ID A0AAD9F9S5_DISEL Unreviewed; 498 AA.
AC A0AAD9F9S5;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 8.
DE RecName: Full=5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase {ECO:0000256|ARBA:ARBA00026102};
DE EC=3.6.1.62 {ECO:0000256|ARBA:ARBA00026102};
GN ORFNames=KUDE01_017699 {ECO:0000313|EMBL:KAK1898173.1};
OS Dissostichus eleginoides (Patagonian toothfish) (Dissostichus amissus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Dissostichus.
OX NCBI_TaxID=100907 {ECO:0000313|EMBL:KAK1898173.1, ECO:0000313|Proteomes:UP001228049};
RN [1] {ECO:0000313|EMBL:KAK1898173.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DE {ECO:0000313|EMBL:KAK1898173.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAK1898173.1};
RA Park H.;
RT "Chromosome-level genome of Chaenocephalus aceratus.";
RL Submitted (APR-2023) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DCP1 family.
CC {ECO:0000256|ARBA:ARBA00008778}.
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:KAK1898173.1}.
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DR EMBL; JASDAP010000008; KAK1898173.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAD9F9S5; -.
DR Proteomes; UP001228049; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IEA:TreeGrafter.
DR GO; GO:0140933; F:5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; IEA:TreeGrafter.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:InterPro.
DR GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IEA:TreeGrafter.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR CDD; cd09804; Dcp1; 1.
DR FunFam; 2.30.29.30:FF:000097; Putative mRNA-decapping enzyme 1A; 1.
DR Gene3D; 6.10.140.2030; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR010334; Dcp1.
DR InterPro; IPR031953; mRNA_decap_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR16290:SF4; MRNA-DECAPPING ENZYME 1A; 1.
DR PANTHER; PTHR16290; TRANSCRIPTION FACTOR SMIF DECAPPING ENZYME DCP1; 1.
DR Pfam; PF06058; DCP1; 1.
DR Pfam; PF16741; mRNA_decap_C; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nonsense-mediated mRNA decay {ECO:0000256|ARBA:ARBA00023161};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP001228049}.
FT DOMAIN 456..497
FT /note="mRNA-decapping enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16741"
FT REGION 129..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 54327 MW; 8C99B4CDFBDB64AD CRC64;
METVNAGQMM SLAALQRQDP YINKLLDVTG QVALYNFNSK ANEWEKTEIE GTLFVYARSA
TPHHGFTIMN RLSTENLVEP INKDLEFQLQ DPFLLYRNGN LGIYSIWFYD KRDCQRIAQL
MVKIVKQEAE HARRESPERA APGRSNGVAE PRPIDILELL SKAKEEYQRA QVGETDASAE
LNLKTTFTAT EQSTPKAEKS SHTMVKQITV EELFGSSLPK GPSLPIMPTQ NSSTASSDPS
TAYLQNQPYP TPALQTPLFP PHHSPQDPAS GQRHQVPGLL PAPYALQPGS VFQSAVLRSD
PQPRCSVSPL MVVPAGPEPH AAPSATPTAY LGQDMLATLK AAVPSVNHDI HKPILAPNFL
PNRLFTPHSF QEPAVRPSLQ HSKEMDVFSQ PPNLIKPMSA VPMSPGFAVP GPAFSLLLSP
SAFQQSFSQT SAASAAPPSP SEPSYPSSGA LEPPPAACSK TQLQDTLIHL IKSDPDFLSA
IHDAYLQSVS KDFSNMKL
//
