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Conserved domains on  [gi|293358903|ref|XP_575654|]
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mRNA-decapping enzyme 1B isoform X1 [Rattus norvegicus]

Protein Classification

Dcp1 family protein( domain architecture ID 10874156)

Dcp1 (mRNA-decapping enzyme subunit 1) family protein similar to Mus musculus mRNA-decapping enzyme 1A/1B that may play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay

Gene Ontology:  GO:0016787|GO:0003729|GO:0000184

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 ...
16-131 1.12e-64

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: 207.38  E-value: 1.12e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293358903  16 ISLAALRRHDPYINRIVDVASQVALYTFGHRANEWEKTGVEGTLFVYTRSASPKHGFTIMNRLSMENRTEPITKDLDFQL 95
Cdd:cd09804    6 LNLKVLQRHDPYIVSILDTASHVAVYEFDDDTNEWEKTDVEGTLFVYKRSAEPRYGFIILNRLSTENLIEPITPELELEL 85
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 293358903  96 QDPFLLYRNGTLSIYGIWFYDKEECQRIAKLMKNLT 131
Cdd:cd09804   86 QDPYLIYRNANGEIYGIWFYDEEDRERIYKLLERLL 121
mRNA_decap_C pfam16741
mRNA-decapping enzyme C-terminus; The C-terminal domain of mRNA-decapping enzyme in Metazoa is ...
539-580 1.60e-15

mRNA-decapping enzyme C-terminus; The C-terminal domain of mRNA-decapping enzyme in Metazoa is responsible for trimerization.


:

Pssm-ID: 465253  Cd Length: 43  Bit Score: 70.36  E-value: 1.60e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 293358903  539 SRPLTRLQLQEALLNLIQNDDNFLSIIYEAYLFSVTQAAMRK 580
Cdd:pfam16741   1 PTPLTKSQLQDALIHLIKNDSDFLNKIHEAYLQSLTKDLSNK 42
PHA03247 super family cl33720
large tegument protein UL36; Provisional
179-430 8.54e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.15  E-value: 8.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293358903  179 SEPKQMTSSSAICDNPKLIKPVPVRPSSSQRLHEPTPSKTLDPEpqhlpltalfgKQDKAPCQETVKPSRTFAHHHHHHH 258
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE-----------RPRDDPAPGRVSRPRRARRLGRAAQ 2675
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293358903  259 HHQQQEK-----LPVHHGVACSLA-CEDPRKLSLPVEKQLCPAIQKLMVGSMGLHSLPQHPGQwpcESGSPSPAGGILPG 332
Cdd:PHA03247 2676 ASSPPQRprrraARPTVGSLTSLAdPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAA---PAPPAVPAGPATPG 2752
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293358903  333 -------PVQLGAPWNGRAAHCTQSTcrSHKLLEQLQGAPAAVHKYSFCAPASPAVTTQVAPGQSVAQSQLVYFSGPLPP 405
Cdd:PHA03247 2753 gparparPPTTAGPPAPAPPAAPAAG--PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830
                         250       260
                  ....*....|....*....|....*
gi 293358903  406 PTPGHQALGKEQCAPPAQAVSLSGS 430
Cdd:PHA03247 2831 PTSAQPTAPPPPPGPPPPSLPLGGS 2855
 
Name Accession Description Interval E-value
Dcp1 cd09804
mRNA decapping enzyme 1 (Dcp1); mRNA decapping enzyme 1 (Dcp1), together with Dcp2, is part of ...
16-131 1.12e-64

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: 207.38  E-value: 1.12e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293358903  16 ISLAALRRHDPYINRIVDVASQVALYTFGHRANEWEKTGVEGTLFVYTRSASPKHGFTIMNRLSMENRTEPITKDLDFQL 95
Cdd:cd09804    6 LNLKVLQRHDPYIVSILDTASHVAVYEFDDDTNEWEKTDVEGTLFVYKRSAEPRYGFIILNRLSTENLIEPITPELELEL 85
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 293358903  96 QDPFLLYRNGTLSIYGIWFYDKEECQRIAKLMKNLT 131
Cdd:cd09804   86 QDPYLIYRNANGEIYGIWFYDEEDRERIYKLLERLL 121
DCP1 pfam06058
Dcp1-like decapping family; An essential step in mRNA turnover is decapping. In yeast, two ...
15-129 3.02e-61

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: 198.16  E-value: 3.02e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293358903   15 DISLAALRRHDPYINRIVDVASQVALYTFGHRANEWEKTGVEGTLFVYTRSASPKHGFTIMNRLSMENRTEPITKDLDFQ 94
Cdd:pfam06058   3 ELNLRVLQRHDPSIESILDTASHVVLYKFDSESNEWEKTGIEGTLFVVKRSAEPRYGLIVLNRLSTENLIEPITKELELE 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 293358903   95 LQDPFLLYRNGTLSIYGIWFYDKEECQRIAKLMKN 129
Cdd:pfam06058  83 LQDPYLIYRNEDGEIYGIWFYDEEDCERIANLLKR 117
mRNA_decap_C pfam16741
mRNA-decapping enzyme C-terminus; The C-terminal domain of mRNA-decapping enzyme in Metazoa is ...
539-580 1.60e-15

mRNA-decapping enzyme C-terminus; The C-terminal domain of mRNA-decapping enzyme in Metazoa is responsible for trimerization.


Pssm-ID: 465253  Cd Length: 43  Bit Score: 70.36  E-value: 1.60e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 293358903  539 SRPLTRLQLQEALLNLIQNDDNFLSIIYEAYLFSVTQAAMRK 580
Cdd:pfam16741   1 PTPLTKSQLQDALIHLIKNDSDFLNKIHEAYLQSLTKDLSNK 42
PHA03247 PHA03247
large tegument protein UL36; Provisional
179-430 8.54e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.15  E-value: 8.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293358903  179 SEPKQMTSSSAICDNPKLIKPVPVRPSSSQRLHEPTPSKTLDPEpqhlpltalfgKQDKAPCQETVKPSRTFAHHHHHHH 258
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE-----------RPRDDPAPGRVSRPRRARRLGRAAQ 2675
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293358903  259 HHQQQEK-----LPVHHGVACSLA-CEDPRKLSLPVEKQLCPAIQKLMVGSMGLHSLPQHPGQwpcESGSPSPAGGILPG 332
Cdd:PHA03247 2676 ASSPPQRprrraARPTVGSLTSLAdPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAA---PAPPAVPAGPATPG 2752
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293358903  333 -------PVQLGAPWNGRAAHCTQSTcrSHKLLEQLQGAPAAVHKYSFCAPASPAVTTQVAPGQSVAQSQLVYFSGPLPP 405
Cdd:PHA03247 2753 gparparPPTTAGPPAPAPPAAPAAG--PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830
                         250       260
                  ....*....|....*....|....*
gi 293358903  406 PTPGHQALGKEQCAPPAQAVSLSGS 430
Cdd:PHA03247 2831 PTSAQPTAPPPPPGPPPPSLPLGGS 2855
 
Name Accession Description Interval E-value
Dcp1 cd09804
mRNA decapping enzyme 1 (Dcp1); mRNA decapping enzyme 1 (Dcp1), together with Dcp2, is part of ...
16-131 1.12e-64

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: 207.38  E-value: 1.12e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293358903  16 ISLAALRRHDPYINRIVDVASQVALYTFGHRANEWEKTGVEGTLFVYTRSASPKHGFTIMNRLSMENRTEPITKDLDFQL 95
Cdd:cd09804    6 LNLKVLQRHDPYIVSILDTASHVAVYEFDDDTNEWEKTDVEGTLFVYKRSAEPRYGFIILNRLSTENLIEPITPELELEL 85
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 293358903  96 QDPFLLYRNGTLSIYGIWFYDKEECQRIAKLMKNLT 131
Cdd:cd09804   86 QDPYLIYRNANGEIYGIWFYDEEDRERIYKLLERLL 121
EVH1-like_Dcp1 cd13182
Decapping enzyme EVH1-like domain; Dcp1 is a small protein containing an EVH1 domain. The ...
16-130 1.31e-63

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: 204.29  E-value: 1.31e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293358903  16 ISLAALRRHDPYINRIVDVASQVALYTFGHRANEWEKTGVEGTLFVYTRSASPKHGFTIMNRLSMENRTEPITKDLDFQL 95
Cdd:cd13182    1 LNLAVLQRYDPYIEEILDTASHVVLYKFDDDSNEWEKTDVEGTLFVYKRSAAPRYGFIVLNRLSPENFVEDITPELEVEL 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 293358903  96 QDPFLLYRNGTLSIYGIWFYDKEECQRIAKLMKNL 130
Cdd:cd13182   81 QDPFLIYRNEDGEIYGIWFYDEDDRERIYKLLEKL 115
DCP1 pfam06058
Dcp1-like decapping family; An essential step in mRNA turnover is decapping. In yeast, two ...
15-129 3.02e-61

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: 198.16  E-value: 3.02e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293358903   15 DISLAALRRHDPYINRIVDVASQVALYTFGHRANEWEKTGVEGTLFVYTRSASPKHGFTIMNRLSMENRTEPITKDLDFQ 94
Cdd:pfam06058   3 ELNLRVLQRHDPSIESILDTASHVVLYKFDSESNEWEKTGIEGTLFVVKRSAEPRYGLIVLNRLSTENLIEPITKELELE 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 293358903   95 LQDPFLLYRNGTLSIYGIWFYDKEECQRIAKLMKN 129
Cdd:pfam06058  83 LQDPYLIYRNEDGEIYGIWFYDEEDCERIANLLKR 117
mRNA_decap_C pfam16741
mRNA-decapping enzyme C-terminus; The C-terminal domain of mRNA-decapping enzyme in Metazoa is ...
539-580 1.60e-15

mRNA-decapping enzyme C-terminus; The C-terminal domain of mRNA-decapping enzyme in Metazoa is responsible for trimerization.


Pssm-ID: 465253  Cd Length: 43  Bit Score: 70.36  E-value: 1.60e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 293358903  539 SRPLTRLQLQEALLNLIQNDDNFLSIIYEAYLFSVTQAAMRK 580
Cdd:pfam16741   1 PTPLTKSQLQDALIHLIKNDSDFLNKIHEAYLQSLTKDLSNK 42
PHA03247 PHA03247
large tegument protein UL36; Provisional
179-430 8.54e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.15  E-value: 8.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293358903  179 SEPKQMTSSSAICDNPKLIKPVPVRPSSSQRLHEPTPSKTLDPEpqhlpltalfgKQDKAPCQETVKPSRTFAHHHHHHH 258
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE-----------RPRDDPAPGRVSRPRRARRLGRAAQ 2675
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293358903  259 HHQQQEK-----LPVHHGVACSLA-CEDPRKLSLPVEKQLCPAIQKLMVGSMGLHSLPQHPGQwpcESGSPSPAGGILPG 332
Cdd:PHA03247 2676 ASSPPQRprrraARPTVGSLTSLAdPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAA---PAPPAVPAGPATPG 2752
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293358903  333 -------PVQLGAPWNGRAAHCTQSTcrSHKLLEQLQGAPAAVHKYSFCAPASPAVTTQVAPGQSVAQSQLVYFSGPLPP 405
Cdd:PHA03247 2753 gparparPPTTAGPPAPAPPAAPAAG--PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830
                         250       260
                  ....*....|....*....|....*
gi 293358903  406 PTPGHQALGKEQCAPPAQAVSLSGS 430
Cdd:PHA03247 2831 PTSAQPTAPPPPPGPPPPSLPLGGS 2855
 
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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