MCES_XENLA
ID MCES_XENLA Reviewed; 402 AA.
AC Q9I8S2; Q52KX9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=mRNA cap guanine-N7 methyltransferase;
DE EC=2.1.1.56 {ECO:0000250|UniProtKB:O43148};
DE AltName: Full=RG7MT1;
DE AltName: Full=mRNA (guanine-N(7))-methyltransferase;
DE AltName: Full=mRNA cap methyltransferase;
DE Short=xCMT1;
GN Name=rnmt;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=10679253; DOI=10.1006/bbrc.2000.2188;
RA Yokoska J., Tsukamoto T., Miura K., Shiokawa K., Mizumoto K.;
RT "Cloning and characterization of mRNA capping enzyme and mRNA (guanine-7-)-
RT methyltransferase cDNAs from Xenopus laevis.";
RL Biochem. Biophys. Res. Commun. 268:617-624(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of the mRNA-capping methyltransferase
CC RNMT:RAMAC complex that methylates the N7 position of the added
CC guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-
CC terminal GpppC. {ECO:0000250|UniProtKB:O43148}.
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:0000250|UniProtKB:O43148, ECO:0000255|PROSITE-
CC ProRule:PRU00895};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43148}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expression decreases after gastrulation. {ECO:0000269|PubMed:10679253}.
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; AF218795; AAF43145.1; -; mRNA.
DR EMBL; BC094147; AAH94147.1; -; mRNA.
DR PIR; JC7199; JC7199.
DR RefSeq; NP_001082004.1; NM_001088535.1.
DR RefSeq; XP_018121821.1; XM_018266332.1.
DR RefSeq; XP_018121822.1; XM_018266333.1.
DR RefSeq; XP_018121823.1; XM_018266334.1.
DR AlphaFoldDB; Q9I8S2; -.
DR SMR; Q9I8S2; -.
DR IntAct; Q9I8S2; 2.
DR MaxQB; Q9I8S2; -.
DR PRIDE; Q9I8S2; -.
DR DNASU; 398173; -.
DR GeneID; 398173; -.
DR KEGG; xla:398173; -.
DR CTD; 398173; -.
DR Xenbase; XB-GENE-944374; rnmt.L.
DR OMA; WDATSIY; -.
DR OrthoDB; 1390749at2759; -.
DR BRENDA; 2.1.1.56; 6725.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 398173; Expressed in gastrula and 19 other tissues.
DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; ISS:UniProtKB.
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 Methyltransferase; mRNA capping; mRNA processing; Nucleus;
KW Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..402
FT /note="mRNA cap guanine-N7 methyltransferase"
FT /id="PRO_0000248326"
FT DOMAIN 55..402
FT /note="mRNA cap 0 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103..104
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 153
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 187
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT BINDING 210
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT BINDING 215
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT SITE 134
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 140
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 165
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 214
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 296
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 393
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT CONFLICT 106
FT /note="M -> I (in Ref. 2; AAH94147)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 46003 MW; 5370C6C956FD0E07 CRC64;
MDHVLNPEEK VSQTNSESGG ADGAFQHVKG EHSSPKLSAS EKSLPGNTKS PLKRKAAEPD
SPPKRPRLEE GHGSLVVTHY NELPETGLEI RSQSRIFHLR NFNNWMKSAL IGEFVEKVQQ
RTRNITVLDL GCGKGGDLLK WRKGGISKLV CTDIADVSVK QCEQRYKDMK RKSRNERIFE
AEFLTSDSTK ELLSEKYIDP EIKFDICSCQ FVYHYSFETY EQADTMLRNA CERLCPGGFF
IGTTPDGFEL VKRLEASDTN SFGNDVYTVT FEKKGKYPLF GCKYDFSLEE VVNVPEFLVY
FPVLVEMAKK YQMKLIYKKT FREFFEEKVK NDEQKMLLKR MKALESYPAA PNTKLVSGRT
EDYEHAQKMV ENGQIKLPLG TLSKSEWDAT SIYLLFAFEK QA
