ID A0A498I2J3_MALDO Unreviewed; 789 AA.
AC A0A498I2J3;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=mRNA m(6)A methyltransferase {ECO:0000256|ARBA:ARBA00012160};
DE EC=2.1.1.348 {ECO:0000256|ARBA:ARBA00012160};
GN ORFNames=DVH24_039999 {ECO:0000313|EMBL:RXH78028.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH78028.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH78028.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH78028.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) 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:RXH78028.1}.
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DR EMBL; RDQH01000340; RXH78028.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498I2J3; -.
DR STRING; 3750.A0A498I2J3; -.
DR Proteomes; UP000290289; Chromosome 14.
DR GO; GO:0090304; P:nucleic acid metabolic process; 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:UP000290289};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 68..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..88
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 789 AA; 87334 MW; D1663624B11C8C91 CRC64;
METQSEGGDE ATIAGIRTMT QQLEARMESQ RTTQLELLSY LQSQIVPTIV PTIDLSLKVL
SAFNDRPFTP TPPLPNSKPD PRNPVEPALP STPEAQRSRL PSPEPKLTNP IEQSPKLSPK
QANSETTHQP ELENFSPIDE MGNPLSLVRA MVAVCLLEIV PFCRIDSSAV LRKLESDQKA
TAEEKAALRE MGGESGAILA VEMALRSMLE ENGGVELEEF VVGGKSGIMV LGIDRTRLMK
ELPESKQFQS RDSNLGDGNL SQSQQQVVTS GRGGDGSGGG VFGMGGPSSR PMQDMWMNPN
DTHMSGLPPM FPGSGQPGSF MGPRGAPSPR VMGMMGMPRG MGGVPPMHRA NSMGPNATMD
SPNSVSYKPQ SEEDELKDVE ALLNKKTFRE LQKSKTGEEI LDLIHRPTAK ETAVAAKFKT
KGGSQLKEYC SSLTKEDCRR QSNSVLACEK VGTQKFLLAS VMVHFRRIIA LHTDVNLGDC
SFLDTCRHMK TCKHVHYELD PTPDVSHMMM GPRDLGPPRQ LRPQRAEYCS EVELGQPQWI
NCDIRNFRMD ILGQFGVIMA DPPWDIHMEL PYGTMADDEM RNLNVPALQT DGLIFLWVTG
RAMELGRECL ELWGYKRIEE IIWVKTNQLQ RIIRTGRTGH WLNHSKEHCL VGIKGEPLVN
RNIDTDVIVA EVRETSRKPD EMYPLLERVS PRTRKLELFA RMHNTHAGWM SLGNQLSGVR
LVDEGLRARF KAAYPDVEVQ PTSPPRPSAM EVDSNAAQMR SPFSEPAVPE APYAASEVRP
SPVDVEMAG
//
