ID A0A2N1JHF0_9BASI Unreviewed; 575 AA.
AC A0A2N1JHF0;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Methyltransferase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=MVES_000155 {ECO:0000313|EMBL:PKI85980.1};
OS Malassezia vespertilionis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=2020962 {ECO:0000313|EMBL:PKI85980.1, ECO:0000313|Proteomes:UP000232875};
RN [1] {ECO:0000313|EMBL:PKI85980.1, ECO:0000313|Proteomes:UP000232875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NWHC:44797-103 {ECO:0000313|EMBL:PKI85980.1,
RC ECO:0000313|Proteomes:UP000232875};
RA Lorch J.M., Palmer J.M., Vanderwolf K.J., Schmidt K.Z., Verant M.L.,
RA Weller T.J., Blehert D.S.;
RT "A novel species of cold-tolerant Malassezia isolated from bats.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ454987; PKI85980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N1JHF0; -.
DR STRING; 2020962.A0A2N1JHF0; -.
DR OrthoDB; 197898at2759; -.
DR Proteomes; UP000232875; 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; IPR025799; Arg_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR11006:SF53; ARGININE METHYLTRANSFERASE 1-RELATED; 1.
DR PANTHER; PTHR11006; PROTEIN ARGININE N-METHYLTRANSFERASE; 1.
DR Pfam; PF06325; PrmA; 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 Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01015};
KW Reference proteome {ECO:0000313|Proteomes:UP000232875};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01015};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU01015}.
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 63869 MW; 67C03F4D734A6C8F CRC64;
MAYRVQLDDT SSTYTGPHMR SEAFDASKTH TPVHEDVDED NDDLDNYDGW QEEAAPTRAL
FPAHDKLYAD AEEALADAKR QGCDFRALVS KLHLDALQVI RLVNYIRRAN VPPTEAAALT
GHESFLKDDA ELKPVPGYEE DGLLQVDFDD DESVDNDPLA ELATLRAAYQ ELRLQYAERL
GIGAADAHGT AKPPSSPAGG DAHYFDSYAG HDIHQTMISD TARTLSYAQF ILSPENAHLL
RGKTVMDVGC GSGILSLFCA RAGAKQVLAI DASDVVERAE ANIAENGFTN VIRVFRGKIE
ELDAQLLSYV GQVDFLVSEW MGYFLLYESM LPSVLYARER YLAKDGILAP SHCRMLLAAA
TDRGNGALRE RYRFWDNVYG FRMPTMTKGL AEDAAVEEVE QDAIVSTVAP ICELPLEQLA
VRQPEFVSPF ALTCTETCTV YGFVSWFDTW FCPAPRVDPA DLPSCRVDPI EQSEVHGLDL
HGNQVTNAPA QGKGQTVSFT TSPFGKQTHW KQTVFLLKMP VEAIEGTRIT GEIRVHTSAN
NERELDVEIH YDVDERPRPG EKRVQSRLVQ LYSVR
//