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Database: UniProt
Entry: A0A3P8Y2L4_ESOLU
LinkDB: A0A3P8Y2L4_ESOLU
Original site: A0A3P8Y2L4_ESOLU 
ID   A0A3P8Y2L4_ESOLU        Unreviewed;       632 AA.
AC   A0A3P8Y2L4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 2.
DT   24-JAN-2024, entry version 25.
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   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000010892.2, ECO:0000313|Proteomes:UP000265140};
RN   [1] {ECO:0000313|Ensembl:ENSELUP00000010892.2, ECO:0000313|Proteomes:UP000265140}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25069045;
RA   Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA   von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT   "The genome and linkage map of the northern pike (Esox lucius): conserved
RT   synteny revealed between the salmonid sister group and the Neoteleostei.";
RL   PLoS ONE 9:e102089-e102089(2014).
RN   [2] {ECO:0000313|Ensembl:ENSELUP00000010892.2}
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; A0A3P8Y2L4; -.
DR   SMR; A0A3P8Y2L4; -.
DR   STRING; 8010.ENSELUP00000010892; -.
DR   Ensembl; ENSELUT00000001386.2; ENSELUP00000010892.2; ENSELUG00000011344.2.
DR   GeneTree; ENSGT00940000158409; -.
DR   InParanoid; A0A3P8Y2L4; -.
DR   OMA; LPMRQGV; -.
DR   Proteomes; UP000265140; LG18.
DR   Bgee; ENSELUG00000011344; Expressed in head kidney and 14 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   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR   CDD; cd09804; Dcp1; 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:SF0; DECAPPING PROTEIN 1, ISOFORM A; 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   Nonsense-mediated mRNA decay {ECO:0000256|ARBA:ARBA00023161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265140}.
FT   DOMAIN          592..631
FT                   /note="mRNA-decapping enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16741"
FT   REGION          141..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          316..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..191
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..443
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..579
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   632 AA;  68678 MW;  09825B2E3CF01E74 CRC64;
     MTASSSGGNT CLTAKGLDIS LAALQRQDPY INNIVDVASQ VALYTFNNRS NEWEKTDVEG
     TLFVYTRLAS PRHGFTIMNR LSMENLTEPI TKDLDFQLQD PFLLYRNARL AIYGIWFYDK
     VDCQRIAELM KNLTKQEQAL AQQSRSGWES PGDLEAAEDP GKTRGVDILQ MLTKARDEYD
     KGGKPEPKEI GRSVLQDNPN LIKPIPVKPM DRHPQPGLQE RPVQDQGEPR PLSLATLFGV
     QQASRGPVSP MSGYGAPGSQ PQAKPAGVRP AVARSLSYED PSQSRLQAQP GAPAPGSGPQ
     QHCPAFQKLM REASTQPGLQ RGGPMELLQP VSESPENRLL ENGAPSTLHH QAQQDPIQRL
     FQNQPTSATL SLTSCSSTAS CCSRPSPLQQ PPHLLPGLQP AQPLLVDPAG FHHHPNLVPH
     QSQPIFFTPT KASQMQASLP SKSLPPSPHL PPYLQQQVSV PRGSPSHLAL QPQPGHPQPG
     QLAGVVPPGE LLQRLQLVQQ EQGLVPVTAR PASNLAPRFH EKLSAGSAAQ KFQVISPQRI
     PATVAPTLLL SPSVFSQAKP PQVQPKAPGD PPGPPTALLS PRAPDETQSW GLTKSQLQAT
     LLHLIQNDSS FLDTIYKAYT QSFSSKTNTD KF
//
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