ID A0A095ASL0_SCHHA Unreviewed; 389 AA.
AC A0A095ASL0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-2023, entry version 33.
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=MS3_0011773 {ECO:0000313|EMBL:KAF1320674.1}, MS3_05736
GN {ECO:0000313|EMBL:KGB37396.1};
OS Schistosoma haematobium (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6185 {ECO:0000313|EMBL:KGB37396.1};
RN [1] {ECO:0000313|EMBL:KGB37396.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22246508; DOI=10.1038/ng.1065;
RA Young N.D., Jex A.R., Li B., Liu S., Yang L., Xiong Z., Li Y.,
RA Cantacessi C., Hall R.S., Xu X., Chen F., Wu X., Zerlotini A., Oliveira G.,
RA Hofmann A., Zhang G., Fang X., Kang Y., Campbell B.E., Loukas A.,
RA Ranganathan S., Rollinson D., Rinaldi G., Brindley P.J., Yang H., Wang J.,
RA Wang J., Gasser R.B.;
RT "Whole-genome sequence of Schistosoma haematobium.";
RL Nat. Genet. 44:221-225(2012).
RN [2] {ECO:0000313|EMBL:KAF1320674.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=31494670;
RA Stroehlein A.J., Korhonen P.K., Chong T.M., Lim Y.L., Chan K.G.,
RA Webster B., Rollinson D., Brindley P.J., Gasser R.B., Young N.D.;
RT "High-quality Schistosoma haematobium genome achieved by single-molecule
RT and long-range sequencing.";
RL Gigascience 8:0-0(2019).
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; AMPZ02000439; KAF1320674.1; -; Genomic_DNA.
DR EMBL; KL250880; KGB37396.1; -; Genomic_DNA.
DR RefSeq; XP_012797158.1; XM_012941704.1.
DR AlphaFoldDB; A0A095ASL0; -.
DR STRING; 6185.A0A095ASL0; -.
DR EnsemblMetazoa; XM_012941704.2; XP_012797158.1; MS3_0011773.
DR OrthoDB; 5490768at2759; -.
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 319
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-1"
SQ SEQUENCE 389 AA; 44564 MW; 9A190FEDC34E17E3 CRC64;
MSENSFRIGD TPVPPKKRAR LDVSTVDTVN GSTDATSFRP ENMHLISVLQ NDLRNKCLVL
HTRFGDDPKE AIVTLQKSSF PNDPNTLKRC KVVNKLIGLH ISDDIDDQCH KKDKTDETEN
DTFPQWQAKS IMKNDIYHRF LITNGLESIN GIEMTVTYPA ESHHFSRYAN SPRHIIQETP
VLYKDVILPF LSQKPKDLTW IDNVVAGIAE QDRTLHNDAD EMFGFTLVLD YRWDGLRIQE
LHCLGIAHDQ KLTCLRDLRS CHVPMLKRIL QLGRDTLLHK YSKSETSDNQ MSGDNPKIIL
SKDQILAYIH YPPTFYRFHI HFVHIDSGDN YGTNACRAHI LEEVIRNLEQ DDLYYANRTI
TMFLHANNPI FAAICQNSSH ISIVGSAPD
//
