ID M3Y5J8_MUSPF Unreviewed; 341 AA.
AC M3Y5J8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
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 Name=DCPS {ECO:0000313|Ensembl:ENSMPUP00000006599.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000006599.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000006599.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
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 -!- SUBUNIT: Homodimer. Associates with components of the exosome
CC multienzyme ribonuclease complex, such as EXOSC3 and EXOSC4. Interacts
CC with NDOR1. {ECO:0000256|ARBA:ARBA00011140}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC 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; AEYP01027141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01027142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3Y5J8; -.
DR STRING; 9669.ENSMPUP00000006599; -.
DR Ensembl; ENSMPUT00000006712.1; ENSMPUP00000006599.1; ENSMPUG00000006653.1.
DR eggNOG; KOG3969; Eukaryota.
DR GeneTree; ENSGT00390000003924; -.
DR HOGENOM; CLU_041045_2_0_1; -.
DR InParanoid; M3Y5J8; -.
DR OMA; HVHINPI; -.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0140932; F:5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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:0045292; P:mRNA cis splicing, via spliceosome; IEA:Ensembl.
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; IPR019808; Histidine_triad_CS.
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.
DR PROSITE; PS00892; HIT_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR028973};
KW mRNA processing {ECO:0000256|PIRNR:PIRNR028973};
KW Nucleus {ECO:0000256|PIRNR:PIRNR028973};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 281
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-1"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 272..283
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
SQ SEQUENCE 341 AA; 38835 MW; 61A44168B67210CC CRC64;
PSNMANLAPQ PSKRKREPDA EEAEAADIEE GTGVGNGTSA PVRLPFSGFR VKKVLRESAR
DKIIFLHGKV NETSGDGDGD GEDAVVILEK TPFQVEQVAQ LLKGNPELQL QFSNDIYSTY
HLFPPRQLSD VKTTVVYPAT EKHLQKYLRQ DLHLVRETGS DYRNITLPHL ESQSLSIQWV
YNILDKKAET DRIVFENPHP SDGFVLIPDL KWNQQQLDDL YLIAICHRRG IRSLRDLTPE
HLPLLRNILR EGQEAILQRY QVKGDQLRVY LHYLPSYYHL HVHFTALGFE APGTGVERAH
LLANVIENLE CDPDYYQRRT LTFALRADDP LLGLLQEAQT S
//
