ID A0A151XK11_9HYME Unreviewed; 473 AA.
AC A0A151XK11;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, 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};
GN ORFNames=ALC60_00191 {ECO:0000313|EMBL:KYQ60744.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ60744.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ60744.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ60744.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ60744.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KQ982045; KYQ60744.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151XK11; -.
DR STRING; 64791.A0A151XK11; -.
DR Proteomes; UP000075809; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000075809};
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 83..467
FT /note="MRNA cap 0 methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51562"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 131..132
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT BINDING 162
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT BINDING 184
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT BINDING 223
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT BINDING 246
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT BINDING 251
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT SITE 165
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 171
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 196
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 250
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 354
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 450
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
SQ SEQUENCE 473 AA; 54057 MW; C0E470AAF54BC36B CRC64;
MSALAAENKT EYEEKEQHKS ETETSSGTSA KSETSKDTNV ESPQSRKHKR SPDRERPSKV
AKHDAEEDAS SASTNVPSDL TTGSNEKNKD ATDANRSLDN TVLVADHYNA LEEKGLSQRN
QSRIVYMRNF NNWIKSMLIN EYVVKVRQGK SFGASLKVLD MCCGKGGDLL KWKKANISHL
ICADIAQVSL EQCQQRYNDM VNKKGSKDRG FAPIFSAEFI TADCTKVRLR EKFTDPSMQL
DFVSCQFAFH YSFESLSQAE CMIRNASESL KPGGYFIGTI PDAYDLVLYF SLIDNTHTRL
SSFWQRSSRW QNCDGHKFGN DVYNVEFLSE DKTKPPFFGA KYNFHLDGVV DCPEFLVHLP
TLCKLALKYG LELISFERFE DFYERFKNEG RSLLGNMQAL ETYPPYHEAP LLGDPERDYH
HAVEYMQNLP ANHRKIGTLS QSEWEVTSLY AVFSFRKMKT IWNSEGKPEY IKL
//
