MCES_MACFA
ID MCES_MACFA Reviewed; 476 AA.
AC Q4R7K1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=QtsA-15044;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-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 -!- ACTIVITY REGULATION: Methyltransferase activity is activated by RAMAC.
CC {ECO:0000250|UniProtKB:O43148}.
CC -!- SUBUNIT: Interacts with importin alpha, leading to stimulate both RNA-
CC binding and methyltransferase activity. Interaction with importin alpha
CC and beta is required for its nuclear localization, importin beta
CC dissociating in response to RanGTP, allowing RNMT-importin alpha to
CC bind RNA substrates. Interacts with elongating form of polymerase II
CC and RNGTT. Interacts with RAMAC, this interaction significantly
CC enhances RNA-binding and cap methyltransferase activity.
CC {ECO:0000250|UniProtKB:O43148}.
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; AB168817; BAE00921.1; -; mRNA.
DR RefSeq; NP_001270332.1; NM_001283403.1.
DR RefSeq; XP_005587335.1; XM_005587278.2.
DR RefSeq; XP_015295261.1; XM_015439775.1.
DR AlphaFoldDB; Q4R7K1; -.
DR SMR; Q4R7K1; -.
DR STRING; 9541.XP_005587334.1; -.
DR Ensembl; ENSMFAT00000004697; ENSMFAP00000030491; ENSMFAG00000042388.
DR GeneID; 101865006; -.
DR KEGG; mcf:101865006; -.
DR CTD; 8731; -.
DR VEuPathDB; HostDB:ENSMFAG00000042388; -.
DR eggNOG; KOG1975; Eukaryota.
DR GeneTree; ENSGT00390000002368; -.
DR OMA; WDATSIY; -.
DR Proteomes; UP000233100; Chromosome 18.
DR Bgee; ENSMFAG00000042388; Expressed in cerebellum and 13 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; Phosphoprotein;
KW Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..476
FT /note="mRNA cap guanine-N7 methyltransferase"
FT /id="PRO_0000248322"
FT DOMAIN 128..476
FT /note="mRNA cap 0 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT REGION 1..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 126..128
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 17..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176..177
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 180
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 205
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 227
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 261
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT BINDING 284
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT BINDING 289
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT SITE 208
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 239
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 288
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 370
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 467
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0L8"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0L8"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2U7"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2U7"
SQ SEQUENCE 476 AA; 54797 MW; D22D4B4CE5A3A1E0 CRC64;
MANSTKAEEY EKMSVEQAKA SVNSEAESSF SINENTTASG TGLSGKTSVC RQVDTARKRK
EFEDDLVKES SSCGEGTPSK KRKLDPEIVP EEKDCGDDEG NSKKRKRETE DVPKDEYSTG
DGTQNKRKIA LEDVPEKQKN LEEGHSSAVA AHYNELQEVG LEKRSQSRIF YLRNFNNWMK
SVLIGEFLEK VRQKKKRDIT VLDLGCGKGG DLLKWKKGRI NKLVCTDIAD VSIKQCQQRY
EDMKNRRDSE YIFSAEFITA DCSKELLIEK FRDPQMCFDI CSCQFVCHYS FESYEQADMM
LRNACERLSP GGYFIGTTPN SFELIRRLEA SETESFGNEI YTVKFQKKGD YPLFGCKYDF
NLEGVVDVPE FLVYFPLLNE MAKKYNMKLV YKKTFLEFYE EKIKNNENKM LLKRMQALEP
YPANESSKLV SERVDDYEHA AKYMKNSQVK LPLGTLSKSE WEATSIYLVF AFEKQQ
