DCPS_ASCSU
ID DCPS_ASCSU Reviewed; 301 AA.
AC D3K0N9;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=m7GpppX diphosphatase;
DE EC=3.6.1.59 {ECO:0000269|PubMed:15383679, ECO:0000269|PubMed:22985415};
DE AltName: Full=Decapping scavenger enzyme;
DE AltName: Full=Scavenger mRNA-decapping enzyme DcpS;
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Davis R.E., McFarland C.;
RT "Ascaris DcpS activity on m7G and m2,2,7G mRNA cap.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=15383679; DOI=10.1261/rna.7690504;
RA Cohen L.S., Mikhli C., Friedman C., Jankowska-Anyszka M., Stepinski J.,
RA Darzynkiewicz E., Davis R.E.;
RT "Nematode m7GpppG and m3(2,2,7)GpppG decapping: activities in Ascaris
RT embryos and characterization of C. elegans scavenger DcpS.";
RL RNA 10:1609-1624(2004).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND ACTIVITY
RP REGULATION.
RX PubMed=22985415; DOI=10.1021/bi300781g;
RA Wypijewska A., Bojarska E., Lukaszewicz M., Stepinski J., Jemielity J.,
RA Davis R.E., Darzynkiewicz E.;
RT "7-Methylguanosine diphosphate (m(7)GDP) is not hydrolyzed but strongly
RT bound by decapping scavenger (dcpS) enzymes and potently inhibits their
RT activity.";
RL Biochemistry 51:8003-8013(2012).
CC -!- FUNCTION: Decapping scavenger enzyme that catalyzes the cleavage of a
CC residual cap structure following the degradation of mRNAs of the 3'->5'
CC exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures
CC like 7-methylguanosine nucleoside triphosphate (m7GpppG) and tri-methyl
CC guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with up to 2
CC nucleotide substrates (small capped oligoribonucleotides) and
CC specifically releases 5'-phosphorylated RNA fragments and 7-
CC methylguanosine monophosphate (m7GMP). Does not hydrolyze unmethylated
CC cap analog (GpppG) and shows no decapping activity on intact m7GpppG-
CC capped mRNA molecules. Does not hydrolyze 7-methylguanosine diphosphate
CC (m7GDP) and tri-methylguanosine diphosphate (m3(2,2,7)GDP) to m(7)GMP
CC and m3(2,2,7)GMP, respectively (PubMed:15383679, PubMed:22985415). May
CC also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream
CC product released by the 5'->3' mRNA mediated decapping activity, may be
CC also converted by dcs-1 to m7GMP. Binds to m7GpppG and strongly to
CC m7GDP. {ECO:0000269|PubMed:15383679, ECO:0000269|PubMed:22985415}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + 2 H(+) +
CC N(7)-methyl-GMP; Xref=Rhea:RHEA:65388, Rhea:RHEA-COMP:17165,
CC Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58285, ChEBI:CHEBI:156461, ChEBI:CHEBI:167616;
CC EC=3.6.1.59; Evidence={ECO:0000269|PubMed:22985415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(2),N(2),N(7)-trimethyl 5'-triphosphoguanosine)-
CC (ribonucleoside) in mRNA + H2O = (N(2),N(2),N(7))-trimethyl-GMP + a
CC 5'-end diphospho-ribonucleoside in mRNA + 2 H(+);
CC Xref=Rhea:RHEA:65384, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17171,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74434,
CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167623; EC=3.6.1.59;
CC Evidence={ECO:0000269|PubMed:15383679, ECO:0000269|PubMed:22985415};
CC -!- ACTIVITY REGULATION: The hydrolytic product 7-methylguanosine
CC diphosphate (m7GDP) efficiently inhibits the decapping scavenger
CC activity and acts as a competitive inhibitor in vitro.
CC {ECO:0000269|PubMed:22985415}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HIT family. {ECO:0000305}.
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DR EMBL; GU350725; ADB92583.1; -; mRNA.
DR AlphaFoldDB; D3K0N9; -.
DR SMR; D3K0N9; -.
DR KEGG; ag:ADB92583; -.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IDA:UniProtKB.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:InterPro.
DR GO; GO:0110156; P:methylguanosine-cap decapping; IDA:WormBase.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; TAS:UniProtKB.
DR GO; GO:0009408; P:response to heat; ISS:UniProtKB.
DR Gene3D; 3.30.200.40; -; 1.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR008594; DcpS/DCS2.
DR InterPro; IPR036265; HIT-like_sf.
DR InterPro; IPR011145; Scavenger_mRNA_decap_enz_N.
DR PANTHER; PTHR12978; PTHR12978; 1.
DR Pfam; PF05652; DcpS; 1.
DR PIRSF; PIRSF028973; Scavenger_mRNA_decap_enz; 1.
DR SUPFAM; SSF102860; SSF102860; 1.
DR SUPFAM; SSF54197; SSF54197; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Nucleus.
FT CHAIN 1..301
FT /note="m7GpppX diphosphatase"
FT /id="PRO_0000420575"
FT MOTIF 244..248
FT /note="Histidine triad motif"
FT /evidence="ECO:0000250"
FT ACT_SITE 246
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 237..248
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 301 AA; 34565 MW; 3FFE233D75E0F217 CRC64;
MVDEVDANST GDNSLVNMKG FSFKEVLGSD SARKSAFILL DSSNGENAIL LADKNAFPVD
KTSWSAILTG STLKPIMKND IYSSYTLCMP NEFSDVKSTL IYPCNEKHIA KYRDQKRFII
NETPEDYRTI TLPYIQRNQM SLEWVYNILD HKAEVDRIIY EETDPHDGFI LAPDLKWSGE
QLECLYVQAL VRRKGIKSIR DLTANDLPLL EGIRDKGLNA IKEKYGLDKH QIRAYFHYQP
SFYHLHVHFI HVSYEAPASG VAKAVLLDDV INNLKLIPDF YQRSTLTFTA KEQDPIYRRE
N
