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Database: UniProt
Entry: K7L1P5_SOYBN
LinkDB: K7L1P5_SOYBN
Original site: K7L1P5_SOYBN 
ID   K7L1P5_SOYBN            Unreviewed;       656 AA.
AC   K7L1P5;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=mRNA guanylyltransferase {ECO:0000256|ARBA:ARBA00012475};
DE            EC=2.7.7.50 {ECO:0000256|ARBA:ARBA00012475};
GN   Name=100818110 {ECO:0000313|EnsemblPlants:KRH49271};
GN   ORFNames=GLYMA_07G144500 {ECO:0000313|EMBL:KRH49271.1};
OS   Glycine max (Soybean) (Glycine hispida).
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=3847 {ECO:0000313|EnsemblPlants:KRH49271};
RN   [1] {ECO:0000313|EMBL:KRH49271.1, ECO:0000313|EnsemblPlants:KRH49271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH49271};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH49271.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH49271}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH49271};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH49271.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH49271.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CM000840; KRH49271.1; -; Genomic_DNA.
DR   AlphaFoldDB; K7L1P5; -.
DR   EnsemblPlants; KRH49271; KRH49271; GLYMA_07G144500.
DR   Gramene; KRH49271; KRH49271; GLYMA_07G144500.
DR   Proteomes; UP000008827; Chromosome 7.
DR   ExpressionAtlas; K7L1P5; baseline and differential.
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   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; 2.
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; GTP--RNA 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; 2.
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.
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:UP000008827}.
FT   DOMAIN          164..232
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          415..555
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          46..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        187
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-1"
FT   ACT_SITE        355
FT                   /note="N6-GMP-lysine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-2"
FT   BINDING         360
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   BINDING         375
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   BINDING         406..408
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   BINDING         525..527
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   BINDING         593..598
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
SQ   SEQUENCE   656 AA;  77487 MW;  43F2A8E44CA2C2CB CRC64;
     MIVAVDLNAS PVPEDDEDDF GRQVEEYRTP EERVESAVDI AHQECEERKR KLKREHSDDK
     PVQVSQSPGH DQLFHTKILK SYDRSKLPPG WLDCPSFGQE IYCMIPSKVP LGESFNDDII
     PGKRYSFKQV IHQQRVLGRK LDLVIDLTNT SRYYSVADLK KEGIKYVKVM QFLLRQKHSR
     KHILVHCTHG HNRTGYMIIH YLMRSMSMSV TQAIKIFSDA RPPGIYKPEY IDALYAFYHE
     KKPEMIVCPP TPEWKRTPEL VDLNGEAMPD DDDDGVPGSP LHENHVTDTI MRNDDVLGDE
     IPNDQQDAFR QFCFRTLKLG VGARGHMQFP GSHPVSLNRE NLQLLRQRYY YATWKADGTR
     YMMLITMDGC YLIDRSFNFR RVQMRFPCRI TKDGMAEKTH HFTLLDGEMI IDTLPDSKKQ
     ERRYLIYDLM AINGVSVIER PFYERWKMLE KVIEPRNQER FQSRNPYYRY DMEPFRVRRK
     DFWLLSTVTK LLSEFIPKLS HDADGLIFQG WDDPYIPRTH EGLLKWKYAE LNSVDFLFEI
     DNDCQLLLLY ERGKRKLLEG YRVAFEGLDP LHYSGKIIEC SWDSDRQEWI FKRIRTDKST
     PNDFNTYRKV MRSIRDNITE DVLLNEINEI ICLPLYADRI RIDSKAHIHT NMARRR
//
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