MCES1_ARATH
ID MCES1_ARATH Reviewed; 370 AA.
AC Q9LHQ7; Q3EB33;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=mRNA cap guanine-N7 methyltransferase 1;
DE EC=2.1.1.56;
DE AltName: Full=mRNA (guanine-N(7))-methyltransferase 1;
DE AltName: Full=mRNA cap methyltransferase 1;
GN OrderedLocusNames=At3g20650; ORFNames=F3H11.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: mRNA-capping methyltransferase that methylates the N7
CC position of the added guanosine to the 5'-cap structure of mRNAs. Binds
CC RNA containing 5'-terminal GpppC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
CC S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00895};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LHQ7-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. mRNA cap 0 methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00895}.
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DR EMBL; AP002034; BAB02241.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76407.1; -; Genomic_DNA.
DR EMBL; BT005804; AAO64206.1; -; mRNA.
DR EMBL; BT006067; AAP04052.1; -; mRNA.
DR EMBL; AK228381; BAF00319.1; -; mRNA.
DR RefSeq; NP_188701.2; NM_112956.6. [Q9LHQ7-1]
DR AlphaFoldDB; Q9LHQ7; -.
DR SMR; Q9LHQ7; -.
DR BioGRID; 6944; 4.
DR STRING; 3702.AT3G20650.1; -.
DR PaxDb; Q9LHQ7; -.
DR PRIDE; Q9LHQ7; -.
DR ProteomicsDB; 238364; -. [Q9LHQ7-1]
DR EnsemblPlants; AT3G20650.1; AT3G20650.1; AT3G20650. [Q9LHQ7-1]
DR GeneID; 821612; -.
DR Gramene; AT3G20650.1; AT3G20650.1; AT3G20650. [Q9LHQ7-1]
DR KEGG; ath:AT3G20650; -.
DR Araport; AT3G20650; -.
DR TAIR; locus:2083420; AT3G20650.
DR eggNOG; KOG1975; Eukaryota.
DR HOGENOM; CLU_020346_1_0_1; -.
DR InParanoid; Q9LHQ7; -.
DR PhylomeDB; Q9LHQ7; -.
DR PRO; PR:Q9LHQ7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LHQ7; baseline and differential.
DR Genevisible; Q9LHQ7; AT.
DR GO; GO:0005845; C:mRNA cap binding complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
DR InterPro; IPR016899; mRNA_G-N7_MeTrfase_euk.
DR InterPro; IPR039753; RG7MT1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12189; PTHR12189; 1.
DR Pfam; PF03291; Pox_MCEL; 1.
DR PIRSF; PIRSF028762; ABD1; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51562; RNA_CAP0_MT; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Methyltransferase; mRNA capping; mRNA processing;
KW Nucleus; Reference proteome; RNA-binding; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..370
FT /note="mRNA cap guanine-N7 methyltransferase 1"
FT /id="PRO_0000248331"
FT DOMAIN 22..347
FT /note="mRNA cap 0 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 70..71
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 150..151
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 172..174
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 95
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 101
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 126
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 176
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 264
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 333
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
SQ SEQUENCE 370 AA; 42238 MW; 48D4DEA9DB81575D CRC64;
MKRGFSDSPS SSAPPPSSRF KSNPEGDSQF LEDETTKNFA RKVADHYSRR TNQTLEEREA
SPIIHLKKLN NWIKSVLIQL YARPDDAVLD LACGKGGDLI KWDKARIGYY VGIDIAEGSI
EDCRTRYNGD ADHHQRRKKF SFPSRLLCGD CFEVELDKIL EEDAPFDICS CQFAMHYSWT
TEARARRALA NVSALLRPGG VFIGTMPDAN VIIKKLREAE GLEIGNSVYW IRFGEEYSQK
KFKSSSPFGI EYVFHLEDAV DCPEWIVPFN VFKSLAEEYD LELVFVKNSH EFVHEYMKKP
EFVELMRRLG ALGDGSNDQS TLSADEWEAA YLYLSFVLRK RGESDGARRS GRRKNGKMNL
SKDDVLYIDS
