ID A0A093SI16_9PASS Unreviewed; 416 AA.
AC A0A093SI16;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=mRNA cap guanine-N7 methyltransferase {ECO:0000256|PIRNR:PIRNR028762};
DE EC=2.1.1.56 {ECO:0000256|PIRNR:PIRNR028762};
GN ORFNames=N305_03524 {ECO:0000313|EMBL:KFW82354.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW82354.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW82354.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW82354.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) 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; KL671404; KFW82354.1; -; Genomic_DNA.
DR RefSeq; XP_017937388.1; XM_018081899.1.
DR RefSeq; XP_017937397.1; XM_018081908.1.
DR AlphaFoldDB; A0A093SI16; -.
DR SMR; A0A093SI16; -.
DR STRING; 328815.ENSMVIP00005011780; -.
DR GeneID; 103759205; -.
DR CTD; 8731; -.
DR OrthoDB; 167537at2759; -.
DR Proteomes; UP000053258; 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:UP000053258};
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 68..416
FT /note="MRNA cap 0 methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51562"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 116..117
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT BINDING 120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT BINDING 144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT BINDING 166
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT BINDING 201
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT BINDING 224
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT BINDING 229
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-1"
FT SITE 147
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 153
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 178
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 228
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 310
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT SITE 407
FT /note="mRNA cap binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
SQ SEQUENCE 416 AA; 47495 MW; 86468699CC0DA9E4 CRC64;
MADVTKTEEQ EVEKSSVEEV VKTPGTSESD LGLGCGGEGD SSTSGTVQPI ANEKEVGHGD
HDGRAKRKNL DSVDEPPKKI SEIGHGQAVA AHYNELQEVG LEKRSQSRIF YLRNFNNWTK
SVLIGEFIDR VRQKKNDITV LDLGCGKGGD LLKWKKGRIK KLVCTDIADI SVQQCKHRYE
EMKARCRYNE HIFDAEFIQA DSTKDLLSSK YNDPGMRFDI CSCQFVYHYS FETYEQADMM
LKNACGNLSP GGYFIGTTPN SFELVKRLEA SETNSFGNDV YNVKFEKKGD YPLFGCKYDF
HLEEVVDVPE FLVYFPLLEE MAKKHGMKLV YKMTFREFYE EKIKNEEHKM LLRRMQALEP
YSTSGDSRLV SDKPDDYDHA KEFMKDGKAK LPLGTLSKSE WEATSIYLVF AFEKQL
//
