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Database: UniProt
Entry: A0A1I8HK30_9PLAT
LinkDB: A0A1I8HK30_9PLAT
Original site: A0A1I8HK30_9PLAT 
ID   A0A1I8HK30_9PLAT        Unreviewed;       342 AA.
AC   A0A1I8HK30;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=mRNA cap guanine-N7 methyltransferase {ECO:0000256|PIRNR:PIRNR028762};
DE            EC=2.1.1.56 {ECO:0000256|PIRNR:PIRNR028762};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0006626-snap-gene-0.5-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-uti_cns_0006626-snap-gene-0.5-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR028762}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. mRNA cap 0 methyltransferase family.
CC       {ECO:0000256|PIRNR:PIRNR028762}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the dsDNA virus mRNA
CC       guanylyltransferase family. {ECO:0000256|ARBA:ARBA00008556}.
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DR   AlphaFoldDB; A0A1I8HK30; -.
DR   WBParaSite; maker-uti_cns_0006626-snap-gene-0.5-mRNA-1; maker-uti_cns_0006626-snap-gene-0.5-mRNA-1; maker-uti_cns_0006626-snap-gene-0.5.
DR   Proteomes; UP000095280; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   ECO:0000256|PIRNR:PIRNR028762};
KW   mRNA capping {ECO:0000256|PIRNR:PIRNR028762, ECO:0000256|PIRSR:PIRSR028762-
KW   2}; mRNA processing {ECO:0000256|PIRNR:PIRNR028762};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR028762};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRNR:PIRNR028762};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRNR:PIRNR028762};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR028762}.
FT   DOMAIN          1..342
FT                   /note="MRNA cap 0 methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51562"
FT   BINDING         32..33
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT   BINDING         36
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT   BINDING         62
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT   BINDING         84
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT   BINDING         121
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT   BINDING         133
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT   BINDING         138
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT   SITE            65
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT   SITE            71
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT   SITE            96
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT   SITE            137
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT   SITE            226
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT   SITE            333
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
SQ   SEQUENCE   342 AA;  38920 MW;  BA667C2C078FA983 CRC64;
     AGQEVAQHYN RVLQSSIASR AESRAFYLRN FNNWVKSVLI GSHLRIIERQ FINSDIRVLD
     LCSGKGGDLL KWRKGGVAKI VFVDIADVSV EQCRRRYGEM AEQHQRDGRG RLPRAEFHVA
     DATLYGCGIC SCQFSLHYCF QSYQAARQFV RNACESLLPG GYFIGTLPDA NEIVRRLRRK
     PGSEAAFGNG VYNVTFSSSA VKTQQVPLFG CKYHFSLEKQ VQDCPEYLVY FPVLEQLCSE
     YGLRCTLRQN FAKFYRDHVT QPEWRSLLGV MQSLEPYPNA DGVELKSQVE GDYRAAQAYL
     NGDGRCDTEE DERDRNGPVG TLSMEEWEAA TLYMVFAFQR AE
//
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