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Conserved domains on  [gi|985482508|ref|NP_001306221|]
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mRNA-decapping enzyme 1B isoform 2 [Homo sapiens]

Protein Classification

mRNA-decapping enzyme subunit 1( domain architecture ID 10176835)

mRNA-decapping enzyme subunit 1 (Dcp1) is a component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay

CATH:  2.30.29.30
Gene Ontology:  GO:0098745|GO:0000184|GO:0110156|GO:0003729|GO:0008047
PubMed:  27183195|15189161|15901504
SCOP:  4000901

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Dcp1 cd09804
mRNA decapping enzyme 1 (Dcp1); mRNA decapping enzyme 1 (Dcp1), together with Dcp2, is part of ...
 16-108 3.56e-53

mRNA decapping enzyme 1 (Dcp1); mRNA decapping enzyme 1 (Dcp1), together with Dcp2, is part of the decapping complex which catalyzes the removal of the 5' cap structure of mRNA. This decapping reaction is an essential step in mRNA degradation, by exposing the 5' end for exonucleolytic digestion. Dcp1 binds to the N-terminal helical domain of catalytic subunit Dcp2 and enhances its function by promoting Dsp2's closed conformation which is catalytically more active.


:

Pssm-ID: 197362  Cd Length: 121  Bit Score: 164.24  E-value: 3.56e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482508  16 ISLAALQRHDPYINRIVDVASQVALYTFGHRANEWEKTDVEGTLFVYTRSASPKHGFTIMNRLSMENRTEPITKDLDFQL 95
Cdd:cd09804    6 LNLKVLQRHDPYIVSILDTASHVAVYEFDDDTNEWEKTDVEGTLFVYKRSAEPRYGFIILNRLSTENLIEPITPELELEL 85

                         90
                 ....*....|...
gi 985482508  96 QDPFLLYRNARCE 108
Cdd:cd09804   86 QDPYLIYRNANGE 98
 
Name Accession Description Interval E-value
Dcp1 cd09804
mRNA decapping enzyme 1 (Dcp1); mRNA decapping enzyme 1 (Dcp1), together with Dcp2, is part of ...
 16-108 3.56e-53

mRNA decapping enzyme 1 (Dcp1); mRNA decapping enzyme 1 (Dcp1), together with Dcp2, is part of the decapping complex which catalyzes the removal of the 5' cap structure of mRNA. This decapping reaction is an essential step in mRNA degradation, by exposing the 5' end for exonucleolytic digestion. Dcp1 binds to the N-terminal helical domain of catalytic subunit Dcp2 and enhances its function by promoting Dsp2's closed conformation which is catalytically more active.


Pssm-ID: 197362  Cd Length: 121  Bit Score: 164.24  E-value: 3.56e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482508  16 ISLAALQRHDPYINRIVDVASQVALYTFGHRANEWEKTDVEGTLFVYTRSASPKHGFTIMNRLSMENRTEPITKDLDFQL 95
Cdd:cd09804    6 LNLKVLQRHDPYIVSILDTASHVAVYEFDDDTNEWEKTDVEGTLFVYKRSAEPRYGFIILNRLSTENLIEPITPELELEL 85

                         90
                 ....*....|...
gi 985482508  96 QDPFLLYRNARCE 108
Cdd:cd09804   86 QDPYLIYRNANGE 98
DCP1 pfam06058
Dcp1-like decapping family; An essential step in mRNA turnover is decapping. In yeast, two ...
 14-108 6.26e-52

Dcp1-like decapping family; An essential step in mRNA turnover is decapping. In yeast, two proteins have been identified that are essential for decapping, Dcp1 (this family) and Dcp2 (pfam05026). The precise role of these proteins in the decapping reaction have not been established. Evidence suggests that the Dcp1 may enhance the function of Dcp2.


Pssm-ID: 461816  Cd Length: 117  Bit Score: 160.80  E-value: 6.26e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482508   14 RDISLAALQRHDPYINRIVDVASQVALYTFGHRANEWEKTDVEGTLFVYTRSASPKHGFTIMNRLSMENRTEPITKDLDF 93
Cdd:pfam06058   2 RELNLRVLQRHDPSIESILDTASHVVLYKFDSESNEWEKTGIEGTLFVVKRSAEPRYGLIVLNRLSTENLIEPITKELEL 81

                          90
                  ....*....|....*
gi 985482508   94 QLQDPFLLYRNARCE 108
Cdd:pfam06058  82 ELQDPYLIYRNEDGE 96
 
Name Accession Description Interval E-value
Dcp1 cd09804
mRNA decapping enzyme 1 (Dcp1); mRNA decapping enzyme 1 (Dcp1), together with Dcp2, is part of ...
 16-108 3.56e-53

mRNA decapping enzyme 1 (Dcp1); mRNA decapping enzyme 1 (Dcp1), together with Dcp2, is part of the decapping complex which catalyzes the removal of the 5' cap structure of mRNA. This decapping reaction is an essential step in mRNA degradation, by exposing the 5' end for exonucleolytic digestion. Dcp1 binds to the N-terminal helical domain of catalytic subunit Dcp2 and enhances its function by promoting Dsp2's closed conformation which is catalytically more active.


Pssm-ID: 197362  Cd Length: 121  Bit Score: 164.24  E-value: 3.56e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482508  16 ISLAALQRHDPYINRIVDVASQVALYTFGHRANEWEKTDVEGTLFVYTRSASPKHGFTIMNRLSMENRTEPITKDLDFQL 95
Cdd:cd09804    6 LNLKVLQRHDPYIVSILDTASHVAVYEFDDDTNEWEKTDVEGTLFVYKRSAEPRYGFIILNRLSTENLIEPITPELELEL 85

                         90
                 ....*....|...
gi 985482508  96 QDPFLLYRNARCE 108
Cdd:cd09804   86 QDPYLIYRNANGE 98
EVH1-like_Dcp1 cd13182
Decapping enzyme EVH1-like domain; Dcp1 is a small protein containing an EVH1 domain. The ...
 16-131 5.24e-53

Decapping enzyme EVH1-like domain; Dcp1 is a small protein containing an EVH1 domain. The Dcp1-Dcp2 complex plays a critical step in mRNA degradation with the removal of the 50 cap structure. Dcp1 stimulates the activity of Dcp2 by promoting and/or stabilizing the closed complex. The interface of Dcp1 and Dcp2 is not fully conserved and in higher eukaryotes it requires an additional factor. The proline-rich sequence (PRS)-binding sites in Dcp1p indicates that it belongs to a novel class of EVH1 domains. Dcp1 has 2 prominent sites,one required for the function of the Dcp1p-Dcp2p complex, and the other, the PRS-binding site of EVH1 domains, a binding site for decapping regulatory proteins. It also has a conserved hydrophobic patch is shown to be critical for decapping. The EVH1 domains are part of the PH domain superamily.


Pssm-ID: 270003  Cd Length: 116  Bit Score: 163.46  E-value: 5.24e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482508  16 ISLAALQRHDPYINRIVDVASQVALYTFGHRANEWEKTDVEGTLFVYTRSASPKHGFTIMNRLSMENRTEPITKDLDFQL 95
Cdd:cd13182    1 LNLAVLQRYDPYIEEILDTASHVVLYKFDDDSNEWEKTDVEGTLFVYKRSAAPRYGFIVLNRLSPENFVEDITPELEVEL 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 985482508  96 QDPFLLYRNARCESFLLqWVVLLLKFGQVFKIVQCL 131
Cdd:cd13182   81 QDPFLIYRNEDGEIYGI-WFYDEDDRERIYKLLEKL 115
DCP1 pfam06058
Dcp1-like decapping family; An essential step in mRNA turnover is decapping. In yeast, two ...
 14-108 6.26e-52

Dcp1-like decapping family; An essential step in mRNA turnover is decapping. In yeast, two proteins have been identified that are essential for decapping, Dcp1 (this family) and Dcp2 (pfam05026). The precise role of these proteins in the decapping reaction have not been established. Evidence suggests that the Dcp1 may enhance the function of Dcp2.


Pssm-ID: 461816  Cd Length: 117  Bit Score: 160.80  E-value: 6.26e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482508   14 RDISLAALQRHDPYINRIVDVASQVALYTFGHRANEWEKTDVEGTLFVYTRSASPKHGFTIMNRLSMENRTEPITKDLDF 93
Cdd:pfam06058   2 RELNLRVLQRHDPSIESILDTASHVVLYKFDSESNEWEKTGIEGTLFVVKRSAEPRYGLIVLNRLSTENLIEPITKELEL 81

                          90
                  ....*....|....*
gi 985482508   94 QLQDPFLLYRNARCE 108
Cdd:pfam06058  82 ELQDPYLIYRNEDGE 96
 
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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