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Database: UniProt
Entry: F2DPF4_HORVV
LinkDB: F2DPF4_HORVV
Original site: F2DPF4_HORVV 
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
//
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