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Database: UniProt
Entry: A0A0E0BGR7_9ORYZ
LinkDB: A0A0E0BGR7_9ORYZ
Original site: A0A0E0BGR7_9ORYZ 
ID   A0A0E0BGR7_9ORYZ        Unreviewed;       671 AA.
AC   A0A0E0BGR7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=mRNA guanylyltransferase {ECO:0000256|ARBA:ARBA00012475};
DE            EC=2.7.7.50 {ECO:0000256|ARBA:ARBA00012475};
OS   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM11G06570.1};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM11G06570.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM11G06570.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-
CC         end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate;
CC         Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50;
CC         Evidence={ECO:0000256|ARBA:ARBA00024520};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013;
CC         Evidence={ECO:0000256|ARBA:ARBA00024520};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   AlphaFoldDB; A0A0E0BGR7; -.
DR   STRING; 40148.A0A0E0BGR7; -.
DR   EnsemblPlants; OGLUM11G06570.1; OGLUM11G06570.1; OGLUM11G06570.
DR   Gramene; OGLUM11G06570.1; OGLUM11G06570.1; OGLUM11G06570.
DR   eggNOG; KOG2386; Eukaryota.
DR   HOGENOM; CLU_021710_3_1_1; -.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140818; F:mRNA 5'-phosphatase activity; IEA:InterPro.
DR   GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd07895; Adenylation_mRNA_capping; 1.
DR   CDD; cd14502; RNA_5'-triphosphatase; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR017074; mRNA_cap_enz_bifunc.
DR   InterPro; IPR001339; mRNA_cap_enzyme_adenylation.
DR   InterPro; IPR013846; mRNA_cap_enzyme_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR10367; MRNA-CAPPING ENZYME; 1.
DR   PANTHER; PTHR10367:SF17; MRNA-CAPPING ENZYME; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   Pfam; PF03919; mRNA_cap_C; 1.
DR   Pfam; PF01331; mRNA_cap_enzyme; 1.
DR   PIRSF; PIRSF036958; mRNA_capping_HCE; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   4: Predicted;
KW   GTP-binding {ECO:0000256|PIRSR:PIRSR036958-3};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   mRNA capping {ECO:0000256|ARBA:ARBA00023042};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR036958-3};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          109..262
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          179..250
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          26..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          268..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        205
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-1"
FT   ACT_SITE        370
FT                   /note="N6-GMP-lysine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-2"
FT   BINDING         375
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   BINDING         390
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   BINDING         417..419
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   BINDING         541..543
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   BINDING         611..616
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
SQ   SEQUENCE   671 AA;  78672 MW;  E2D6BED6ED572A80 CRC64;
     MDLNASPLPE EDEQPYEQQV EVDFAQEEHV ESAVATMRRE REERRKKLKR EQQDEGSRLH
     SQQIRNDYAP YNRAGRGRIK EAPDGWMNCP AFGEPIDKII PSKVPLDETF NDSVPPGKRY
     SSKQVVNKQR KAGREIGLVI DLTNTTRYYS PAEWTRQGIK HVKIPCKGRD AVPDNESVNW
     FVYEVMMFLD RQKQSKNPKY ILVHCTHGHN RTGFMIIHYL MRTQVSCVAE AINIFAKRRP
     PGIYKRDYIE ALYSFYHEVP EHMITCPSTP EWKRSSDLDL NGEAKQDDDD ENGDLAPVHN
     EVEDKVITND DVLGDAVPYD QQDALRVVCY RLLEMPPVRG HAQFPGSHPV SLNSENLQLL
     RQRYYFATWK ADGTRYMMLI MRDGCFLIDR NFCFRRVQMR FPHRNLNEGL HEMTLIDGEM
     IIDTVPDSGL KRRYLAYDLM ALDAVSKTKL PFSERWRLLE DEIIRPRYYE KKQFESGVKS
     NPMYKYDMEL FSVRRKDFWL LSTVTKLLKE FIPSLSHDAD GLIFQGWDDP YVTRTHEGLL
     KWKYPSMNSV DFLFEVGGDN RQLVFLYERG KKKLMDGSRI AFPNEEDPSS ISGRIVECSW
     NKEEGCWVCM RIRSDKSTPN DINTYRKVMR SITDNITEEK LLEEIHEITR LPMYADRIKQ
     AQAKMAQHRR R
//
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