ID A0A1D2MRP9_ORCCI Unreviewed; 484 AA.
AC A0A1D2MRP9;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=mRNA m(6)A methyltransferase {ECO:0000256|ARBA:ARBA00012160};
DE EC=2.1.1.348 {ECO:0000256|ARBA:ARBA00012160};
GN ORFNames=Ocin01_11276 {ECO:0000313|EMBL:ODM95405.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODM95405.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODM95405.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODM95405.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
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:ODM95405.1}.
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DR EMBL; LJIJ01000677; ODM95405.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D2MRP9; -.
DR STRING; 48709.A0A1D2MRP9; -.
DR OrthoDB; 179166at2759; -.
DR Proteomes; UP000094527; 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 ECO:0000313|EMBL:ODM95405.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000094527};
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:ODM95405.1}.
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 53958 MW; 69334A12A9ABCAF1 CRC64;
MSDAWAEIQA LKSKRESRRI RLEERKKERQ DILNRGLVVG ENAPSGSSPS SSPRVKADPN
AASSDIKHNA GGSQAGGGGD SLPVTPITSG SASEPIKFQS PEKIKSDAEP EHFIDGSFED
YVLQTLSDVA LRLPMDSKQL LVTVNKALAT SVTHLQIFNL LQKFAVQQLI SIEEKLSDGG
PYIEIITADH TKLLAIVHST RKLKDDKSRF RRVLGCEHPE KKSQERLIID VFGERRPKKA
IRSSTDTRLP LLSPNGVLSS TLETQAAPTT VLNPPQWIQC DLRFFDMATL GKFSVIMADP
PWDIHMELPY GTLSDDEMRQ LNIPALQDEG LIFLWVTGRA MELGRECLEL WGYERVDELI
WVKTNQLQRI IRTGRTGHWL NHGKEHCLVG MKGNPPVNRG LDCDVIVAEV RATSHKPDEI
YGIIERLSPG TRKIELFGRP HNIQPNWVTL GNQLSGTHIV EEDIRNRVVG RYPDGNFGAG
KSTK
//
