ID A5DVJ3_LODEL Unreviewed; 339 AA.
AC A5DVJ3;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=HNRNP arginine N-methyltransferase {ECO:0000313|EMBL:EDK43201.1};
GN ORFNames=LELG_01379 {ECO:0000313|EMBL:EDK43201.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK43201.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK43201.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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DR EMBL; CH981525; EDK43201.1; -; Genomic_DNA.
DR RefSeq; XP_001526551.1; XM_001526501.1.
DR AlphaFoldDB; A5DVJ3; -.
DR STRING; 379508.A5DVJ3; -.
DR KEGG; lel:LELG_01379; -.
DR VEuPathDB; FungiDB:LELG_01379; -.
DR eggNOG; KOG1499; Eukaryota.
DR HOGENOM; CLU_017375_1_2_1; -.
DR InParanoid; A5DVJ3; -.
DR OMA; GFWDNVW; -.
DR OrthoDB; 197898at2759; -.
DR Proteomes; UP000001996; 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; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006:SF53; ARGININE METHYLTRANSFERASE 1-RELATED; 1.
DR PANTHER; PTHR11006; PROTEIN ARGININE N-METHYLTRANSFERASE; 1.
DR Pfam; PF13649; Methyltransf_25; 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 ECO:0000313|EMBL:EDK43201.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001996};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01015};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU01015,
KW ECO:0000313|EMBL:EDK43201.1}.
FT DOMAIN 57..154
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
SQ SEQUENCE 339 AA; 39083 MW; 4950A4FD9942CA17 CRC64;
MSESATDKTQ LNAYEQHYFS SYDHFGIHEE MLKDTSRTLS YRNAMYRNKD AFKGKVVLDV
GCGTGILSMF AVKAGAKHVY AVDMSSIIGR AKEIVELNGF SDKITLLQGK LEDIKLPVDS
VDIIISEWMG YFLLYESMLD TVLYARDRYL VPGGLILPDK CQMYIAGIED GQYKEEKIHY
WEDVYGFDYS PFIKTAMEEP LVDTVNNQAL VTKSFKFFEF DINTVKKEEL SFSKTFELEA
LANEQCHAYI VYWDAIFPGK EKVILPTGPM NQYTHWKQTV FYMDQVLDLK TGDKIKGSIT
AKPSTVNPRE YDIDLEWDLK TAENDASREQ KGQYKYFLR
//
