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Conserved domains on  [gi|589269220|ref|NP_001277133|]
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mRNA-decapping enzyme 1A isoform b [Homo sapiens]

Protein Classification

Dcp1 family protein( domain architecture ID 12967202)

Dcp1 (mRNA-decapping enzyme subunit 1) family protein similar to Homo sapiens mRNA-decapping enzyme 1A that is necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay

Gene Ontology:  GO:0016787|GO:0003729|GO:0000184
PubMed:  19966221

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 ...
 6-126 9.89e-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: 203.91  E-value: 9.89e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589269220   6 RAGQEMSLAALKQHDPYITSIADLTGQVALYTFCPKANQWEKTDIEGTLFVYRRSASPYHGFTIVNRLNMHNLVEPVNKD 85
Cdd:cd09804    1 EARQALNLKVLQRHDPYIVSILDTASHVAVYEFDDDTNEWEKTDVEGTLFVYKRSAEPRYGFIILNRLSTENLIEPITPE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 589269220  86 LEFQLHEPFLLYRNASLSIYSIWFYDKNDCHRIAKLMADVV 126
Cdd:cd09804   81 LELELQDPYLIYRNANGEIYGIWFYDEEDRERIYKLLERLL 121
mRNA_decap_C pfam16741
mRNA-decapping enzyme C-terminus; The C-terminal domain of mRNA-decapping enzyme in Metazoa is ...
 501-543 9.11e-18

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: 76.91  E-value: 9.11e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 589269220  501 SIILSKSQLQDTLIHLIKNDSSFLSTLHEVYLQVLTKNKDNHN 543
Cdd:pfam16741   1 PTPLTKSQLQDALIHLIKNDSDFLNKIHEAYLQSLTKDLSNKK 43
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 230-494 1.06e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 41.83  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589269220  230 APQSETLGVPSAAHHSVQPEITT----PVLITPASITQSNEKHAPTYTIPLSPVLSPTLPAEAPTAQVPPSLPrNSTMMQ 305
Cdd:pfam05109 460 APASTGPTVSTADVTSPTPAGTTsgasPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTP-NATSPT 538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589269220  306 AVKTTPrqrSPLLNQPVPELShaslianqSPfrAPLNVTNTAGTSLPSVDllqklRLTPQHDQIQTQPLGKGAMVASFSP 385
Cdd:pfam05109 539 LGKTSP---TSAVTTPTPNAT--------SP--TPAVTTPTPNATIPTLG-----KTSPTSAVTTPTPNATSPTVGETSP 600

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589269220  386 AA--------GQLATPESFIEPPSKTAAARV----AASASLSNMVLAPlQSMQQNQDPEV----FVQPKVLSSAIPVAGA 449
Cdd:pfam05109 601 QAnttnhtlgGTSSTPVVTSPPKNATSAVTTgqhnITSSSTSSMSLRP-SSISETLSPSTsdnsTSHMPLLTSAHPTGGE 679

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 589269220  450 PLVTATTTAVSSVLL---APSVFQQTVTRSSDLERKASSPSP----LTIGTP 494
Cdd:pfam05109 680 NITQVTPASTSTHHVstsSPAPRPGTTSQASGPGNSSTSTKPgevnVTKGTP 731
 
Name Accession Description Interval E-value
Dcp1 cd09804
mRNA decapping enzyme 1 (Dcp1); mRNA decapping enzyme 1 (Dcp1), together with Dcp2, is part of ...
 6-126 9.89e-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: 203.91  E-value: 9.89e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589269220   6 RAGQEMSLAALKQHDPYITSIADLTGQVALYTFCPKANQWEKTDIEGTLFVYRRSASPYHGFTIVNRLNMHNLVEPVNKD 85
Cdd:cd09804    1 EARQALNLKVLQRHDPYIVSILDTASHVAVYEFDDDTNEWEKTDVEGTLFVYKRSAEPRYGFIILNRLSTENLIEPITPE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 589269220  86 LEFQLHEPFLLYRNASLSIYSIWFYDKNDCHRIAKLMADVV 126
Cdd:cd09804   81 LELELQDPYLIYRNANGEIYGIWFYDEEDRERIYKLLERLL 121
DCP1 pfam06058
Dcp1-like decapping family; An essential step in mRNA turnover is decapping. In yeast, two ...
 9-122 1.60e-59

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: 192.77  E-value: 1.60e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589269220    9 QEMSLAALKQHDPYITSIADLTGQVALYTFCPKANQWEKTDIEGTLFVYRRSASPYHGFTIVNRLNMHNLVEPVNKDLEF 88
Cdd:pfam06058   2 RELNLRVLQRHDPSIESILDTASHVVLYKFDSESNEWEKTGIEGTLFVVKRSAEPRYGLIVLNRLSTENLIEPITKELEL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 589269220   89 QLHEPFLLYRNASLSIYSIWFYDKNDCHRIAKLM 122
Cdd:pfam06058  82 ELQDPYLIYRNEDGEIYGIWFYDEEDCERIANLL 115
mRNA_decap_C pfam16741
mRNA-decapping enzyme C-terminus; The C-terminal domain of mRNA-decapping enzyme in Metazoa is ...
 501-543 9.11e-18

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: 76.91  E-value: 9.11e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 589269220  501 SIILSKSQLQDTLIHLIKNDSSFLSTLHEVYLQVLTKNKDNHN 543
Cdd:pfam16741   1 PTPLTKSQLQDALIHLIKNDSDFLNKIHEAYLQSLTKDLSNKK 43
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 230-494 1.06e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 41.83  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589269220  230 APQSETLGVPSAAHHSVQPEITT----PVLITPASITQSNEKHAPTYTIPLSPVLSPTLPAEAPTAQVPPSLPrNSTMMQ 305
Cdd:pfam05109 460 APASTGPTVSTADVTSPTPAGTTsgasPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTP-NATSPT 538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589269220  306 AVKTTPrqrSPLLNQPVPELShaslianqSPfrAPLNVTNTAGTSLPSVDllqklRLTPQHDQIQTQPLGKGAMVASFSP 385
Cdd:pfam05109 539 LGKTSP---TSAVTTPTPNAT--------SP--TPAVTTPTPNATIPTLG-----KTSPTSAVTTPTPNATSPTVGETSP 600

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589269220  386 AA--------GQLATPESFIEPPSKTAAARV----AASASLSNMVLAPlQSMQQNQDPEV----FVQPKVLSSAIPVAGA 449
Cdd:pfam05109 601 QAnttnhtlgGTSSTPVVTSPPKNATSAVTTgqhnITSSSTSSMSLRP-SSISETLSPSTsdnsTSHMPLLTSAHPTGGE 679

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 589269220  450 PLVTATTTAVSSVLL---APSVFQQTVTRSSDLERKASSPSP----LTIGTP 494
Cdd:pfam05109 680 NITQVTPASTSTHHVstsSPAPRPGTTSQASGPGNSSTSTKPgevnVTKGTP 731
 
Name Accession Description Interval E-value
Dcp1 cd09804
mRNA decapping enzyme 1 (Dcp1); mRNA decapping enzyme 1 (Dcp1), together with Dcp2, is part of ...
 6-126 9.89e-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: 203.91  E-value: 9.89e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589269220   6 RAGQEMSLAALKQHDPYITSIADLTGQVALYTFCPKANQWEKTDIEGTLFVYRRSASPYHGFTIVNRLNMHNLVEPVNKD 85
Cdd:cd09804    1 EARQALNLKVLQRHDPYIVSILDTASHVAVYEFDDDTNEWEKTDVEGTLFVYKRSAEPRYGFIILNRLSTENLIEPITPE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 589269220  86 LEFQLHEPFLLYRNASLSIYSIWFYDKNDCHRIAKLMADVV 126
Cdd:cd09804   81 LELELQDPYLIYRNANGEIYGIWFYDEEDRERIYKLLERLL 121
DCP1 pfam06058
Dcp1-like decapping family; An essential step in mRNA turnover is decapping. In yeast, two ...
 9-122 1.60e-59

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: 192.77  E-value: 1.60e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589269220    9 QEMSLAALKQHDPYITSIADLTGQVALYTFCPKANQWEKTDIEGTLFVYRRSASPYHGFTIVNRLNMHNLVEPVNKDLEF 88
Cdd:pfam06058   2 RELNLRVLQRHDPSIESILDTASHVVLYKFDSESNEWEKTGIEGTLFVVKRSAEPRYGLIVLNRLSTENLIEPITKELEL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 589269220   89 QLHEPFLLYRNASLSIYSIWFYDKNDCHRIAKLM 122
Cdd:pfam06058  82 ELQDPYLIYRNEDGEIYGIWFYDEEDCERIANLL 115
EVH1-like_Dcp1 cd13182
Decapping enzyme EVH1-like domain; Dcp1 is a small protein containing an EVH1 domain. The ...
 11-126 3.53e-58

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: 189.27  E-value: 3.53e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589269220  11 MSLAALKQHDPYITSIADLTGQVALYTFCPKANQWEKTDIEGTLFVYRRSASPYHGFTIVNRLNMHNLVEPVNKDLEFQL 90
Cdd:cd13182    1 LNLAVLQRYDPYIEEILDTASHVVLYKFDDDSNEWEKTDVEGTLFVYKRSAAPRYGFIVLNRLSPENFVEDITPELEVEL 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 589269220  91 HEPFLLYRNASLSIYSIWFYDKNDCHRIAKLMADVV 126
Cdd:cd13182   81 QDPFLIYRNEDGEIYGIWFYDEDDRERIYKLLEKLL 116
mRNA_decap_C pfam16741
mRNA-decapping enzyme C-terminus; The C-terminal domain of mRNA-decapping enzyme in Metazoa is ...
 501-543 9.11e-18

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: 76.91  E-value: 9.11e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 589269220  501 SIILSKSQLQDTLIHLIKNDSSFLSTLHEVYLQVLTKNKDNHN 543
Cdd:pfam16741   1 PTPLTKSQLQDALIHLIKNDSDFLNKIHEAYLQSLTKDLSNKK 43
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 230-494 1.06e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 41.83  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589269220  230 APQSETLGVPSAAHHSVQPEITT----PVLITPASITQSNEKHAPTYTIPLSPVLSPTLPAEAPTAQVPPSLPrNSTMMQ 305
Cdd:pfam05109 460 APASTGPTVSTADVTSPTPAGTTsgasPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTP-NATSPT 538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589269220  306 AVKTTPrqrSPLLNQPVPELShaslianqSPfrAPLNVTNTAGTSLPSVDllqklRLTPQHDQIQTQPLGKGAMVASFSP 385
Cdd:pfam05109 539 LGKTSP---TSAVTTPTPNAT--------SP--TPAVTTPTPNATIPTLG-----KTSPTSAVTTPTPNATSPTVGETSP 600

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589269220  386 AA--------GQLATPESFIEPPSKTAAARV----AASASLSNMVLAPlQSMQQNQDPEV----FVQPKVLSSAIPVAGA 449
Cdd:pfam05109 601 QAnttnhtlgGTSSTPVVTSPPKNATSAVTTgqhnITSSSTSSMSLRP-SSISETLSPSTsdnsTSHMPLLTSAHPTGGE 679

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 589269220  450 PLVTATTTAVSSVLL---APSVFQQTVTRSSDLERKASSPSP----LTIGTP 494
Cdd:pfam05109 680 NITQVTPASTSTHHVstsSPAPRPGTTSQASGPGNSSTSTKPgevnVTKGTP 731
 
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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