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Database: UniProt
Entry: A0A445JWQ1_GLYSO
LinkDB: A0A445JWQ1_GLYSO
Original site: A0A445JWQ1_GLYSO 
ID   A0A445JWQ1_GLYSO        Unreviewed;       672 AA.
AC   A0A445JWQ1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=mRNA guanylyltransferase {ECO:0000256|ARBA:ARBA00012475};
DE            EC=2.7.7.50 {ECO:0000256|ARBA:ARBA00012475};
GN   ORFNames=D0Y65_017851 {ECO:0000313|EMBL:RZC02925.1};
OS   Glycine soja (Wild soybean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3848 {ECO:0000313|EMBL:RZC02925.1, ECO:0000313|Proteomes:UP000289340};
RN   [1] {ECO:0000313|EMBL:RZC02925.1, ECO:0000313|Proteomes:UP000289340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC   TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZC02925.1};
RA   Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT   "A high-quality reference genome of wild soybean provides a powerful tool
RT   to mine soybean genomes.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:RZC02925.1}.
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DR   EMBL; QZWG01000007; RZC02925.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445JWQ1; -.
DR   Proteomes; UP000289340; Chromosome 7.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; 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   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; 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; IPR012310; DNA_ligase_ATP-dep_cent.
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:SF21; MRNA GUANYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR10367; 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; PS50160; DNA_LIGASE_A3; 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|PIRSR:PIRSR036958-3};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289340}.
FT   DOMAIN          104..260
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          179..248
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          431..571
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          45..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        203
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-1"
FT   ACT_SITE        371
FT                   /note="N6-GMP-lysine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-2"
FT   BINDING         376
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   BINDING         391
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   BINDING         422..424
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         609..614
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
SQ   SEQUENCE   672 AA;  79397 MW;  11E1EC5BD2255021 CRC64;
     MIVAVDLNAS PVPEDDEDDF GRQVEEYRTP EERVESAVDI AHQECEERKR KLKREHSDDK
     PVQVSQSPGH DQLFHTKILK SYDRSWLDCP SFGQEIYCMI PSKVPLGESF NDDIIPGKRY
     SFKQVIHQQR VLGRKLDLVI DLTNTSRYYS VADLKKEGIK YVKIQCKGRD SVPDNLSVNH
     FVYEVMQFLL RQKHSRKHIL VHCTHGHNRT GYMIIHYLMR SMSMSVTQAI KIFSDARPPG
     IYKPEYIDAL YAFYHEKKPE MIVCPPTPEW KRTPELVDLN GEAMPDDDDD GVPGSPLHEN
     HVTDTIMRND DVLGDEIPND QQDAFRQFCF RTLKLGVGAR GHMQFPGSHP VSLNRENLQL
     LRQRYYYATW KADGTRYMML ITMDGCYLID RSFNFRRVQM RFPCRITKDG MAEKTHHFTL
     LDGEMIIDTL PDSKKQERRY LIYDLMAING VSVIERPFYE RWKMLEKVIE PRNQERFQSR
     NPYYRYDMEP FRVRRKDFWL LSTVTKLLSE FIPKLSHDAD GLIFQGWDDP YIPRTHEGLL
     KWKYAELNSV DFLFEIDNDC QLLLLYERGK RKLLEGYRVA FEGLDPLHYS GKIIECSWDS
     DRQEWIFKRI RTDKSTPNDF NTYRKVMRSI RDNITEDVLL NEINEIICLP LYADRIRIDS
     KAHIHTNMAR RR
//
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