ID F2DPF4_HORVV Unreviewed; 684 AA.
AC F2DPF4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=mRNA guanylyltransferase {ECO:0000256|ARBA:ARBA00012475};
DE EC=2.7.7.50 {ECO:0000256|ARBA:ARBA00012475};
OS Hordeum vulgare subsp. vulgare (Domesticated barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=112509 {ECO:0000313|EMBL:BAJ96975.1};
RN [1] {ECO:0000313|EMBL:BAJ96975.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Shoot and root {ECO:0000313|EMBL:BAJ96975.1};
RX PubMed=21415278; DOI=10.1104/pp.110.171579;
RA Matsumoto T., Tanaka T., Sakai H., Amano N., Kanamori H., Kurita K.,
RA Kikuta A., Kamiya K., Yamamoto M., Ikawa H., Fujii N., Hori K., Itoh T.,
RA Sato K.;
RT "Comprehensive sequence analysis of 24,783 barley full-length cDNAs derived
RT from 12 clone libraries.";
RL Plant Physiol. 156:20-28(2011).
RN [2] {ECO:0000313|Proteomes:UP000011116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Morex {ECO:0000313|Proteomes:UP000011116};
RX PubMed=23075845; DOI=10.1038/nature11543;
RG The International Barley Genome Sequencing Consortium;
RA Mayer K.F., Waugh R., Brown J.W., Schulman A., Langridge P., Platzer M.,
RA Fincher G.B., Muehlbauer G.J., Sato K., Close T.J., Wise R.P., Stein N.;
RT "A physical, genetic and functional sequence assembly of the barley
RT genome.";
RL Nature 491:711-716(2012).
RN [3] {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.4HG0345360.1}
RP IDENTIFICATION.
RC STRAIN=subsp. vulgare
RC {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.4HG0345360.1};
RG EnsemblPlants;
RL Submitted (JAN-2022) 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 EMBL; AK365772; BAJ96975.1; -; mRNA.
DR AlphaFoldDB; F2DPF4; -.
DR STRING; 112509.F2DPF4; -.
DR EnsemblPlants; HORVU.MOREX.r3.4HG0345360.1; HORVU.MOREX.r3.4HG0345360.1; HORVU.MOREX.r3.4HG0345360.
DR Gramene; HORVU.MOREX.r2.4HG0288290.1; HORVU.MOREX.r2.4HG0288290.1; HORVU.MOREX.r2.4HG0288290.
DR Gramene; HORVU.MOREX.r2.4HG0288290.1.mrna1; HORVU.MOREX.r2.4HG0288290.1.mrna1; HORVU.MOREX.r2.4HG0288290.1.
DR Gramene; HORVU.MOREX.r3.4HG0345360.1; HORVU.MOREX.r3.4HG0345360.1; HORVU.MOREX.r3.4HG0345360.
DR eggNOG; KOG2386; Eukaryota.
DR OrthoDB; 49440at2759; -.
DR Proteomes; UP000011116; Chromosome 4H.
DR ExpressionAtlas; F2DPF4; baseline and differential.
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; IBA:GO_Central.
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 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.
PE 2: Evidence at transcript level;
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:UP000011116};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 186..257
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 212
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-1"
FT ACT_SITE 378
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-2"
FT BINDING 383
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT BINDING 398
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT BINDING 425..427
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT BINDING 549..551
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT BINDING 619..624
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
SQ SEQUENCE 684 AA; 80112 MW; 165A92675DE687D0 CRC64;
MTFSMDLNAS PLPEEEDEQP YEELPGEADY AHEEEHVESA VATLRREREE RRRKLKREHQ
DEGSMQHPQQ IRNDYAPPIK VGRGRIKEAP EGWLGCPAFG EPIDKIIPSK VPLDETFNES
VPPGKRYSSK QAVNKQRKAG REIGLVIDLT NTSRYYSSAE WTKQGTKHLK IPCKGRDAVP
DNESVNTFVY EVMMYLERQK HTKAPKYILV HCTHGHNRTG FMIIHYLMRT RISCVAEAIR
IFAQRRPPGI YKRDYIEALY SFYHEVPENI IVTCPSTPEW KRPSDLDLNG EAKLDDDDDN
GDVSPVHNEV EEKVITNDDV LGDAVPFDQQ EALRIVCYRL LELPSARGHA QFPGSHPVSL
NSDNLQLLRQ RYYYATWKAD GTRYMMLIMR DGCFLIDRNF CFRRVQMRFP HRNLNEGPHD
MTLIDGEMII DTVPDSGLKR RYLAYDLMAL DSVSKTKLPF SERWRLIEDE IIRPRYNERK
LFESGTKGNP MYKYDMELFS ARRKDFWLLH TAKRVLKEFI PSLCHDADGL IFQGWDDPYV
TRTHEGLLKW KYPEMNSVDF LFEVGNDNRQ LVFLYERGKK KLMDGSRMIF PNNEDPSSIS
GRIIECSWNK ERQCWFCMRV RFDKSTPNDI NTYRKVMRSI TDNITEDKLL KEIDEIISLP
MYADRKKADE RMAQHRRRGQ MPPQ
//