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Database: UniProt
Entry: A0A087RBC6_APTFO
LinkDB: A0A087RBC6_APTFO
Original site: A0A087RBC6_APTFO 
ID   A0A087RBC6_APTFO        Unreviewed;       405 AA.
AC   A0A087RBC6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=mRNA (guanine-N(7))-methyltransferase {ECO:0000256|ARBA:ARBA00011926};
DE            EC=2.1.1.56 {ECO:0000256|ARBA:ARBA00011926};
DE   AltName: Full=RG7MT1 {ECO:0000256|ARBA:ARBA00033043};
DE   Flags: Fragment;
GN   ORFNames=AS27_05770 {ECO:0000313|EMBL:KFM10780.1};
OS   Aptenodytes forsteri (Emperor penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC   Aptenodytes.
OX   NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM10780.1, ECO:0000313|Proteomes:UP000053286};
RN   [1] {ECO:0000313|EMBL:KFM10780.1, ECO:0000313|Proteomes:UP000053286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM10780.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-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   -!- 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; KL226269; KFM10780.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087RBC6; -.
DR   STRING; 9233.A0A087RBC6; -.
DR   Proteomes; UP000053286; 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   ECO:0000313|EMBL:KFM10780.1};
KW   mRNA capping {ECO:0000256|PIRSR:PIRSR028762-2};
KW   mRNA processing {ECO:0000256|PIRSR:PIRSR028762-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053286};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFM10780.1}.
FT   DOMAIN          66..405
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..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         114..115
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT   SITE            145
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT   SITE            151
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT   SITE            176
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            308
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT   SITE            405
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028762-2"
FT   NON_TER         405
FT                   /evidence="ECO:0000313|EMBL:KFM10780.1"
SQ   SEQUENCE   405 AA;  46748 MW;  F28E5E8DC6AEF1EE CRC64;
     MADITKIEEQ EAEKSLDEEV EKTPRTLEAD SGIGWEGDSS TSGTVLSTEN EKEVGSVNQD
     GRARRKNLDS EDEPPKKVRE IGHGQAVAAH YNELQEVGLE KRSQSRIFYL RNFNNWTKSV
     LIGEFIDRVR RKKNDITVLD LGCGKGGDLL KWKKGRIKKL VCTAIADISV QQCKQRYEDM
     KARCRYNEHI FDAEFIQADS TKDLLSSKYN DPDMRFDICS CQFVYHYSFE TYEQADMMLK
     NACGNLSPGG YFIGTTPNSF ELVKRLEASE TNSFGNEVYS VKFEKKGEYP LFGCKYDFHL
     EEVVDVPEFL VYFPLLEEMA KKHGMKLVYK MTFREFYEEK IKNEEHKMLL RRMQALEPYS
     TFGDSRLVSD KPDDYEHAKE FIKDGKAKLP LGTLSKSEWE ATSKY
//
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