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Database: UniProt
Entry: A0A2I3MPQ6_PAPAN
LinkDB: A0A2I3MPQ6_PAPAN
Original site: A0A2I3MPQ6_PAPAN 
ID   A0A2I3MPQ6_PAPAN        Unreviewed;       590 AA.
AC   A0A2I3MPQ6;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   24-JAN-2024, 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};
GN   Name=DCP1A {ECO:0000313|Ensembl:ENSPANP00000037717.2};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000037717.2, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000037717.2, ECO:0000313|Proteomes:UP000028761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA   Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA   Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA   Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA   Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA   Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA   Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA   Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA   Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA   Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA   Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA   Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA   Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA   Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA   Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA   Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA   Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA   Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA   Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA   Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA   Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA   Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA   Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT   "Whole Genome Assembly of Papio anubis.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPANP00000037717.2}
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; A0A2I3MPQ6; -.
DR   Ensembl; ENSPANT00000038720.2; ENSPANP00000037717.2; ENSPANG00000011562.3.
DR   GeneTree; ENSGT00940000158818; -.
DR   OMA; PGFKMES; -.
DR   Proteomes; UP000028761; Chromosome 2.
DR   Bgee; ENSPANG00000011562; Expressed in testis and 66 other cell types or tissues.
DR   ExpressionAtlas; A0A2I3MPQ6; baseline.
DR   GO; GO:0000932; C:P-body; IEA:Ensembl.
DR   GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:InterPro.
DR   GO; GO:1903608; P:protein localization to cytoplasmic stress granule; IEA:Ensembl.
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; 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   SUPFAM; SSF50729; PH domain-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000028761}.
FT   REGION          132..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..283
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   590 AA;  64039 MW;  BE1DFC5E8F511846 CRC64;
     MEALSRAGQE MSLAALKQHD PYITSIADLT GQVALYTFCP KANQWEKTDI EGTLFVYRRS
     ASPYHGFTIV NRLNMHNLVE PVNKDLEFQL HEPFLLYRNA SLSIYSIWFY DKNDCHRIAK
     LMADVVEEET RRSQQAARDK QSPSQANGCS DHRPIDILEM LSRAKDEYER NQMGDSNISS
     PGLQPSTQLS NLGSTETLEE TPSGSQDKSA PSGHKHLTVE ELFGTSLPKE QPAVVGLDSE
     EVERLPGDAS QKEPNSFLPF PFEQSGGAPQ SETLGVPSAA HHSVQPEITT PVLITPASIT
     QSNEKHAPTY TIPLSPVLSP TLPSEAPTTQ VPPSLPRNST MIQAVKTTPR QRSPLLNQPV
     PELSHAGLIA SQSPFRAPLN VANTAGTSLP SVDLLQKLRL TPQHDQIQTQ PLGKGAMVAS
     FSPAAGQLAT PESFIEPPSK TAAARAAASA SLSNMVLAPL QSMQQNQDPE VFVQPKVLSS
     AIPVAGAPLV TATTTAVSSV LLAPSVFQQT VTRSSDLERK ASSPSPLTIG TPESQRKPSI
     ILSKSQLQDT LIHLIKVCRI PILSLIFHYL IKEIVYIPPT ESVHKVNSKD
//
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