ID A0A158PKQ2_ANGCS Unreviewed; 249 AA.
AC A0A158PKQ2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=m7GpppX diphosphatase {ECO:0000256|ARBA:ARBA00015636};
DE EC=3.6.1.59 {ECO:0000256|ARBA:ARBA00012520};
DE AltName: Full=Decapping scavenger enzyme {ECO:0000256|ARBA:ARBA00030609};
DE AltName: Full=Scavenger mRNA-decapping enzyme DcpS {ECO:0000256|ARBA:ARBA00029885};
GN ORFNames=ACOC_LOCUS10386 {ECO:0000313|EMBL:VDM61971.1};
OS Angiostrongylus costaricensis (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0001038501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ACOC_0001038501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM61971.1, ECO:0000313|Proteomes:UP000267027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Costa Rica {ECO:0000313|EMBL:VDM61971.1,
RC ECO:0000313|Proteomes:UP000267027};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00024271};
CC -!- SIMILARITY: Belongs to the HIT family. {ECO:0000256|ARBA:ARBA00010208}.
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DR EMBL; UYYA01004462; VDM61971.1; -; Genomic_DNA.
DR STRING; 334426.A0A158PKQ2; -.
DR WBParaSite; ACOC_0001038501-mRNA-1; ACOC_0001038501-mRNA-1; ACOC_0001038501.
DR Proteomes; UP000050601; Unplaced.
DR Proteomes; UP000267027; Unassembled WGS sequence.
DR GO; GO:0140932; F:5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:InterPro.
DR Gene3D; 3.30.428.10; HIT-like; 1.
DR Gene3D; 3.30.2240.10; mRNA decapping enzyme DcpS N-terminal domain; 2.
DR InterPro; IPR008594; DcpS/DCS2.
DR InterPro; IPR036265; HIT-like_sf.
DR InterPro; IPR011145; Scavenger_mRNA_decap_enz_N.
DR PANTHER; PTHR12978; HISTIDINE TRIAD HIT PROTEIN MEMBER; 1.
DR PANTHER; PTHR12978:SF0; M7GPPPX DIPHOSPHATASE; 1.
DR Pfam; PF05652; DcpS; 1.
DR SUPFAM; SSF54197; HIT-like; 1.
DR SUPFAM; SSF102860; mRNA decapping enzyme DcpS N-terminal domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000267027}.
SQ SEQUENCE 249 AA; 28201 MW; 583FF6485CCE6ECB CRC64;
MELAEDCEST TEKSNVAGNG AIETQENAAQ SWLRGATFRE VLGSDVSHKS LFVLLSGVNG
EQGVLLMNKS AFSEDANDIN AILHSAELLE VMKNDIYGSY NAIVAKYRQE EKFIINETAE
DYRTITVEYI EKFQMDLKWV YNILSKECEA ERILFEDPDP YNGFILAPDI KWDSVSLENL
YVLAMIHRRG VRLKYDAPAS STLAAVLLDD VINNLKIAPD YYRRATLSFT RKNSDKLLQM
FREAGRCEA
//
