ID A0A2T4AS09_TRIHA Unreviewed; 536 AA.
AC A0A2T4AS09;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Methyltransferase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=M431DRAFT_478865 {ECO:0000313|EMBL:PTB59859.1};
OS Trichoderma harzianum CBS 226.95.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983964 {ECO:0000313|EMBL:PTB59859.1, ECO:0000313|Proteomes:UP000241690};
RN [1] {ECO:0000313|EMBL:PTB59859.1, ECO:0000313|Proteomes:UP000241690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 226.95 {ECO:0000313|EMBL:PTB59859.1,
RC ECO:0000313|Proteomes:UP000241690};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ679676; PTB59859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4AS09; -.
DR STRING; 983964.A0A2T4AS09; -.
DR OrthoDB; 197898at2759; -.
DR Proteomes; UP000241690; Unassembled WGS sequence.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.70.160.11; Hnrnp arginine n-methyltransferase1; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR049482; ANM3-like_C2H2_Zf.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR11006; PROTEIN ARGININE N-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11006:SF116; PROTEIN METHYLTRANSFERASE; 1.
DR Pfam; PF21137; ANM3_C2H2_Zf; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01015}; Reference proteome {ECO:0000313|Proteomes:UP000241690};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01015}.
FT DOMAIN 65..109
FT /note="Protein arginine N-methyltransferase 3-like C2H2
FT zinc finger"
FT /evidence="ECO:0000259|Pfam:PF21137"
FT DOMAIN 237..334
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 536 AA; 60270 MW; DF221120061351E8 CRC64;
MSARSESGSS SATSDVSNEG EWLDIENDEE SITIVSLFDS QTFSSWNEML DSCKKHHDFD
FIATIKNLQL DFHGAVKLVN YIRSRVRDQQ PVAKNLTLAD FEDDGYFKPV LENDALIVSL
DEILDSDLVK ADTTASQLDS SQGELLVQKQ ALEAELESVR TQFSNYRLAV QETLDRRWGD
DTEQSPAKAV KGDRGNYYFE SYAYNDIHET MLKDTVRTDA YRDFIYNNKH IFKGKVVLDI
GCGSGILSMF CAKAGAARVI AVDNSDIIKK ATENIFNNGL SDIITCVKGA IEEVKLPVNE
VDIIVSEWMG YCLLYEAMLP SVLYARDRYL KPDGLLVPSS GTIWMAPIQD TEYMSEHISY
WRDVYGFDMK AMQEGIYDDV RVEAMPQNTL CGEPYPFKVL DLHTIKPEEL SFTARWESKL
LRRPDGLDGF LIWFDNFFAT SRSEPVPEPT TTPEVFGKAK NGNVAFTTGP SGIVTHWKQG
LLLVPPENPP SKLELPETIS GQITFAALEE NARALRIDVT CSSGSKEGKK WSWKLE
//
