ID A0A7L0KS76_9SYLV Unreviewed; 590 AA.
AC A0A7L0KS76;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 17.
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};
DE Flags: Fragment;
GN Name=Dcp1b {ECO:0000313|EMBL:NXK59708.1};
GN ORFNames=SYLVIR_R00352 {ECO:0000313|EMBL:NXK59708.1};
OS Sylvietta virens (Green crombec).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Sylvioidea; Sylviidae; Acrocephalinae; Sylvietta.
OX NCBI_TaxID=208069 {ECO:0000313|EMBL:NXK59708.1, ECO:0000313|Proteomes:UP000567822};
RN [1] {ECO:0000313|EMBL:NXK59708.1, ECO:0000313|Proteomes:UP000567822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-009-59 {ECO:0000313|EMBL:NXK59708.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXK59708.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) 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:NXK59708.1}.
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DR EMBL; VXAN01000031; NXK59708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7L0KS76; -.
DR Proteomes; UP000567822; 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:SF5; MRNA-DECAPPING ENZYME 1B; 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:UP000567822}.
FT DOMAIN 548..588
FT /note="mRNA-decapping enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16741"
FT REGION 181..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..347
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..535
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXK59708.1"
FT NON_TER 590
FT /evidence="ECO:0000313|EMBL:NXK59708.1"
SQ SEQUENCE 590 AA; 64499 MW; CE3C908803CFA118 CRC64;
LGRGLDISLA ALRQHDPYIS GIVDVASQVA LYTFGHRASQ WEKTDVEGTL FVYTRSASPR
HGFTIMNRLS MENRTEPITK DLDFQLQDPF LLYRNARLSI YGIWFYDKEE CQRIAELMKN
LTQQEQFKAQ QGTGTGVSPM IMNSANNKEV DILRMLTKAK DEYTKCKTCS EPKQITSSSA
IYNNPNLIKP IPVKPSENQH QRISQQSKSV DPEPQHLSLT ALFGKQEKAD VSEAPSKQHQ
ENLPARQGVV RSLSYEEPSR HSPCAEKQLC PAIQKLMVRG TELQPLAEFP ESRLCENGAI
PAVGETLAGL FQPVPSHGIA ASHGAQDAAG TQSLLQKLQS QSGSGTKMDP SATAPVNSTA
SVFTRTPAPV GAPVNNVSQP PLVYFNGSLP GQTLEPQTLG KEQSKLPRQP LPLSGNQAAN
SGVISPQELL KKLQIVQQEQ QLHVSSRPTL AAKFPVVTQN TNTLKPLDSW IEKAPGTEKQ
SALFQVISPQ RIPATVTPTL LMSPMVFSQP TPAAPKAAER AANPEPAASP ASLLLPLPAP
EPALANSSSI TKMQLQETLL HLIQNDDNFL NIIYEAYLFS VRKAAMKKSM
//
