ID   A0A1I7V4S5_9PELO        Unreviewed;       309 AA.
AC   A0A1I7V4S5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=m7GpppX diphosphatase {ECO:0000256|ARBA:ARBA00015636, ECO:0000256|PIRNR:PIRNR028973};
DE            EC=3.6.1.59 {ECO:0000256|ARBA:ARBA00012520, ECO:0000256|PIRNR:PIRNR028973};
OS   Caenorhabditis tropicalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold75.g457.t1};
RN   [1] {ECO:0000313|WBParaSite:Csp11.Scaffold75.g457.t1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- FUNCTION: Decapping scavenger enzyme that catalyzes the cleavage of a
CC       residual cap structure following the degradation of mRNAs by the 3'->5'
CC       exosome-mediated mRNA decay pathway. {ECO:0000256|PIRNR:PIRNR028973}.
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         ECO:0000256|PIRNR:PIRNR028973};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR028973}.
CC   -!- SIMILARITY: Belongs to the HIT family. {ECO:0000256|ARBA:ARBA00010208,
CC       ECO:0000256|PIRNR:PIRNR028973}.
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DR   AlphaFoldDB; A0A1I7V4S5; -.
DR   STRING; 1561998.A0A1I7V4S5; -.
DR   WBParaSite; Csp11.Scaffold75.g457.t1; Csp11.Scaffold75.g457.t1; Csp11.Scaffold75.g457.
DR   Proteomes; UP000095282; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140932; F:5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:UniProtKB-UniRule.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.428.10; HIT-like; 1.
DR   Gene3D; 3.30.200.40; Scavenger mRNA decapping enzyme, N-terminal domain; 1.
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   Pfam; PF11969; DcpS_C; 1.
DR   PIRSF; PIRSF028973; Scavenger_mRNA_decap_enz; 1.
DR   SUPFAM; SSF54197; HIT-like; 1.
DR   SUPFAM; SSF102860; mRNA decapping enzyme DcpS N-terminal domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR028973};
KW   mRNA processing {ECO:0000256|PIRNR:PIRNR028973};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR028973}.
FT   ACT_SITE        251
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028973-1"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT   BINDING         181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT   BINDING         242..253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
SQ   SEQUENCE   309 AA;  36034 MW;  54A8849EBB812C17 CRC64;
     MKRVADGQLT EEERTEASSQ EWLKTAKFQE VLGADSSHKS LFLLLSQPDG SQGILLANKS
     PFSEDKADIE KLLETAKLQE ISRNDIFGSY NIEVDAGLNL LKSQLIYPVN DRLIAKYRQE
     EKYVIRETPE LYEKVTKPYI EKFQLNLNWV YNCLEKRSEV DKIIFEDEDR TNGFLLLQDI
     KWDGKTLENL YLLAIIHRHG LKSVRDLTGD DLEMLYNIRD KSLKAINEKY GLRTDQIKCY
     FHYQPSFYHL HVHFINLKYD APASTTMSAI LLDDVINNLE LNPDHYKKST LTFTRKHGDK
     LTEMFQISQ
//