ID A0A164Z3Q4_9AGAM Unreviewed; 542 AA.
AC A0A164Z3Q4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=mRNA m(6)A methyltransferase {ECO:0000256|ARBA:ARBA00012160};
DE EC=2.1.1.348 {ECO:0000256|ARBA:ARBA00012160};
GN ORFNames=SISNIDRAFT_405204 {ECO:0000313|EMBL:KZS97511.1};
OS Sistotremastrum niveocremeum HHB9708.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314777 {ECO:0000313|EMBL:KZS97511.1, ECO:0000313|Proteomes:UP000076722};
RN [1] {ECO:0000313|EMBL:KZS97511.1, ECO:0000313|Proteomes:UP000076722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB9708 {ECO:0000313|EMBL:KZS97511.1,
RC ECO:0000313|Proteomes:UP000076722};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(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}.
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DR EMBL; KV419396; KZS97511.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164Z3Q4; -.
DR STRING; 1314777.A0A164Z3Q4; -.
DR OrthoDB; 179166at2759; -.
DR Proteomes; UP000076722; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000076722};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 104..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 60913 MW; 12D419CE610D40D9 CRC64;
MESSTDSFLS TVSSALHRLL QDTHKYKLHF PLTSRELFFK CISSSPVTPG SNASPIRLPD
LPRFERALEQ FSQTWELGEI VLNKSTDNSD VLILNISLGA RKAKGKKRKR DEEDDSGEDE
DEGLTEAATK KEDMPLGVFS PELQEVYALI QRGTAKKRLL AQQFASAHEQ FEPICPMITK
DDCARSRWND DVNHPTPICE KVHFRTLIRP HTDPTLGHCS YLNTCYSEPS YALSPSIPPT
PSRFPGNSQQ PGRFPQPDGG RGPTSLPSGL GAGGRGKEKA PCRYLHFEVD WDGGDGGDQP
RPLPPPTKKP VTLPMGLGPD GKNSKTYPPQ WLNCDLRKFD YSVLGKFHVI MADPPWDIHM
SLPYGTMTDD EMRAMPIPML QDEGLLFLWV TGRALEVGRE CMRVWGYTRV DEVVWVKTNQ
LQRVIRTGRT GHWLNHTKEH MLVGLKAPTN DAGELIWPSW INRGIDADVI VSEVRETSRK
PEEAYGLIER ICPGGRKVEI FGRKHNTRPG WLTLGNQLGN DQIYEEDLAA RIKARYAPIL
SK
//
