ID A0A0B2UEX0_9MICR Unreviewed; 279 AA.
AC A0A0B2UEX0;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=mRNA cap guanine-N7 methyltransferase {ECO:0000256|ARBA:ARBA00021751};
DE EC=2.1.1.56 {ECO:0000256|ARBA:ARBA00011926};
DE AltName: Full=mRNA (guanine-N(7))-methyltransferase {ECO:0000256|ARBA:ARBA00032772};
DE AltName: Full=mRNA cap methyltransferase {ECO:0000256|ARBA:ARBA00033387};
GN ORFNames=M896_050320 {ECO:0000313|EMBL:KHN69626.1};
OS Ordospora colligata OC4.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Ordosporidae;
OC Ordospora.
OX NCBI_TaxID=1354746 {ECO:0000313|EMBL:KHN69626.1, ECO:0000313|Proteomes:UP000031056};
RN [1] {ECO:0000313|EMBL:KHN69626.1, ECO:0000313|Proteomes:UP000031056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OC4 {ECO:0000313|EMBL:KHN69626.1,
RC ECO:0000313|Proteomes:UP000031056};
RA Pombert J.-F., Haag K.L., Beidas S., Ebert D., Keeling P.J.;
RT "The Ordospora colligata genome; evolution of extreme reduction in
RT microsporidia and host-to-parasite horizontal gene transfer.";
RL MBio 0:0-0(2014).
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:KHN69626.1}.
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DR EMBL; JOKQ01000005; KHN69626.1; -; Genomic_DNA.
DR RefSeq; XP_014563668.1; XM_014708182.1.
DR AlphaFoldDB; A0A0B2UEX0; -.
DR STRING; 1354746.A0A0B2UEX0; -.
DR GeneID; 26261685; -.
DR VEuPathDB; MicrosporidiaDB:M896_050320; -.
DR HOGENOM; CLU_020346_1_2_1; -.
DR InParanoid; A0A0B2UEX0; -.
DR OrthoDB; 167537at2759; -.
DR Proteomes; UP000031056; 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; IPR016899; mRNA_G-N7_MeTrfase_euk.
DR InterPro; IPR039753; RG7MT1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12189:SF2; MRNA CAP GUANINE-N7 METHYLTRANSFERASE; 1.
DR PANTHER; PTHR12189; MRNA GUANINE-7- METHYLTRANSFERASE; 1.
DR Pfam; PF03291; mRNA_G-N7_MeTrfase; 1.
DR PIRSF; PIRSF028762; ABD1; 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 mRNA capping {ECO:0000256|ARBA:ARBA00023042, ECO:0000256|PIRSR:PIRSR028762-
KW 2};
KW mRNA processing {ECO:0000256|ARBA:ARBA00023042,
KW ECO:0000256|PIRSR:PIRSR028762-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000031056};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..279
FT /note="MRNA cap 0 methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51562"
FT BINDING 35..36
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT BINDING 39
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT BINDING 57
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT BINDING 107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT BINDING 125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT SITE 60
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 66
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 91
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 129
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 210
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 269
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
SQ SEQUENCE 279 AA; 32045 MW; 747B8F4D792B88BF CRC64;
MDEHKIEIKE HYNSIKDKGL GGRSQSKAIN IRNTNNFIKA CLIRMYVKRG DSVLDLGCGK
GGDLLKYEKA GIGVYHGIDI ADVSINDAKL RFDSRKKSFK ASFSVSDVYG QHMDLGMQFD
LVSSQFSFHY AFSDSLLLDV ALQNVERHLK PGGFFIATVP SKDVILQRHQ QGRLHNEFYK
IELDTDIKMS LETAKEYRFT LIDSVNNCIE YFVDFDRMVE GFQKLKIDLI SRKGFIDFYE
AECDKNLELL KRMNLCKLKS DEAEVVGIYE VIVFRKQMA
//
