ID B3RIU5_TRIAD Unreviewed; 295 AA.
AC B3RIU5;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 66.
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};
GN ORFNames=TRIADDRAFT_18652 {ECO:0000313|EMBL:EDV29254.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV29254.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV29254.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV29254.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
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 EMBL; DS985241; EDV29254.1; -; Genomic_DNA.
DR RefSeq; XP_002108456.1; XM_002108420.1.
DR AlphaFoldDB; B3RIU5; -.
DR STRING; 10228.B3RIU5; -.
DR EnsemblMetazoa; TriadT18652; TriadP18652; TriadG18652.
DR GeneID; 6748866; -.
DR KEGG; tad:TRIADDRAFT_18652; -.
DR CTD; 6748866; -.
DR eggNOG; KOG3969; Eukaryota.
DR HOGENOM; CLU_041045_1_0_1; -.
DR InParanoid; B3RIU5; -.
DR OMA; HVHINPI; -.
DR OrthoDB; 5490768at2759; -.
DR PhylomeDB; B3RIU5; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT ACT_SITE 234
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-1"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 225..236
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
SQ SEQUENCE 295 AA; 34277 MW; 5731D8BA2F3542D7 CRC64;
MPLVNLKDIQ ISRILAENPA SKSINILAKF KDRDGDVILL ISKPPFTKDL MQNIISEDTL
AQVQLENDIY SQYSLTPKAE LNLLKSTVIY PATEKHINKY SDHQFYLLQE TPNDYRNITL
PFIEKNAFSA QWVERILKHE SESENIIFED PDRDTGFILL PDLKWDKKQL SDLYLVAICH
RHGLRSLRDL TSSDLPLLRN IRNQGIAAIK EKYGVNQSQL RIYIHYQPSY YHFHVHFTHV
KYEAPGSVVG RAHLLEDVIE NLELFPNFYS QKTLSFVIQE CDALLAEYRK CGRLT
//
