ID   A0A093I884_STRCA        Unreviewed;       536 AA.
AC   A0A093I884;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   08-NOV-2023, entry version 27.
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   ORFNames=N308_01958 {ECO:0000313|EMBL:KFV88105.1};
OS   Struthio camelus australis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV88105.1, ECO:0000313|Proteomes:UP000053584};
RN   [1] {ECO:0000313|EMBL:KFV88105.1, ECO:0000313|Proteomes:UP000053584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV88105.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KL206989; KFV88105.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093I884; -.
DR   STRING; 441894.ENSSCUP00000020816; -.
DR   Proteomes; UP000053584; Unassembled WGS sequence.
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: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   Nonsense-mediated mRNA decay {ECO:0000256|ARBA:ARBA00023161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053584}.
FT   DOMAIN          493..535
FT                   /note="mRNA-decapping enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16741"
FT   REGION          135..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          365..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV88105.1"
FT   NON_TER         536
FT                   /evidence="ECO:0000313|EMBL:KFV88105.1"
SQ   SEQUENCE   536 AA;  59368 MW;  BD5FE890E0C2C34D CRC64;
     EKTDIEGTLF VYKRSASPYH GFTIVNRLNM HNLVEPVNKD LEFQLHEPFL LYRNASLSIY
     SIWFYDKNDC HRIAKLMAKV VEQEAQRSRQ VCHDRKSPSR TNGCNENRPI DILEMLSKAK
     DEYERNQVSD LSIVSSSGMQ QNANPPKPDS TEASEQATSL QMQDQPFQSR QKHLTLEELF
     GTSVPKEQAA VPYPTPERME TSQPDTSARE QRNLLLPFSF DQSTVIHQPL GKSESPGVKT
     STSALNQQVF LPPASVSQSD VKNISNYSVH LSPVLNSAST MEAAPAQMLP GLKQNNSIMQ
     VMQQAAKQIS PLVNQLPSEV NHAPQNLMAG QSQFVPPLTS TNAGTVSNTS HTSVDLLQKL
     RLTPQHDQMQ QQALTKTSLT PNTSASVGQL ATPESFKESH SKPSTLNSKI ISPLQTAQQN
     KESEPFSQPK SLPKASQVVP PQFVTTTTTV TPSILLSPSV FQQSATKTTE VENKAHSSSP
     LTLATTEIQT IPPTVLSRSQ LQEALIHLIK NDSRFLSTIH EVYLQVLTKN TDNIKL
//