ID   MTA70_MEDTR             Reviewed;         614 AA.
AC   Q2HVD6;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Putative N6-adenosine-methyltransferase MT-A70-like;
DE            EC=2.1.1.348 {ECO:0000250|UniProtKB:O82486};
GN   ORFNames=MtrDRAFT_AC148918g15v1;
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The International Medicago Genome Annotation Group;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Putative N6-methyltransferase that methylates adenosine
CC       residues of some mRNAs. N6-methyladenosine (m6A), which is present at
CC       internal sites of some mRNAs, may play a role in the efficiency of mRNA
CC       splicing, transport or translation (By similarity).
CC       {ECO:0000250|UniProtKB:O82486}.
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:0000250|UniProtKB:O82486};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O82486}.
CC   -!- SIMILARITY: Belongs to the MT-A70-like family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00489}.
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DR   EMBL; AC148918; ABD28511.1; -; Genomic_DNA.
DR   RefSeq; XP_003597586.1; XM_003597538.1.
DR   AlphaFoldDB; Q2HVD6; -.
DR   SMR; Q2HVD6; -.
DR   PaxDb; 3880-AES67837; -.
DR   EnsemblPlants; AES67837; AES67837; MTR_2g099870.
DR   GeneID; 11429893; -.
DR   Gramene; AES67837; AES67837; MTR_2g099870.
DR   KEGG; mtr:11429893; -.
DR   eggNOG; KOG2098; Eukaryota.
DR   HOGENOM; CLU_018702_3_0_1; -.
DR   OMA; ARIHNTH; -.
DR   OrthoDB; 179166at2759; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
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; Nucleus; RNA-binding; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..614
FT                   /note="Putative N6-adenosine-methyltransferase MT-A70-like"
FT                   /id="PRO_0000260071"
FT   REGION          59..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..492
FT                   /note="Positively charged region required for RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q86U44"
FT   REGION          589..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         391..392
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q86U44"
FT   BINDING         409
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q86U44"
FT   BINDING         526
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q86U44"
FT   BINDING         549..552
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q86U44"
FT   BINDING         562..563
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q86U44"
SQ   SEQUENCE   614 AA;  69286 MW;  6D23498646697FAA CRC64;
     MEMETDEGIN SLKARIETQH KSHMYMLSSV QSVIPNFVSS LDLSLKVLSS FNHRPFAPTP
     PLTNFNPPKS SSLQQLPQKP SVKTLKTSLV VTTNPVLEKV TPLSVVLSMV AVCLLSRLPF
     MEIDSSTLWR KLENDETFTP QDKAAFQELA GDSGGPTLAV EIALRSMADD NGAVELEEFA
     VSGKSRIMVL NIDRTRLLRQ LPETAQHQLQ QQQDELSLGD GNMNQNQQQI AKCSMNLEDV
     DALINKKSFR EMQKYETAKE LLKIIQTPSI REAAVAAKFK TKGGSQMRPY CDLPTKEDCR
     RRTGSFIACN KLHFRRIIAL HTDINLGDCP FLRTCRHMNT CKYVHYEEDP TPDLPPTMMC
     APPPPLKPLK QQRAEYCSEA ELGQPQWINC DIRNFRMDIL GKFGVIMADP PWDIHMELPY
     GTMADDEMRT LNVPALQTHG LIFLWVTGRA MELGRECLER WGYKCVEEII WVKTNQLQRI
     IRTGRTGHWL NHSKEHCLVG IKGSPEVNRN IDTNVIVSEV RETSRKPDEM YAMMERISPG
     TRKVELFARM HNTHAGWMSL GNQLSGVRLV DEGLRARFKA AYPDVEVQPA SPSRASAMEL
     DSSVAAQTTT SAMM
//