MCES_ENCCU
ID MCES_ENCCU Reviewed; 283 AA.
AC Q8SR66;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=mRNA cap guanine-N7 methyltransferase;
DE EC=2.1.1.56 {ECO:0000250|UniProtKB:O43148};
DE AltName: Full=mRNA (guanine-N(7))-methyltransferase;
DE AltName: Full=mRNA cap methyltransferase;
GN Name=ABD1; OrderedLocusNames=ECU10_0380;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GB-M1;
RX PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT "Identification of transcriptional signals in Encephalitozoon cuniculi
RT widespread among Microsporidia phylum: support for accurate structural
RT genome annotation.";
RL BMC Genomics 10:607-607(2009).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEXES WITH SUBSTRATES, AND
RP MUTAGENESIS OF ARG-32; ASN-35; ASN-36; LYS-39; LYS-60; ASP-63; LYS-66;
RP ASP-79; ILE-80; ARG-91; 107-ASP-SER-108; TYR-109; PHE-126; LEU-201 AND
RP TYR-269.
RX PubMed=14731396; DOI=10.1016/s1097-2765(03)00522-7;
RA Fabrega C., Hausmann S., Shen V., Shuman S., Lima C.D.;
RT "Structure and mechanism of mRNA cap (guanine-N7) methyltransferase.";
RL Mol. Cell 13:77-89(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP LYS-39; ASP-55; ASP-63 AND ASP-79.
RX PubMed=15760890; DOI=10.1074/jbc.m501073200;
RA Hausmann S., Zheng S., Fabrega C., Schneller S.W., Lima C.D., Shuman S.;
RT "Encephalitozoon cuniculi mRNA cap (guanine N-7) methyltransferase: methyl
RT acceptor specificity, inhibition by S-adenosylmethionine analogs, and
RT structure-guided mutational analysis.";
RL J. Biol. Chem. 280:20404-20412(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, AND
RP MUTAGENESIS OF ASN-36; LYS-39; ASP-55; LYS-60; ASP-63; LYS-66; ASP-79;
RP ARG-91; TYR-109; PHE-126; HIS-129; TYR-130 AND GLU-210.
RX PubMed=16971388; DOI=10.1074/jbc.m607292200;
RA Zheng S., Hausmann S., Liu Q., Ghosh A., Schwer B., Lima C.D., Shuman S.;
RT "Mutational analysis of Encephalitozoon cuniculi mRNA cap (guanine-N7)
RT methyltransferase, structure of the enzyme bound to sinefungin, and
RT evidence that cap methyltransferase is the target of sinefungin's
RT antifungal activity.";
RL J. Biol. Chem. 281:35904-35913(2006).
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. {ECO:0000269|PubMed:15760890}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 mM for GTP {ECO:0000269|PubMed:15760890};
CC KM=25 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:15760890};
CC KM=0.1 mM for cap dinucleotide GpppA {ECO:0000269|PubMed:15760890};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15760890,
CC ECO:0000269|PubMed:16971388}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. mRNA cap 0 methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00895}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL590449; CAD25757.2; -; Genomic_DNA.
DR RefSeq; NP_586153.1; NM_001041986.1.
DR PDB; 1RI1; X-ray; 2.50 A; A=1-283.
DR PDB; 1RI2; X-ray; 2.70 A; A=1-283.
DR PDB; 1RI3; X-ray; 2.50 A; A=1-283.
DR PDB; 1RI4; X-ray; 2.40 A; A=1-283.
DR PDB; 1RI5; X-ray; 2.10 A; A=1-283.
DR PDB; 1Z3C; X-ray; 2.20 A; A=1-283.
DR PDB; 2HV9; X-ray; 2.60 A; A=1-283.
DR PDBsum; 1RI1; -.
DR PDBsum; 1RI2; -.
DR PDBsum; 1RI3; -.
DR PDBsum; 1RI4; -.
DR PDBsum; 1RI5; -.
DR PDBsum; 1Z3C; -.
DR PDBsum; 2HV9; -.
DR AlphaFoldDB; Q8SR66; -.
DR SMR; Q8SR66; -.
DR STRING; 284813.Q8SR66; -.
DR GeneID; 859802; -.
DR KEGG; ecu:ECU10_0380; -.
DR VEuPathDB; MicrosporidiaDB:ECU10_0380; -.
DR HOGENOM; CLU_020346_1_2_1; -.
DR InParanoid; Q8SR66; -.
DR OrthoDB; 1390749at2759; -.
DR BRENDA; 2.1.1.56; 7412.
DR SABIO-RK; Q8SR66; -.
DR EvolutionaryTrace; Q8SR66; -.
DR Proteomes; UP000000819; Chromosome X.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; mRNA capping; mRNA processing; Nucleus;
KW Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..283
FT /note="mRNA cap guanine-N7 methyltransferase"
FT /id="PRO_0000210142"
FT DOMAIN 1..283
FT /note="mRNA cap 0 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 35..36
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT BINDING 39
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 57
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
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:0000250|UniProtKB:O43148"
FT BINDING 125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT SITE 60
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 66
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 91
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 129
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 210
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 269
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT MUTAGEN 32
FT /note="R->A: No effect. Loss of activity; when associated
FT with A-60."
FT /evidence="ECO:0000269|PubMed:14731396"
FT MUTAGEN 35
FT /note="N->A: No effect. Loss of activity; when associated
FT with A-269."
FT /evidence="ECO:0000269|PubMed:14731396"
FT MUTAGEN 36
FT /note="N->A: Reduces activity by 85%."
FT /evidence="ECO:0000269|PubMed:14731396,
FT ECO:0000269|PubMed:16971388"
FT MUTAGEN 36
FT /note="N->D: Reduces activity by 96%."
FT /evidence="ECO:0000269|PubMed:14731396,
FT ECO:0000269|PubMed:16971388"
FT MUTAGEN 39
FT /note="K->A,Q,R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:14731396,
FT ECO:0000269|PubMed:15760890, ECO:0000269|PubMed:16971388"
FT MUTAGEN 55
FT /note="D->A,N: Reduces activity by 95%."
FT /evidence="ECO:0000269|PubMed:15760890,
FT ECO:0000269|PubMed:16971388"
FT MUTAGEN 55
FT /note="D->E: Reduces activity by 60%."
FT /evidence="ECO:0000269|PubMed:15760890,
FT ECO:0000269|PubMed:16971388"
FT MUTAGEN 60
FT /note="K->A: Reduces activity by 92%. Loss of activity;
FT when associated with A-32."
FT /evidence="ECO:0000269|PubMed:14731396,
FT ECO:0000269|PubMed:16971388"
FT MUTAGEN 63
FT /note="D->A,N: Reduces activity by 99%."
FT /evidence="ECO:0000269|PubMed:14731396,
FT ECO:0000269|PubMed:15760890, ECO:0000269|PubMed:16971388"
FT MUTAGEN 63
FT /note="D->E: Reduces activity by 75%."
FT /evidence="ECO:0000269|PubMed:14731396,
FT ECO:0000269|PubMed:15760890, ECO:0000269|PubMed:16971388"
FT MUTAGEN 66
FT /note="K->A: Reduces activity by 80%."
FT /evidence="ECO:0000269|PubMed:14731396,
FT ECO:0000269|PubMed:16971388"
FT MUTAGEN 66
FT /note="K->Q,R: Reduces activity by 90%."
FT /evidence="ECO:0000269|PubMed:14731396,
FT ECO:0000269|PubMed:16971388"
FT MUTAGEN 79
FT /note="D->A,N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:14731396,
FT ECO:0000269|PubMed:15760890, ECO:0000269|PubMed:16971388"
FT MUTAGEN 79
FT /note="D->E: Reduces activity by 77%."
FT /evidence="ECO:0000269|PubMed:14731396,
FT ECO:0000269|PubMed:15760890, ECO:0000269|PubMed:16971388"
FT MUTAGEN 80
FT /note="I->A: No effect. Strongly reduced activity; when
FT associated with A-109."
FT /evidence="ECO:0000269|PubMed:14731396"
FT MUTAGEN 91
FT /note="R->A,Q: Reduces activity by over 98%."
FT /evidence="ECO:0000269|PubMed:14731396,
FT ECO:0000269|PubMed:16971388"
FT MUTAGEN 91
FT /note="R->K: Reduces activity by 96%."
FT /evidence="ECO:0000269|PubMed:14731396,
FT ECO:0000269|PubMed:16971388"
FT MUTAGEN 107..108
FT /note="DS->AA: Slightly reduced activity."
FT /evidence="ECO:0000269|PubMed:14731396"
FT MUTAGEN 109
FT /note="Y->A: Reduces activity by 83%. Strongly reduced
FT activity; when associated with A-80."
FT /evidence="ECO:0000269|PubMed:14731396,
FT ECO:0000269|PubMed:16971388"
FT MUTAGEN 126
FT /note="F->A,N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:14731396,
FT ECO:0000269|PubMed:16971388"
FT MUTAGEN 126
FT /note="F->H: Reduces activity by 92%."
FT /evidence="ECO:0000269|PubMed:14731396,
FT ECO:0000269|PubMed:16971388"
FT MUTAGEN 126
FT /note="F->I: Reduces activity by 75%."
FT /evidence="ECO:0000269|PubMed:14731396,
FT ECO:0000269|PubMed:16971388"
FT MUTAGEN 126
FT /note="F->L: Reduces activity by 55%."
FT /evidence="ECO:0000269|PubMed:14731396,
FT ECO:0000269|PubMed:16971388"
FT MUTAGEN 126
FT /note="F->V: Reduces activity by 84%."
FT /evidence="ECO:0000269|PubMed:14731396,
FT ECO:0000269|PubMed:16971388"
FT MUTAGEN 129
FT /note="H->A: Reduces activity by 53%. Reduces activity by
FT 99%; when associated with L-130."
FT /evidence="ECO:0000269|PubMed:16971388"
FT MUTAGEN 130
FT /note="Y->A,S,V: Reduces activity by 98%."
FT /evidence="ECO:0000269|PubMed:16971388"
FT MUTAGEN 130
FT /note="Y->F: Reduces activity by 66%."
FT /evidence="ECO:0000269|PubMed:16971388"
FT MUTAGEN 130
FT /note="Y->L: Reduces activity by 99%; when associated with
FT A-129."
FT /evidence="ECO:0000269|PubMed:16971388"
FT MUTAGEN 201
FT /note="L->A: No effect."
FT /evidence="ECO:0000269|PubMed:14731396"
FT MUTAGEN 210
FT /note="E->A: Reduces activity by 87%."
FT /evidence="ECO:0000269|PubMed:16971388"
FT MUTAGEN 269
FT /note="Y->A: Reduced activity. Loss of activity; when
FT associated with A-35."
FT /evidence="ECO:0000269|PubMed:14731396"
FT HELIX 29..46
FT /evidence="ECO:0007829|PDB:1RI5"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:1RI5"
FT TURN 59..63
FT /evidence="ECO:0007829|PDB:1RI5"
FT HELIX 64..70
FT /evidence="ECO:0007829|PDB:1RI5"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:1RI5"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:1RI5"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:1RI5"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:1RI5"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:1RI5"
FT HELIX 128..132
FT /evidence="ECO:0007829|PDB:1RI5"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:1RI5"
FT STRAND 149..160
FT /evidence="ECO:0007829|PDB:1RI5"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:1RI5"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:1RI5"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:1RI5"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:1RI5"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:1RI5"
FT HELIX 215..223
FT /evidence="ECO:0007829|PDB:1RI5"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1RI5"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:1RI5"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:1RI5"
FT HELIX 247..251
FT /evidence="ECO:0007829|PDB:1RI5"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:1RI5"
FT HELIX 260..266
FT /evidence="ECO:0007829|PDB:1RI5"
FT STRAND 269..276
FT /evidence="ECO:0007829|PDB:1RI5"
SQ SEQUENCE 283 AA; 33074 MW; 40ABA7B1522C7001 CRC64;
MEGKKEEIRE HYNSIRERGR ESRQRSKTIN IRNANNFIKA CLIRLYTKRG DSVLDLGCGK
GGDLLKYERA GIGEYYGVDI AEVSINDARV RARNMKRRFK VFFRAQDSYG RHMDLGKEFD
VISSQFSFHY AFSTSESLDI AQRNIARHLR PGGYFIMTVP SRDVILERYK QGRMSNDFYK
IELEKMEDVP MESVREYRFT LLDSVNNCIE YFVDFTRMVD GFKRLGLSLV ERKGFIDFYE
DEGRRNPELS KKMGLGCLTR EESEVVGIYE VVVFRKLVPE SDA
