MCES_XENTR
ID MCES_XENTR Reviewed; 405 AA.
AC Q28FT4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
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;
GN Name=rnmt; ORFNames=TGas135f12.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (JUN-2006) 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 -!- 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; CR761774; CAJ83499.1; -; mRNA.
DR RefSeq; NP_001017053.1; NM_001017053.2.
DR RefSeq; XP_012820220.1; XM_012964766.1.
DR AlphaFoldDB; Q28FT4; -.
DR SMR; Q28FT4; -.
DR STRING; 8364.ENSXETP00000059893; -.
DR PaxDb; Q28FT4; -.
DR Ensembl; ENSXETT00000096010; ENSXETP00000085183; ENSXETG00000014707.
DR GeneID; 549807; -.
DR KEGG; xtr:549807; -.
DR CTD; 8731; -.
DR Xenbase; XB-GENE-944369; rnmt.
DR eggNOG; KOG1975; Eukaryota.
DR InParanoid; Q28FT4; -.
DR OrthoDB; 1390749at2759; -.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000014707; Expressed in ovary and 14 other tissues.
DR ExpressionAtlas; Q28FT4; differential.
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..405
FT /note="mRNA cap guanine-N7 methyltransferase"
FT /id="PRO_0000248327"
FT DOMAIN 58..405
FT /note="mRNA cap 0 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106..107
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 110
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 134
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 156
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 190
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT BINDING 213
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT BINDING 218
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT SITE 137
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 143
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 168
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 217
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 299
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 396
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
SQ SEQUENCE 405 AA; 46714 MW; 3D4DF47C7FFC369F CRC64;
MDNILNPEDN VSQTNTETDV TDGPFQYVKE EHSSHKFTAS GQNLDSPPKN KKSPLKRKAG
EPESPSKRPR LEEGHGSLVV THYNELPETG LETRSQSRIF HLRNFNNWMK SALIGEFVEK
VRQRTRNIAV LDLGCGKGGD LLKWRKGGIS KLVCTDIADV SVKQCEERYK DLKRKSRNER
VFEAEFLTAD STKELLSEKY NDPEIKFDIC SCQFVYHYSF ETYEQADMML RNACERLCPG
GFFIGTTPDG FELVKRLEAS DTNSFGNDVY TVKFEKKGKY PLFGCKYDFS LEEVVNVPEF
LVYFPVLVEM AKKYQMKLIY KKTFREFFEE KVKNDEQKML LKRMKALEPY PAAPNFKLVS
GRTEDYEHAQ KLVENGQVKL PLGTLSKSEW EATSIYLLFA FEKQA
