ID   A0A0M3HNA6_ASCLU        Unreviewed;       410 AA.
AC   A0A0M3HNA6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Decapping nuclease {ECO:0000256|RuleBase:RU367113};
DE            EC=3.6.1.- {ECO:0000256|RuleBase:RU367113};
OS   Ascaris lumbricoides (Giant roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0000313801-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ALUE_0000313801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- FUNCTION: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes
CC       the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs
CC       by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA.
CC       {ECO:0000256|RuleBase:RU367113}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|RuleBase:RU367113};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367113}.
CC   -!- SIMILARITY: Belongs to the DXO/Dom3Z family.
CC       {ECO:0000256|ARBA:ARBA00006562, ECO:0000256|RuleBase:RU367113}.
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DR   AlphaFoldDB; A0A0M3HNA6; -.
DR   WBParaSite; ALUE_0000313801-mRNA-1; ALUE_0000313801-mRNA-1; ALUE_0000313801.
DR   Proteomes; UP000036681; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR013961; RAI1.
DR   InterPro; IPR039039; RAI1-like_fam.
DR   PANTHER; PTHR12395:SF9; DECAPPING AND EXORIBONUCLEASE PROTEIN; 1.
DR   PANTHER; PTHR12395; DOM-3 RELATED; 1.
DR   Pfam; PF08652; RAI1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU367113};
KW   Metal-binding {ECO:0000256|RuleBase:RU367113};
KW   Nuclease {ECO:0000256|RuleBase:RU367113};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU367113};
KW   Nucleus {ECO:0000256|RuleBase:RU367113};
KW   RNA-binding {ECO:0000256|RuleBase:RU367113}.
FT   DOMAIN          271..323
FT                   /note="RAI1-like"
FT                   /evidence="ECO:0000259|Pfam:PF08652"
SQ   SEQUENCE   410 AA;  47934 MW;  1645E58DFEDBF2BF CRC64;
     MEHDGKRTMR PLPETNVVPK RRRLENEKMS TLMSLSEYFP PESFPLYKFP SPIAEYSVTK
     ERNVVPGRAE AKYFYGKILE KDAAFHFDLN KGFEIFESKD DLLQDERLDI LSKWLISRAA
     PNVGLSEVCF HADFVCYRGL LTRIASTPYD VMEDWIVGAV RIGSTIFLCE FRTEEKKLRQ
     EMLDRRDKLM CYWGFKFEQY VTTDSPLVRR KKAFFFFWKE KQLSWSLYLT TPVTDQVVSN
     MKEFDVVMRT TLGNKGGGIR LLFSAETDCL DSEGHYLELK TQAYGMVSNF WKLKAMKWWI
     QSFLAGVQQI VVGIRDNKGV VRSVKRVKVA ELCRRAVDWT PSRTFNFLLD VLTLIKSRMY
     EVHSLSYMLF EYNHANGKIT FRHVPTEGDE FAQYRFLSDD FLKHFGAGAE
//