ID A0A165IDG9_9APHY Unreviewed; 564 AA.
AC A0A165IDG9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=mRNA m(6)A methyltransferase {ECO:0000256|ARBA:ARBA00012160};
DE EC=2.1.1.348 {ECO:0000256|ARBA:ARBA00012160};
GN ORFNames=LAESUDRAFT_719228 {ECO:0000313|EMBL:KZT12930.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT12930.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT12930.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT12930.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an adenosine in mRNA + S-adenosyl-L-methionine = an N(6)-
CC methyladenosine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:55584, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12417,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; EC=2.1.1.348;
CC Evidence={ECO:0000256|ARBA:ARBA00036277};
CC -!- SIMILARITY: Belongs to the MT-A70-like family. {ECO:0000256|PROSITE-
CC ProRule:PRU00489}.
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DR EMBL; KV427605; KZT12930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165IDG9; -.
DR STRING; 1314785.A0A165IDG9; -.
DR InParanoid; A0A165IDG9; -.
DR OrthoDB; 179166at2759; -.
DR Proteomes; UP000076871; Unassembled WGS sequence.
DR GO; GO:0001734; F:mRNA (N6-adenosine)-methyltransferase activity; IEA:UniProt.
DR InterPro; IPR007757; MT-A70-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12829; N6-ADENOSINE-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR12829:SF2; N6-ADENOSINE-METHYLTRANSFERASE CATALYTIC SUBUNIT; 1.
DR Pfam; PF05063; MT-A70; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51143; MT_A70; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 106..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 62442 MW; F8B46E6B927985CE CRC64;
MSADDRLKLV ASSALLNLFS SYKVTTPISS FDLLTRVIAS GPPPAGLLPG PGPPPTFRLT
DLSRFETVLE SLSETWEHGN ISVLREARDG ELMVMEVNVG EAASSAALGH GRKRKRVVDE
DADSAAGDAE EEEDERLEQM RARMKPAPTT LASLSKDMKE VYNILQRSTA KGRLLAEHFR
SVNSGFEPIC PHITKNECAK ARRLAAAATD PAAADAPATI CDRVHFRPLI RPHTDPSLGH
CSYLNTCYSE PTYAQSPSIP PLPSHRQTGY GAQGAATVSL PSGLGAGGRG KEKAPCRYLH
FEIDWDASDG ATQPESRVEV RKKVYKLPIG MGPTGKETPM LPPQWINCDL RRFDYSVLGK
FHVIMADPPW DIHMSLPYGT MTDDEMRAMP IPALQDEGLL FLWVTGRAME VGRECLRVWG
YTRVDEVVWV KTNQLQRVIR TGRTGHWLNH TKEHMLVGVK TVTDEAGNLK FPSWANRGLD
TDVIVSEVRE TSRKPDEVYG MIERMCPGGR KIEIFGRKHN TRPGWLTLGN QLGLADQIYE
EDLAARIKAR YPERNVNALP MGGQ
//
