ID A0A150V357_9PEZI Unreviewed; 497 AA.
AC A0A150V357;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Methyltransferase domain-containing protein {ECO:0000259|Pfam:PF13649};
GN ORFNames=M433DRAFT_154992 {ECO:0000313|EMBL:KYG45004.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG45004.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG45004.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG45004.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
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:KYG45004.1}.
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DR EMBL; JPDO01000190; KYG45004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150V357; -.
DR STRING; 766039.A0A150V357; -.
DR Proteomes; UP000075602; Unassembled WGS sequence.
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 PANTHER; PTHR43591; METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43591:SF113; SAM BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000075602}.
FT DOMAIN 179..278
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 55708 MW; 7DEE2FBEA9FCBF59 CRC64;
MDGLIYAYHA PRSAAQQQYT RERLAAIAEE RRQKLQQQRS KEGGGDSVEC IERTLTGESA
RSGGSTTTEP LRLQQQQQQQ QQQQHRRDDS YYGGGMDHLR TGTSSSSGSS AHSEQAHQYL
LNHPYELRHG RRYLQEVPYP LPCDLAEMQR QNLRTLLSCR IFGRPVCSPN LSKEVPKKVL
ELGCGSGFWS ATCHDYFASR GHKHVAFTGL DVAPLAPDLK KQGMNWTFVQ HDIRRIPLPF
DDGDFDMVML KDLSLTLPLG PPYQKFLDEA IRILREGGTL EIWDSDYILR SLLPHPPPPS
KKPLDQDIAD ATATFLIAPG TPFTPAQNKY LQQANQWISE ALDKRNLPPV PCARISQVLY
QEPDSLKDIG LKRVAIPLGE QNRWERDSPR HTRHASEVVD SPQSSKGKTK VGGGDKALTP
DQAALRQTAL LTVLQMIESM EPLLKEVSGK NSEEWSHWWA SMMADLLDPS RGALTGECLE
IGAWWATKVG SGENTTR
//
