ID   A0A3B6ARF2_WHEAT        Unreviewed;       679 AA.
AC   A0A3B6ARF2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   29-SEP-2021, entry version 16.
DE   RecName: Full=GTP--RNA guanylyltransferase {ECO:0000256|ARBA:ARBA00018051};
DE            EC=2.7.7.50 {ECO:0000256|ARBA:ARBA00012475};
DE   AltName: Full=mRNA guanylyltransferase {ECO:0000256|ARBA:ARBA00016289};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS2A02G065100.4};
RN   [1] {ECO:0000313|EnsemblPlants:TraesCS2A02G065100.4}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) 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:ARBA00024268};
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DR   SMR; A0A3B6ARF2; -.
DR   EnsemblPlants; TraesCS2A02G065100.4; TraesCS2A02G065100.4; TraesCS2A02G065100.
DR   Gramene; TraesCS2A02G065100.4; TraesCS2A02G065100.4; TraesCS2A02G065100.
DR   OMA; IVECAWD; -.
DR   Proteomes; UP000019116; Unplaced.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004484; F:mRNA guanylyltransferase activity; IBA:GO_Central.
DR   GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IEA:InterPro.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0006370; P:7-methylguanosine mRNA capping; IBA:GO_Central.
DR   CDD; cd07895; Adenylation_mRNA_capping; 1.
DR   Gene3D; 3.90.190.10; -; 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_PHOSPHATASE_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
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; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE   4: Predicted;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRSR:PIRSR036958-
KW   3}; 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:UP000019116}.
FT   DOMAIN          180..251
FT                   /note="TYR_PHOSPHATASE_2"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   NP_BIND         418..420
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   NP_BIND         542..544
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   NP_BIND         612..617
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          660..679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..26
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..297
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        206
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                   /note="GTP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   BINDING         391
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
SQ   SEQUENCE   679 AA;  78890 MW;  2C9AE9FE1A386FBD CRC64;
     MDLNASPLPE EDDHEEPVEL DFGQDDEDHV ESAVEIMRRE REERRRKLKR DQPDDGPRPR
     PQQVRNDHVT QNKIGGYKRV KETPQGWLDC PASGQPIDKI IPSKVPLDET FNESIPPGKR
     YSSKQVVNKQ RKAGRDIGLV IDLTNTSRYY SPAEWTKQGT KHVKIACRGR DAVPENEAVN
     TFVYEVLAFH ERQKPSRNPK YVLVHCTHGH NRTGFMIVHY LMRTQLSSVT EALNIFAQRR
     PPGIYKTDYI QALYTFYHEI PESITCPPTP EWKRPSDLDL NGEAKQDDDD DNGEPAPSPD
     PVDDKAITND DVLGDAVPFD QQDILRGICF KLLDFVPNGR ANAQFPGSHP VSLNSENLQL
     LRQRYYYATW KADGTRYMML IMRDGCFLID RNFCFRRVQM RFPIRNVNDG FHNFTLIDGE
     MVVDTIPGGG LKRRYLAYDL MAINFSSKVK LPFSDRWKLL EDEIIRPRIY ERKQFETGLK
     GNPSYRYDLE LFSVRRKDFW LLSTVKKLLK EFIPALSHES DGLIFQGWDD PYVNRTHEGL
     LKWKYPEMNS VDFLFETGSE NRQLIFLYER GKKKLMDGTR VVFPDDVDPS SISGKIVECS
     WNKQEDCWFC MRIRADKSTP NDINTYRKVM RSITDNITED KLLGEMNEIS SLPMYADRKA
     HADRKAHAEK MAHQHRRRG
//