ID A0A1M8A638_MALS4 Unreviewed; 395 AA.
AC A0A1M8A638;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=mRNA m(6)A methyltransferase {ECO:0000256|ARBA:ARBA00012160};
DE EC=2.1.1.348 {ECO:0000256|ARBA:ARBA00012160};
GN ORFNames=MSYG_2243 {ECO:0000313|EMBL:SHO77901.1};
OS Malassezia sympodialis (strain ATCC 42132) (Atopic eczema-associated
OS yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=1230383 {ECO:0000313|EMBL:SHO77901.1, ECO:0000313|Proteomes:UP000186303};
RN [1] {ECO:0000313|Proteomes:UP000186303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42132 {ECO:0000313|Proteomes:UP000186303};
RX PubMed=28100699; DOI=10.1093/nar/gkx006;
RA Zhu Y., Engstroem P.G., Tellgren-Roth C., Baudo C.D., Kennell J.C., Sun S.,
RA Billmyre R.B., Schroeder M.S., Andersson A., Holm T., Sigurgeirsson B.,
RA Wu G., Sankaranarayanan S.R., Siddharthan R., Sanyal K., Lundeberg J.,
RA Nystedt B., Boekhout T., Dawson T.L. Jr., Heitman J., Scheynius A.,
RA Lehtioe J.;
RT "Proteogenomics produces comprehensive and highly accurate protein-coding
RT gene annotation in a complete genome assembly of Malassezia sympodialis.";
RL Nucleic Acids Res. 45:2629-2643(2017).
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; LT671823; SHO77901.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M8A638; -.
DR STRING; 1230383.A0A1M8A638; -.
DR VEuPathDB; FungiDB:MSYG_2243; -.
DR Proteomes; UP000186303; Chromosome 3.
DR GO; GO:0001734; F:mRNA (N6-adenosine)-methyltransferase activity; IEA:UniProt.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
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.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:SHO77901.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000186303};
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:SHO77901.1}.
SQ SEQUENCE 395 AA; 44672 MW; 8E6E76DA1369F304 CRC64;
MRAAQEDAAT VIAIRYLSRP TGKQRILAKL LQSTDNRFQA LCEHITRPAC AQARAAQGAP
TFCERVHFKP LIMPHTKVEL GHCGYLSSCH RKMTCPFLHF VVDDSLLQTP FEWKCSSLTP
YPMCSERAME ASLREPMQQL DRYGLAAWVR AGPERALDKQ FRPGQWIDCD LRAFDLSTLG
HFDVILADPP WDIHMSLPYG TLSDDDMRAL DVPALQAEGL LFLWVTGRSM ELGRQLLGQW
GYTRADELIW IKTNQMERLV RTGRTGHWLN HSKEHCLVGI KYAKRRDQPD AWAPGQSRHV
LPWLHDGLGT DVIVSQVRDT SRKPDELYAM IEKMCPGGRK IELFGRRHNV RPGWLTLGNQ
LKSTYVVEPK LQAACAATEP AGPAVPRTPA RTSIT
//
