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20  structures 724  species 0  interactions 1192  sequences 21  architectures

Family: DcpS_C (PF11969)

Summary: Scavenger mRNA decapping enzyme C-term binding

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This is the Wikipedia entry entitled "DCPS (gene)". More...

DCPS (gene) Edit Wikipedia article

Decapping enzyme, scavenger

PDB rendering based on 1st0.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols DCPS; HINT-5; HSL1
External IDs OMIM610534 MGI1916555 HomoloGene32202 GeneCards: DCPS Gene
EC number 3.6.1.59
Orthologs
Species Human Mouse
Entrez 28960 69305
Ensembl ENSG00000110063 ENSMUSG00000032040
UniProt Q96C86 Q9DAR7
RefSeq (mRNA) NM_014026 NM_027030
RefSeq (protein) NP_054745 NP_081306
Location (UCSC) Chr 11:
126.17 – 126.22 Mb
Chr 9:
35.12 – 35.18 Mb
PubMed search [1] [2]
Scavenger mRNA decapping enzyme (DcpS) N-terminal
PDB 1vlr EBI.jpg
crystal structure of mrna decapping enzyme (dcps) from mus musculus at 1.83 a resolution
Identifiers
Symbol DcpS
Pfam PF05652
InterPro IPR008594
SCOP 1st4
SUPERFAMILY 1st4
Scavenger mRNA decapping enzyme C-term binding
Identifiers
Symbol DcpS_C
Pfam PF11969
Pfam clan CL0265
SCOP 1st4
SUPERFAMILY 1st4

Scavenger mRNA-decapping enzyme DcpS is a protein that in humans is encoded by the DCPS gene.[1][2][3]

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).[4] 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.[5] 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.


References[edit]

  1. ^ 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): 4699–4708. doi:10.1093/emboj/cdf448. PMC 126188. PMID 12198172. 
  2. ^ 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): 12081–12086. doi:10.1073/pnas.1635192100. PMC 218716. PMID 14523240. 
  3. ^ "Entrez Gene: DCPS decapping enzyme, scavenger". 
  4. ^ Liu H, Kiledjian M (February 2006). "Decapping the message: a beginning or an end". Biochem. Soc. Trans. 34 (Pt 1): 35–8. doi:10.1042/BST20060035. PMID 16246173. 
  5. ^ 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): 797–802. doi:10.1002/prot.20467. PMID 16001405. 

Further reading[edit]


This article incorporates text from the public domain Pfam and InterPro IPR008594


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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 C-term binding Provide feedback

This family consists of several scavenger mRNA decapping enzymes (DcpS) and is the C-terminal region. 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. The C-terminal domain contains a histidine triad (HIT) sequence 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.

Literature references

  1. Liu H, Rodgers ND, Jiao X, Kiledjian M; , EMBO J 2002;21:4699-4708.: The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases. PUBMED:12198172 EPMC:12198172


Internal database links

External database links

This tab holds annotation information from the InterPro database.

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Domain organisation

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Pfam Clan

This family is a member of clan HIT (CL0265), which contains the following 5 members:

CwfJ_C_1 DcpS_C GalP_UDP_tr_C GalP_UDP_transf HIT

Alignments

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  Seed
(99)
Full
(1192)
Representative proteomes NCBI
(5559)
Meta
(3144)
RP15
(218)
RP35
(363)
RP55
(534)
RP75
(661)
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  Seed
(99)
Full
(1192)
Representative proteomes NCBI
(5559)
Meta
(3144)
RP15
(218)
RP35
(363)
RP55
(534)
RP75
(661)
Alignment:
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  Seed
(99)
Full
(1192)
Representative proteomes NCBI
(5559)
Meta
(3144)
RP15
(218)
RP35
(363)
RP55
(534)
RP75
(661)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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Pfam alignments:

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Curation and family details

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Curation View help on the curation process

Seed source: Pfam-B_9894 (release 8.0)
Previous IDs: none
Type: Family
Author: Moxon SJ
Number in seed: 99
Number in full: 1192
Average length of the domain: 113.70 aa
Average identity of full alignment: 25 %
Average coverage of the sequence by the domain: 50.60 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.9 20.9
Trusted cut-off 20.9 20.9
Noise cut-off 20.8 20.8
Model length: 116
Family (HMM) version: 3
Download: download the raw HMM for this family

Species distribution

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Structures

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_C domain has been found. There are 20 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 seqence.

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