ID A0A165M813_9AGAM Unreviewed; 366 AA.
AC A0A165M813;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=S-adenosyl-L-methionine-dependent methyltransferase {ECO:0000313|EMBL:KZT18014.1};
GN ORFNames=NEOLEDRAFT_1184674 {ECO:0000313|EMBL:KZT18014.1};
OS Neolentinus lepideus HHB14362 ss-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT18014.1, ECO:0000313|Proteomes:UP000076761};
RN [1] {ECO:0000313|EMBL:KZT18014.1, ECO:0000313|Proteomes:UP000076761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT18014.1,
RC ECO:0000313|Proteomes:UP000076761};
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).
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DR EMBL; KV425728; KZT18014.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165M813; -.
DR STRING; 1314782.A0A165M813; -.
DR InParanoid; A0A165M813; -.
DR OrthoDB; 1467982at2759; -.
DR Proteomes; UP000076761; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000313|EMBL:KZT18014.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076761};
KW Transferase {ECO:0000313|EMBL:KZT18014.1}.
FT DOMAIN 130..219
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..48
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 366 AA; 41083 MW; B8522450893A5169 CRC64;
MDDGSGRPST RHPSAGQPVL LNSGDMSDDN ALDDDEDVHS DASSDLVEVS EEDICDSFVT
RDGRLFHSHG SLPYPLPADG LEQHVSHFFR TYLIWRLKVQ NEVLKALMGS ICPEMQLVRE
VLASGTGRAL DLCTGTGQWV LDMASMFPNV KFIGVDIVPI QTRRPPRNAQ FEIADVTEPF
RHLDGSFDLV HARCTAFSVS DHKYPIMLRE VVRVLRGGGL FISGEFKNYP AFPSRRAESA
DPNVSCPSFH RFLMLTAQAL HRLGVRLNLF HKIPLLLEES GSFYGISRRS FQLPIGNRHP
EESNRILGSQ AAEIFINFVK AMESFLRSSG IITREHLQEL MRGSIYELQH VNGLVMDYDV
VCARKR
//