MTA70_ORYSJ
ID MTA70_ORYSJ Reviewed; 706 AA.
AC Q6EU10; A0A0P0VMW0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Probable N6-adenosine-methyltransferase MT-A70-like;
DE EC=2.1.1.348 {ECO:0000250|UniProtKB:O82486};
GN OrderedLocusNames=Os02g0672600, LOC_Os02g45110;
GN ORFNames=OJ1197_E09.7, OJ1493_H11.20;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- FUNCTION: Probable 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; AP004160; BAD27818.1; -; Genomic_DNA.
DR EMBL; AP004188; BAD27860.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09621.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS80247.1; -; Genomic_DNA.
DR EMBL; AK070286; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK101174; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015625439.1; XM_015769953.1.
DR AlphaFoldDB; Q6EU10; -.
DR SMR; Q6EU10; -.
DR STRING; 4530.OS02T0672600-01; -.
DR iPTMnet; Q6EU10; -.
DR PaxDb; Q6EU10; -.
DR PRIDE; Q6EU10; -.
DR EnsemblPlants; Os02t0672600-01; Os02t0672600-01; Os02g0672600.
DR GeneID; 4330284; -.
DR Gramene; Os02t0672600-01; Os02t0672600-01; Os02g0672600.
DR KEGG; osa:4330284; -.
DR eggNOG; KOG2098; Eukaryota.
DR HOGENOM; CLU_018702_3_0_1; -.
DR InParanoid; Q6EU10; -.
DR OMA; PESAQYQ; -.
DR OrthoDB; 349671at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6EU10; OS.
DR GO; GO:0016607; C:nuclear speck; IEA:EnsemblPlants.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IEA:EnsemblPlants.
DR GO; GO:0080009; P:mRNA methylation; IBA:GO_Central.
DR InterPro; IPR007757; MT-A70-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF05063; MT-A70; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51143; MT_A70; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Nucleus; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..706
FT /note="Probable N6-adenosine-methyltransferase MT-A70-like"
FT /id="PRO_0000260072"
FT REGION 64..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..580
FT /note="Positively charged region required for RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q86U44"
FT REGION 669..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 479..480
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86U44"
FT BINDING 497
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86U44"
FT BINDING 614
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86U44"
FT BINDING 637..640
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86U44"
FT BINDING 650..651
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86U44"
FT CONFLICT 504
FT /note="M -> I (in Ref. 4; AK101174)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="D -> N (in Ref. 4; AK101174)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="R -> L (in Ref. 4; AK070286)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="K -> R (in Ref. 4; AK101174)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 706 AA; 77803 MW; 91BDDF2AAEABA405 CRC64;
MEAQADAGGD DLAAMREQCR SLEEAIGFRR ETQMGLVASL QRLVPDLVPS LDRSLRIIAA
FNDRPFVPTP NPDGGHGKSP AALKPHHRRA LPDPARSTRR KTSPGSSPAS VAAAPGGLDA
VRTMVAVCLL ELVPFAEIDA AALARRLQAE SSSASEAERT ALADLAAELG GSAASAVVLA
LRRIAEDTGG VQIEEAMIGG KSMTMVWAID RNKLLKELPE SATLPLLQPP PAPQMPPSET
DAGSAMIPRT PQQQQPQPDM WPHSMPPIFP RPRGMTMQGM QRVPGVPPGL MPLQRPFMGP
AGVITMGGGV GPSPNQQKQK SEEDELKDLE LLLNKKTYRE KQNTKTGEEL LDLIHRPTAK
ETAVAAKFKT KGGSQLKEYC TNLTKEDCRR QSGSFVACDK VHFRRIIAPH TDTNLGDCSF
LDTCRHTKTC KYVHYELDQT PDIPPMMAGA LAPPRQIRLQ RAEYCSEVEL GEAQWINCDI
RNFRMDILGQ FGVIMADPPW DIHMELPYGT MADDEMRTLN VPALQTDGLI FLWVTGRAME
LGRECLELWG YKRVEEIIWV KTNQLQRIIR TGRTGHWLNH SKEHCLVGIK GNPLVNRNID
TDVIVAEVRE TSRKPDEMYP MLERISPRTR KLELFARMHN AHAGWLSLGN QLNGVRLVDE
GLRARYKAAY PDSEVQPPSP PRASAPIDGD QGTSQKPTVS DGERPA
