ID A0A1J8PN31_9AGAM Unreviewed; 540 AA.
AC A0A1J8PN31;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, 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=AZE42_04882 {ECO:0000313|EMBL:OJA09919.1};
OS Rhizopogon vesiculosus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=180088 {ECO:0000313|EMBL:OJA09919.1, ECO:0000313|Proteomes:UP000183567};
RN [1] {ECO:0000313|EMBL:OJA09919.1, ECO:0000313|Proteomes:UP000183567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-056 {ECO:0000313|EMBL:OJA09919.1,
RC ECO:0000313|Proteomes:UP000183567};
RA Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA Barry K., Grigoriev I.V., Spatafora J.W.;
RT "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT divergence of the mating type B locus.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJA09919.1}.
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DR EMBL; LVVM01005715; OJA09919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J8PN31; -.
DR STRING; 180088.A0A1J8PN31; -.
DR OrthoDB; 179166at2759; -.
DR Proteomes; UP000183567; 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:UP000183567};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 100..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 60420 MW; E0173943434A8F60 CRC64;
MSDNDVSLLV SISLQTLLSS GKISTPLTSM DFLLALISYN ASTSFSGLKI PRLSDLPRVE
KVLQAFSSNW EHGSILLSRE GGELTITDVH LGNSRVLNSR KRKRAPIDED ADSAAGDNPD
ETSSSNGDND SPNVNTPLGS LSKDLREVYV ILQKSTAKGR LLAERFRCVN GGFEPICTYI
TKADCAKSRS QADPANPFNP AFCDRLHFRP LIRLHTDPNL GHCSYLNTCY SEPTYSQSPS
ITPFPPGTGA RVSLPSGLGA GGRGKEKAPC RYLHFEIDWD EKDGPLAPTD AWRSQRVKKP
FKIELGMGPD GKNMQVLPPQ WLNCDLRRFD YSVLGKFHVI MADPPWDIHM SLPYGTMTDD
EMRAMPIPTL QDEGILFLWV TGRAMEVGRE CLRVWGYTRV DEVVWVKTNQ LQRVIRTGRT
GHWLNHTKEH MLVGVKTRTD AAGNLVFPSW ANRGLDTDVI VSEVRETSRK PDEVYGLIER
MCPGGRKIEI FGRKHNTRPG WLTLGNQLGQ DQIYEEDLAA RIKARYPERF MTAPSQPMHH
//
