Summary: Scavenger mRNA decapping enzyme (DcpS) N-terminal
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DCPS (gene) Edit Wikipedia article
|, DCS1, HINT-5, HINT5, HSL1, ARS, HSPC015, decapping enzyme, scavenger|
|Scavenger mRNA decapping enzyme (DcpS) N-terminal|
|SCOP2||1st4 / SCOPe / SUPFAM|
|Scavenger mRNA decapping enzyme C-term binding|
|SCOP2||1st4 / SCOPe / SUPFAM|
The scavenger mRNA decapping enzymes include Dcp2 and DcpS. DcpS is a scavenger pyrophosphatase that hydrolyses the residual cap structure following 3' to 5' mRNA degradation. DcpS uses cap dinucleotides or capped oligonucleotides as substrates to release m(7)GMP (N7-methyl GMP), while Dcp2 uses capped mRNA as a substrate in order to hydrolyse the cap to release m(7)GDP (N7-methyl GDP). The association of DcpS with 3' to 5' exonuclease exosome components suggests that these two activities are linked and there is a coupled exonucleolytic decay-dependent decapping pathway. The family contains a histidine triad (HIT) sequence in its C-terminal domain, with three histidines separated by hydrophobic residues. The central histidine within the DcpS HIT motif is critical for decapping activity and defines the HIT motif as a new mRNA decapping domain, making DcpS the first member of the HIT family of proteins with a defined biological function.
- GRCh38: Ensembl release 89: ENSG00000110063 - Ensembl, May 2017
- GRCm38: Ensembl release 89: ENSMUSG00000032040 - Ensembl, May 2017
- "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- Liu H, Rodgers ND, Jiao X, Kiledjian M (Aug 2002). "The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases". EMBO J. 21 (17): 4699â€“4708. doi:10.1093/emboj/cdf448. PMCÂ 126188. PMIDÂ 12198172.
- van Dijk E, Le Hir H, Seraphin B (Oct 2003). "DcpS can act in the 5'-3' mRNA decay pathway in addition to the 3'-5' pathway". Proc Natl Acad Sci U S A. 100 (21): 12081â€“12086. Bibcode:2003PNAS..10012081V. doi:10.1073/pnas.1635192100. PMCÂ 218716. PMIDÂ 14523240.
- "Entrez Gene: DCPS decapping enzyme, scavenger".
- Liu H, Kiledjian M (February 2006). "Decapping the message: a beginning or an end". Biochem. Soc. Trans. 34 (Pt 1): 35â€“8. doi:10.1042/BST20060035. PMIDÂ 16246173.
- Han GW, Schwarzenbacher R, McMullan D, Abdubek P, Ambing E, Axelrod H, Biorac T, Canaves JM, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Haugen J, Hornsby M, Jaroszewski L, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, McPhillips TM, Miller MD, Moy K, Nigoghossian E, Paulsen J, Quijano K, Reyes R, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Wilson IA (September 2005). "Crystal structure of an Apo mRNA decapping enzyme (DcpS) from Mouse at 1.83 A resolution". Proteins. 60 (4): 797â€“802. doi:10.1002/prot.20467. PMIDÂ 16001405. S2CIDÂ 20494085.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1â€“2): 171â€“174. doi:10.1016/0378-1119(94)90802-8. PMIDÂ 8125298.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etÂ al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1â€“2): 149â€“156. doi:10.1016/S0378-1119(97)00411-3. PMIDÂ 9373149.
- Zhang QH, Ye M, Wu XY, etÂ al. (2001). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res. 10 (10): 1546â€“1560. doi:10.1101/gr.140200. PMCÂ 310934. PMIDÂ 11042152.
- Wang Z, Kiledjian M (2002). "Functional link between the mammalian exosome and mRNA decapping". Cell. 107 (6): 751â€“762. doi:10.1016/S0092-8674(01)00592-X. PMIDÂ 11747811. S2CIDÂ 8098116.
- Strausberg RL, Feingold EA, Grouse LH, etÂ al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899â€“16903. doi:10.1073/pnas.242603899. PMCÂ 139241. PMIDÂ 12477932.
- Kwasnicka DA, Krakowiak A, Thacker C, etÂ al. (2003). "Coordinate expression of NADPH-dependent flavin reductase, Fre-1, and Hint-related 7meGMP-directed hydrolase, DCS-1". J. Biol. Chem. 278 (40): 39051â€“39058. doi:10.1074/jbc.M306355200. PMCÂ 2556063. PMIDÂ 12871939.
- Ota T, Suzuki Y, Nishikawa T, etÂ al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40â€“45. doi:10.1038/ng1285. PMIDÂ 14702039.
- Gu M, Fabrega C, Liu SW, etÂ al. (2004). "Insights into the structure, mechanism, and regulation of scavenger mRNA decapping activity". Mol. Cell. 14 (1): 67â€“80. doi:10.1016/S1097-2765(04)00180-7. PMIDÂ 15068804.
- Liu SW, Jiao X, Liu H, etÂ al. (2004). "Functional analysis of mRNA scavenger decapping enzymes". RNA. 10 (9): 1412â€“1422. doi:10.1261/rna.7660804. PMCÂ 1370627. PMIDÂ 15273322.
- Gerhard DS, Wagner L, Feingold EA, etÂ al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121â€“2127. doi:10.1101/gr.2596504. PMCÂ 528928. PMIDÂ 15489334.
- Malys N, Carroll K, Miyan J, Tollervey D, McCarthy JE (2004). "The 'scavenger' m7GpppX pyrophosphatase activity of Dcs1 modulates nutrient-induced responses in yeast". Nucleic Acids Res. 32 (12): 3590â€“3600. doi:10.1093/nar/gkh687. PMCÂ 484174. PMIDÂ 15240832.
- Chen N, Walsh MA, Liu Y, etÂ al. (2005). "Crystal structures of human DcpS in ligand-free and m7GDP-bound forms suggest a dynamic mechanism for scavenger mRNA decapping". J. Mol. Biol. 347 (4): 707â€“718. doi:10.1016/j.jmb.2005.01.062. PMIDÂ 15769464.
- KwaÅ›nicka-Crawford DA, Vincent SR (2005). "Role of a novel dual flavin reductase (NR1) and an associated histidine triad protein (DCS-1) in menadione-induced cytotoxicity". Biochem. Biophys. Res. Commun. 336 (2): 565â€“571. doi:10.1016/j.bbrc.2005.08.129. PMIDÂ 16140270.
- Malys N, McCarthy JEG (2006). "Dcs2, a novel stress-induced modulator of m7GpppX pyrophosphatase activity that locates to P bodies". J. Mol. Biol. 363 (2): 370â€“382. doi:10.1016/j.jmb.2006.08.015. PMIDÂ 16963086.
- PDBe-KB provides an overview of all the structure information available in the PDB for Human m7GpppX diphosphatase (DCPS)
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Scavenger mRNA decapping enzyme (DcpS) N-terminal Provide feedback
This family consists of several scavenger mRNA decapping enzymes (DcpS) and is the N-terminal domain of these proteins. DcpS is a scavenger pyrophosphatase that hydrolyses the residual cap structure following 3' to 5' decay of an mRNA. The association of DcpS with 3' to 5' exonuclease exosome components suggests that these two activities are linked and there is a coupled exonucleolytic decay-dependent decapping pathway.
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR008594
This entry represents scavenger mRNA decapping enzymes, such as Dcp2 and DcpS. DcpS is a scavenger pyrophosphatase that hydrolyses the residual cap structure following 3' to 5' mRNA degradation. DcpS uses cap dinucleotides or capped oligonucleotides as substrate to release m(7)GMP (N7-methyl GMP), while Dcp2 uses capped mRNA as substrate in order to hydrolyse the cap to release m(7)GDP (N7-methyl GDP) [ PUBMED:16246173 ]. The association of DcpS with 3' to 5' exonuclease exosome components suggests that these two activities are linked and there is a coupled exonucleolytic decay-dependent decapping pathway. The family contains a histidine triad (HIT) sequence with three histidines separated by hydrophobic residues [ PUBMED:16001405 ]. The central histidine within the DcpS HIT motif is critical for decapping activity and defines the HIT motif as a new mRNA decapping domain, making DcpS the first member of the HIT family of proteins with a defined biological function. This family is related to ( INTERPRO ).
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||hydrolase activity (GO:0016787)|
|Biological process||deadenylation-dependent decapping of nuclear-transcribed mRNA (GO:0000290)|
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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|Seed source:||Pfam-B_9894 (release 8.0)|
|Number in seed:||109|
|Number in full:||1304|
|Average length of the domain:||104.80 aa|
|Average identity of full alignment:||31 %|
|Average coverage of the sequence by the domain:||30.34 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||15|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the DcpS domain has been found. There are 42 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.