ID A0A200R595_9MAGN Unreviewed; 373 AA.
AC A0A200R595;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=mRNA (guanine-N(7))-methyltransferase {ECO:0000256|ARBA:ARBA00011926};
DE EC=2.1.1.56 {ECO:0000256|ARBA:ARBA00011926};
GN ORFNames=BVC80_1835g277 {ECO:0000313|EMBL:OVA17881.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA17881.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA17881.1, ECO:0000313|Proteomes:UP000195402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BLH2017 {ECO:0000313|Proteomes:UP000195402};
RC TISSUE=Root {ECO:0000313|EMBL:OVA17881.1};
RX PubMed=28552780; DOI=.1016/j.molp.2017.05.007;
RA Liu X., Liu Y., Huang P., Ma Y., Qing Z., Tang Q., Cao H., Cheng P.,
RA Zheng Y., Yuan Z., Zhou Y., Liu J., Tang Z., Zhuo Y., Zhang Y., Yu L.,
RA Huang J., Yang P., Peng Q., Zhang J., Jiang W., Zhang Z., Lin K., Ro D.K.,
RA Chen X., Xiong X., Shang Y., Huang S., Zeng J.;
RT "The Genome of Medicinal Plant Macleaya cordata Provides New Insights into
RT Benzylisoquinoline Alkaloids Metabolism.";
RL Mol. Plant 10:975-989(2017).
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;
CC Evidence={ECO:0000256|ARBA:ARBA00024288};
CC -!- SIMILARITY: In the N-terminal section; belongs to the dsDNA virus mRNA
CC guanylyltransferase family. {ECO:0000256|ARBA:ARBA00008556}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OVA17881.1}.
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DR EMBL; MVGT01000437; OVA17881.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200R595; -.
DR STRING; 56857.A0A200R595; -.
DR InParanoid; A0A200R595; -.
DR OrthoDB; 167537at2759; -.
DR Proteomes; UP000195402; Unassembled WGS sequence.
DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
DR InterPro; IPR039753; RG7MT1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12189:SF3; MRNA (GUANINE-N(7))-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR12189; MRNA GUANINE-7- METHYLTRANSFERASE; 1.
DR Pfam; PF03291; mRNA_G-N7_MeTrfase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51562; RNA_CAP0_MT; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:OVA17881.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000195402};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OVA17881.1}.
FT DOMAIN 1..291
FT /note="MRNA cap 0 methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51562"
SQ SEQUENCE 373 AA; 41878 MW; 741E1485948A992C CRC64;
MSSRAESTHF RLYEFVKTAL IKIFVSPYAT VCDLYCGAGV DTDKWDDSQI GHYIGIDAST
SGISEAQDIW ESQKKGCPAD FCNVDPCVEN LESYLQDKGI PADIVCCLQH LQLCFETEER
ARSLLRNVSS LLRPGGYFFG ITPDSSTIWA KYQKNVEASH NKVGGMKPNV VPNCIRSESY
MITFEVEEEK FPLFGKKYQL KFANDAGSEI HCLVHFPSFI RLAREVGLEY VEIQNLTEFY
DDNRAQFAGM FHNAGPNFVD ARGRLLPRSF DILGLYTTFI FQKPDPDIVP PITTPIMHEA
SHVPEEREWQ GSSWRHQTSV VVVVDEEKNG HTEPSSIAIN GKIAEQEKGI LGPGPADLRF
SEAFAPDYTR HAG
//
