ID D8RTN6_SELML Unreviewed; 560 AA.
AC D8RTN6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=mRNA guanylyltransferase {ECO:0000256|ARBA:ARBA00012475};
DE EC=2.7.7.50 {ECO:0000256|ARBA:ARBA00012475};
DE Flags: Fragment;
GN ORFNames=SELMODRAFT_100916 {ECO:0000313|EMBL:EFJ24711.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ24711.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
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};
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DR EMBL; GL377589; EFJ24711.1; -; Genomic_DNA.
DR RefSeq; XP_002974489.1; XM_002974443.1.
DR AlphaFoldDB; D8RTN6; -.
DR STRING; 88036.D8RTN6; -.
DR EnsemblPlants; EFJ24711; EFJ24711; SELMODRAFT_100916.
DR GeneID; 9636414; -.
DR Gramene; EFJ24711; EFJ24711; SELMODRAFT_100916.
DR KEGG; smo:SELMODRAFT_100916; -.
DR eggNOG; KOG2386; Eukaryota.
DR HOGENOM; CLU_021710_3_1_1; -.
DR InParanoid; D8RTN6; -.
DR OMA; LGPPDRW; -.
DR OrthoDB; 49440at2759; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 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|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR036958-3};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 91..158
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 183..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..201
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 113
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-1"
FT ACT_SITE 273
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-2"
FT BINDING 278
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT BINDING 293
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT BINDING 322..324
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT BINDING 439..441
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT BINDING 508..513
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFJ24711.1"
SQ SEQUENCE 560 AA; 64873 MW; 613AB4945783D6F6 CRC64;
GWIDCPPFGE PVLRFVPSKV FLGEAYNAAI EPGKRYSWKR ILRQHKDVGL IIDLTNTTRY
YSANEVTRAG LSHFKIPCKG RNEVPDAEAV NTFVYETHRY LQRSKTSRVL VHCTHGFNRT
GYMIVNYLVR YCGLPVTQAL AKFAAARPPG IYKKSYIRKL YALYHDPTPF AAPAVPDWKR
LDLNGTVDDD DGDDEEDDPT LDRQENAAPM TNDDVLGDAI SSEEQIELQR LCLSLLDLAS
QSRNLSFPGS HPVSLDRSKL QLLKQHYYFA TWKADGTRYM MLILSYGCYL IDRKFEFRRI
QMRFPHPRKD SPLPVHHMTL LDGEMVIDKH PETGKLERRY LIYDMMVVNA ESLVKKPFSQ
RFHGIESDVI RPRHNDAGSS GYLYKDEEFR VRRKNFWPLS STKLLFQKLI PGLSHRSDGL
IFQGFEMPYV CRTSDSLLKW KFPSLNSVDF YLQRSGDTFT LSLLEKGNHQ VLPGASVSFD
DSVDPSTLEN KVIECSWNNE RQSWEFMRLR PDKPLANAFN TYRKVFNSIK DNITQEELVE
EIDRTVKLPM YKEKDKQFLK
//
