ID A0A2I4F3B3_JUGRE Unreviewed; 540 AA.
AC A0A2I4F3B3;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=type I protein arginine methyltransferase {ECO:0000256|ARBA:ARBA00011925};
DE EC=2.1.1.319 {ECO:0000256|ARBA:ARBA00011925};
GN Name=LOC108995079 {ECO:0000313|RefSeq:XP_018826128.1};
OS Juglans regia (English walnut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Juglandaceae; Juglans.
OX NCBI_TaxID=51240 {ECO:0000313|Proteomes:UP000235220, ECO:0000313|RefSeq:XP_018826128.1};
RN [1] {ECO:0000313|RefSeq:XP_018826128.1}
RP IDENTIFICATION.
RC TISSUE=Leaves {ECO:0000313|RefSeq:XP_018826128.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319;
CC Evidence={ECO:0000256|ARBA:ARBA00001817};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_018826128.1; XM_018970583.2.
DR AlphaFoldDB; A0A2I4F3B3; -.
DR STRING; 51240.A0A2I4F3B3; -.
DR EnsemblPlants; Jr07_18690_p1; cds.Jr07_18690_p1; Jr07_18690.
DR GeneID; 108995079; -.
DR Gramene; Jr07_18690_p1; cds.Jr07_18690_p1; Jr07_18690.
DR KEGG; jre:108995079; -.
DR InParanoid; A0A2I4F3B3; -.
DR OrthoDB; 197898at2759; -.
DR Proteomes; UP000235220; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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 PANTHER; PTHR11006:SF10; HISTONE-ARGININE METHYLTRANSFERASE CARMER-RELATED; 1.
DR PANTHER; PTHR11006; PROTEIN ARGININE N-METHYLTRANSFERASE; 1.
DR Pfam; PF06325; PrmA; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01015,
KW ECO:0000313|RefSeq:XP_018826128.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000235220};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01015};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU01015}.
FT REGION 521..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 60470 MW; 9E04326FF4D53801 CRC64;
MEGPTGQKLK QQEFALVSVS ELSPSSSTSP SKLVVARFCA DSGISELRFH KEPESIATRN
VDLRTARLFK LGPVQSVCIS EGSEASKETS YSRGITVQFR NEEESRTFHS AFEQWKKEVS
QGKQLSNGTV LDTRSKFDDK IEPSSAKMYF HYYGQLLHQQ NMLQDYVRTG TYYAAVVENR
TDFIGRVVVD VGAGSGILSL FAAQAGAKHV YAVEASEMAE YAQKLIAGNP SLGQRITVVK
GKVEEVELPE KADILISEPM GTLLVNERML ESYVIARDRF LVPNGKMFPT VGRIHMAPFS
DEYLFVEIAN KALFWQQHNY YGVDLTPLHG SAFQGYFSQP VVDAFDPRLL VAPPIFHGID
FMKIKEEELY EIDIPLRFTS SVGARVHGLA CWFDVLFNGS TVQRWLSTAP GAPTTHWYQL
RCVLSQPIYV MAGQEITGRL HMIAHNAQSY TIYLTLSAKM WGPGAEQGGI LQTSSCKLDL
KEPYYRMSQP QAYPIVQDQQ SHQLISTQDI PIQSHDLEEP ELMQQPSPNS GTHLNIMENV
//