the eukaryotic ...
 49-126 6.68e-05

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: 40.16  E-value: 6.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965563523  49 YLQLRNVIERLQEAKPSELYMQ---------VDLGCNFFVDTVVPDTSRIYVALGYGFFLELTLTEALKFIDRKSSLLTE 119
Cdd:cd23157    20 LQQLKTAQAKFKESKEALEQLKkenegkeilVPLTSSLYVPGKLSDVDKVLVDIGTGYYVEKSVEDAKDYFKRKIEFLNE 99


                  ....*..
gi 1965563523 120 LSDSLTK 126
Cdd:cd23157   100 QIEKLQK 106
 
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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