ID G7MRL7_MACMU Unreviewed; 396 AA.
AC G7MRL7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Decapping nuclease {ECO:0000256|RuleBase:RU367113};
DE EC=3.6.1.- {ECO:0000256|RuleBase:RU367113};
GN ORFNames=EGK_14741 {ECO:0000313|EMBL:EHH18190.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:EHH18190.1};
RN [1] {ECO:0000313|EMBL:EHH18190.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-5 {ECO:0000313|EMBL:EHH18190.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end CoA-ribonucleoside in mRNA + H2O = 3'-dephospho-CoA +
CC a 5'-end phospho-ribonucleoside in mRNA + H(+); Xref=Rhea:RHEA:67496,
CC Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17276, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57328, ChEBI:CHEBI:138282,
CC ChEBI:CHEBI:172371; Evidence={ECO:0000256|ARBA:ARBA00024564};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67497;
CC Evidence={ECO:0000256|ARBA:ARBA00024564};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end FAD-phospho-ribonucleoside in mRNA + H2O = a 5'-end
CC phospho-ribonucleoside in mRNA + FAD + H(+); Xref=Rhea:RHEA:67492,
CC Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17275, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:138282,
CC ChEBI:CHEBI:172372; Evidence={ECO:0000256|ARBA:ARBA00024458};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67493;
CC Evidence={ECO:0000256|ARBA:ARBA00024458};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in snoRNA + H2O = a 5'-
CC end phospho-ribonucleoside in snoRNA + H(+) + NAD(+);
CC Xref=Rhea:RHEA:60892, Rhea:RHEA-COMP:15699, Rhea:RHEA-COMP:15700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:138282, ChEBI:CHEBI:144029;
CC Evidence={ECO:0000256|ARBA:ARBA00023687};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60893;
CC Evidence={ECO:0000256|ARBA:ARBA00023687};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU367113};
CC Note=Binds 2 magnesium ions. {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 EMBL; CM001256; EHH18190.1; -; Genomic_DNA.
DR AlphaFoldDB; G7MRL7; -.
DR Proteomes; UP000013456; Chromosome 4.
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 Magnesium {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 235..301
FT /note="RAI1-like"
FT /evidence="ECO:0000259|Pfam:PF08652"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 396 AA; 44936 MW; C43682333CE7DB77 CRC64;
MDPGGTKRGA EKTEVAEPRN KLPRPAPSLP TDPALYSGPF PFYRRPSELG CFSLDAQRQY
HGDARALRYY SPPPTNGPGP NFDLRDGYPD RYQPRDEEVQ ERLDHLLCWL LEHRGRLEGG
PGWLAEAIVT WRGHLTKLLT TPYERQEGWQ LAASRFQGTL YLSEVETPKA RAQRLARPPL
LRELMYMGYK FEQYMCADKP GSSPDPSGEV NTNVAFCSVL RSRLGSHPLL FSGEVDCTDP
QTPSTQPPTC YVELKTSKEM HSPGQWRSFY RHKLLKWWAQ SFLPGVPNVV AGFRNPEGFV
SSLKTFPTMK MFDYVRNDRD GWNPSVCMNF CAAFLSFAQS TVVQDDPRLV HLFSWEPGGP
VTVSVHRDAP YAFLPIWYVE AMTQDFPSPP KTPSPK
//
