ID A0A178EDT8_9PLEO Unreviewed; 523 AA.
AC A0A178EDT8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=S-adenosyl-L-methionine-dependent methyltransferase {ECO:0000313|EMBL:OAL53303.1};
GN ORFNames=IQ07DRAFT_585244 {ECO:0000313|EMBL:OAL53303.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL53303.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL53303.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL53303.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METL family.
CC {ECO:0000256|ARBA:ARBA00009725}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV441640; OAL53303.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178EDT8; -.
DR STRING; 765867.A0A178EDT8; -.
DR InParanoid; A0A178EDT8; -.
DR OrthoDB; 5471626at2759; -.
DR Proteomes; UP000077535; Unassembled WGS sequence.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:UniProt.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProt.
DR GO; GO:0001510; P:RNA methylation; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR026113; METTL2/6/8-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22809:SF11; METHYLTRANSFERASE-LIKE PROTEIN; 1.
DR PANTHER; PTHR22809; METHYLTRANSFERASE-RELATED; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000313|EMBL:OAL53303.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW Transferase {ECO:0000313|EMBL:OAL53303.1}.
FT DOMAIN 219..327
FT /note="Methyltransferase type 12"
FT /evidence="ECO:0000259|Pfam:PF08242"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 58495 MW; BC8F3C8124DA29BA CRC64;
MATNSEGATT VSTENAQDAR FQTDNSVSRK VQPKQQLSKS MEHMRFAVTV DPIPHSSTPP
LPNIPTDAAK SPSAAPSLPT ATPEPASNDA YGVPASFEPV RNPASRSHDA SNNQKRSDPF
AFGSRLLEEG DNIFEFNAWD HVTVDPTYQA FSEEQYEKQR QDPVSEFDYT RFNAQPEKWW
NQFYKNNKTN FFKNRKWLAQ EFPILEQLGR EDAPPATLLE VGAGAGNSAF PILQASQNKN
LKIHACDFSK KAVDLIRAHE LYNPALIQAD VWDVASPPTA DNGGLPPGLG EGTVDVVLMI
FIFSALSPRQ WDQAVRNVWR VLKPGGQVLF RDYGRGDLAQ VRFKKGRYME ENFYVRGDGT
RVYFFEKEEL EEIWGGKKRD VQVGNVAGTQ DVGDDVEERI EALALHEPGV EGEAASEDAG
DPQMSNADVE NAHTPRPVFE VAHIGVDRRM LVNRQRRLKM YRCWMQAVFR KAGQESAVPT
STLRQESEEK EEGKSDEELG EDPVEKVGRD PVEKVQEEPE GLA
//
