ID A0AA39F1P4_MICHY Unreviewed; 424 AA.
AC A0AA39F1P4;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE RecName: Full=m7GpppN-mRNA hydrolase {ECO:0000256|ARBA:ARBA00068566};
DE AltName: Full=mRNA-decapping enzyme 2 {ECO:0000256|ARBA:ARBA00078183};
GN ORFNames=PV327_009640 {ECO:0000313|EMBL:KAK0161128.1};
OS Microctonus hyperodae (Parasitoid wasp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Ichneumonoidea; Braconidae;
OC Euphorinae; Microctonus.
OX NCBI_TaxID=165561 {ECO:0000313|EMBL:KAK0161128.1, ECO:0000313|Proteomes:UP001168972};
RN [1] {ECO:0000313|EMBL:KAK0161128.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Lincoln {ECO:0000313|EMBL:KAK0161128.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KAK0161128.1};
RA Inwood S., Skelly J., Guhlin J., Harrop T., Goldson S., Dearden P.;
RT "Scaffold-level genome assemblies of two parasitoid biocontrol wasps reveal
RT the parthenogenesis mechanism and an associated novel virus.";
RL bioRxiv 0:0-0(2023).
RN [2] {ECO:0000313|EMBL:KAK0161128.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Lincoln {ECO:0000313|EMBL:KAK0161128.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KAK0161128.1};
RA Inwood S.N., Skelly J.G., Guhlin J., Harrop T.W.R., Goldson S.G.,
RA Dearden P.K.;
RL Submitted (MAR-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Decapping metalloenzyme that catalyzes the cleavage of the
CC cap structure on mRNAs. Removes the 7-methyl guanine cap structure from
CC mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP.
CC Necessary for the degradation of mRNAs, both in normal mRNA turnover
CC and in nonsense-mediated mRNA decay. Plays a role in replication-
CC dependent histone mRNA degradation. Has higher activity towards mRNAs
CC that lack a poly(A) tail. Has no activity towards a cap structure
CC lacking an RNA moiety. The presence of a N(6)-methyladenosine
CC methylation at the second transcribed position of mRNAs (N(6),2'-O-
CC dimethyladenosine cap; m6A(m)) provides resistance to DCP2-mediated
CC decapping. Blocks autophagy in nutrient-rich conditions by repressing
CC the expression of ATG-related genes through degradation of their
CC transcripts. {ECO:0000256|ARBA:ARBA00060003}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + H2O = N(7)-methyl-GDP + a 5'-end phospho-ribonucleoside in
CC mRNA + 2 H(+); Xref=Rhea:RHEA:67484, Rhea:RHEA-COMP:15692, Rhea:RHEA-
CC COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:63714,
CC ChEBI:CHEBI:138282, ChEBI:CHEBI:156461; EC=3.6.1.62;
CC Evidence={ECO:0000256|ARBA:ARBA00047661};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67485;
CC Evidence={ECO:0000256|ARBA:ARBA00047661};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC {ECO:0000256|ARBA:ARBA00004201}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DCP2 subfamily.
CC {ECO:0000256|ARBA:ARBA00005279}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAK0161128.1}.
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DR EMBL; JAQQBR010001835; KAK0161128.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AA39F1P4; -.
DR Proteomes; UP001168972; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0140933; F:5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:InterPro.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:InterPro.
DR CDD; cd03672; NUDIX_Dcp2p_Nudt20; 1.
DR FunFam; 1.10.10.1050:FF:000001; M7GpppN-mRNA hydrolase isoform 2; 1.
DR FunFam; 3.90.79.10:FF:000003; M7GpppN-mRNA hydrolase isoform 2; 1.
DR Gene3D; 1.10.10.1050; Dcp2, box A domain; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR007722; DCP2_BoxA.
DR InterPro; IPR036189; DCP2_BoxA_sf.
DR InterPro; IPR044099; Dcp2_NUDIX.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR23114; M7GPPPN-MRNA HYDROLASE; 1.
DR PANTHER; PTHR23114:SF17; M7GPPPN-MRNA HYDROLASE; 1.
DR Pfam; PF05026; DCP2; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SMART; SM01125; DCP2; 1.
DR SUPFAM; SSF140586; Dcp2 domain-like; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP001168972};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 95..226
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT REGION 285..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 49146 MW; F9557C2CF71D8982 CRC64;
MAEHAIPLDI LDDLSSRFII NVPEEERKDL IRFCFQIELA HWFYLDFYCT DDNTRGLKPC
NMKEFTMHIF QHIPFLRMHI SRVDTILEQW REYKQSVPTF GAIVLNEDMT RVLLVQNYWA
KNSWGFPKGK VNEDEDPSHC AAREVFEETG FDISNLIDKN EYIESIINDR LVRLYIITGV
QKDTKFEPQT RKEIKNVEWF ALADLPNTSK DMTPKVKMGV GPNAFFMVVP FIKRMKRWVL
EKRQKDKQAS TSKRHRHKSL GDVDVVLKGN RHHQQIHIVH NNTIDSKNSR QSNTSPIRNK
RTVEYKNTPK GIGGDKNSSK AGIKRNLFGD LTDDKNVKSP NTVLAKQLID SPGVIASNRK
NKLTQQAVIS EEVKHADEKK NSAFDNAVDK LHPMSISELC DKFNLRSSAW NHFEFDMQAI
LNCI
//
