ID   A0A3Q4G9Z9_NEOBR        Unreviewed;       105 AA.
AC   A0A3Q4G9Z9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
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};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000005316.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000005316.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC         in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H(+) +
CC         N(7)-methyl-GDP; Xref=Rhea:RHEA:67484, Rhea:RHEA-COMP:15692,
CC         Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:63714, ChEBI:CHEBI:138282, ChEBI:CHEBI:156461;
CC         EC=3.6.1.62; Evidence={ECO:0000256|ARBA:ARBA00024496};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67485;
CC         Evidence={ECO:0000256|ARBA:ARBA00024496};
CC   -!- SIMILARITY: Belongs to the DCP1 family.
CC       {ECO:0000256|ARBA:ARBA00008778}.
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DR   AlphaFoldDB; A0A3Q4G9Z9; -.
DR   Ensembl; ENSNBRT00000005474.1; ENSNBRP00000005316.1; ENSNBRG00000004185.1.
DR   GeneTree; ENSGT00940000158409; -.
DR   Proteomes; UP000261580; Unplaced.
DR   Bgee; ENSNBRG00000004185; Expressed in testis and 9 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR   GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR   GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:InterPro.
DR   CDD; cd09804; Dcp1; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR010334; Dcp1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   PANTHER; PTHR16290:SF5; MRNA-DECAPPING ENZYME 1B; 1.
DR   PANTHER; PTHR16290; TRANSCRIPTION FACTOR SMIF DECAPPING ENZYME DCP1; 1.
DR   Pfam; PF06058; DCP1; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000261580}.
SQ   SEQUENCE   105 AA;  12270 MW;  EED020114E174AC7 CRC64;
     CEAIRLDISL AALQRQDPYI NNIVDLASQV ALYTFNNRTN EWEKTEVEGS LFIYTRLASP
     RHGFTIMNRL SMQNLTEPLT KDLDFQLQDP FLLYRNARCK EKLTD
//