ID A0A2K5KKQ5_CERAT Unreviewed; 339 AA.
AC A0A2K5KKQ5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
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:ENSCATP00000001286.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000001286.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000001286.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2K5KKQ5; -.
DR STRING; 9531.ENSCATP00000001286; -.
DR Ensembl; ENSCATT00000006718.1; ENSCATP00000001286.1; ENSCATG00000006118.1.
DR GeneTree; ENSGT00390000003924; -.
DR OMA; HVHINPI; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000006118; Expressed in liver and 12 other cell types or tissues.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060}.
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 277
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-1"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 268..279
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
SQ SEQUENCE 339 AA; 38493 MW; 259A0D105F3832ED CRC64;
MADAAPQLGK RKRELAVEEA QAASTEEKEA GVGNGTCAPV RLPFSGFRVQ KVLRESARDK
IIFLHGKVNE SSGDGDGEDA VVILEKTPFQ VEQVAQLLTG SPELQLQFSN DIYSTYHLFP
PRQLSDVKTT VVYPATEKHL QKYLRQDLRL IRETGDDYRN ITLPHLESQS LSIQWVYNIL
DKKAEVDRIV FENPDPSDGF VLIPDLKWNQ QQLDDLYLIA ICHRRGIRSL RDLTPEHLPL
LRNILHQGQE AILQRYQMKG DRLRVYLHYL PSYYHLHVHF TALGFEAPGS GVERAHLLAE
VIENLECDPR HYQQRTLTFA LRADDPLAQA LAGGSAKLN
//
