ID A0A0J7KQ31_LASNI Unreviewed; 512 AA.
AC A0A0J7KQ31;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=mRNA m(6)A methyltransferase {ECO:0000256|ARBA:ARBA00012160};
DE EC=2.1.1.348 {ECO:0000256|ARBA:ARBA00012160};
GN ORFNames=RF55_7537 {ECO:0000313|EMBL:KMQ92462.1};
OS Lasius niger (Black garden ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Lasius; Lasius.
OX NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ92462.1, ECO:0000313|Proteomes:UP000036403};
RN [1] {ECO:0000313|EMBL:KMQ92462.1, ECO:0000313|Proteomes:UP000036403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole {ECO:0000313|EMBL:KMQ92462.1};
RA Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT "Lasius niger genome sequencing.";
RL Submitted (APR-2015) 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:KMQ92462.1}.
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DR EMBL; LBMM01004397; KMQ92462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7KQ31; -.
DR STRING; 67767.A0A0J7KQ31; -.
DR PaxDb; 67767-A0A0J7KQ31; -.
DR OrthoDB; 179166at2759; -.
DR Proteomes; UP000036403; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0016422; F:mRNA (2'-O-methyladenosine-N6-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0001734; F:mRNA (N6-adenosine)-methyltransferase activity; IEA:UniProt.
DR InterPro; IPR025848; MT-A70.
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; PS51563; SAM_MTA70L_1; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KMQ92462.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000036403};
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:KMQ92462.1}.
FT REGION 102..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 512 AA; 57445 MW; 6EF65E0C5391989D CRC64;
MKKNSFAILM YKSVADSNAS SRSDHSEYER DVLCILHESL PNLPITSADL IDQLRKNLNA
DVSSSDIHKI LEKLAAQDIV KIKEVTENGV FGYTVLSVTE SHSSCQSQSD DTENPESVET
SASDPNDHVP PEKQAKIEKK NTEDIMSLIS MPTIREKESK KVGEQILDLL SKQTSKEKSL
AERFRSQGGA QVMEFCPHGT RVDCVKLNGG PGFAEKCKKL HFKKIIQSHT DESLGDCSFL
NTCFHMDTCK YVHYEVDGPT AQPKETNDPD SLNNSASSKT LNLDNKNNGG TSSNVGSELT
LYPPQWIQCD LRYLDMTVLG KFAVIMADPP WDIHMELPYG TMSDDEMRQL GIPALQDEGL
LFLWVTGRAM ELGRECLQLW GYERVDEIIW VKTNQLQRII RTGRTGHWLN HGKEHCLVGM
KGNPRINRGL DSDVIVAEVR ATSHKPDEIY GIIERMSPGT RKIELFGRPH NVQPNWITLG
NQVDGVHLID PQLIKAFKKR YPDGNSMKPA KP
//