ID A0A1D6F447_MAIZE Unreviewed; 548 AA.
AC A0A1D6F447;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=type I protein arginine methyltransferase {ECO:0000256|ARBA:ARBA00011925};
DE EC=2.1.1.319 {ECO:0000256|ARBA:ARBA00011925};
GN ORFNames=ZEAMMB73_Zm00001d007133 {ECO:0000313|EMBL:ONM26102.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM26102.1};
RN [1] {ECO:0000313|EMBL:ONM26102.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM26102.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CM007648; ONM26102.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6F447; -.
DR SMR; A0A1D6F447; -.
DR IntAct; A0A1D6F447; 2.
DR STRING; 4577.A0A1D6F447; -.
DR InParanoid; A0A1D6F447; -.
DR ExpressionAtlas; A0A1D6F447; baseline and differential.
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:0000313|EMBL:ONM26102.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|EMBL:ONM26102.1}.
SQ SEQUENCE 548 AA; 60443 MW; D639BE35EBA35E3C CRC64;
MASSPDLFPN VTFSDVSEAA AGPAAEGATA AFGLGAATGA PRLSLVKAEA EPTVEIDLAD
AQVFKLGPTE WLCVCDESEA KDGVEEYVLN GYMLTLSSLR QKSFSRAIKV VLRTEAESKA
FSLAFQRWQH QVISGKAGER LENGSIIASK NKFDTKIEAS SAKMYFHYYG QLLHQQNMLQ
DFVRTGTYYA AVMENRSDFE GRVVVDVGAG SGILSLFAVQ AGARHVYAVE ASEMAEHAQR
LISGNPSLGH RITVIKGKVE EVVLPEKADI LISEPMGTLL VNERMLESYV IARDRLLAPD
GKMFPTTGRI HMAPFSDEYL YVEMANKALF WQQHNFFGVD LTPLHGSAFQ GYFSQPVVDA
FDPRLLISPP TYHTLDFTSM KEEELYEINI PLSFVASVGT RVHGLACWFD VLFNGSTVQR
WLTTAPGSPT THWYQLRCVL SQPLYVMAGQ EITGHLRLVA HSAQSYTIYL TMSAKMWGVG
AEQGGILQTS TGKLELKEPY YRLSQPQSCT LPQDQQQQQL PSLQAQGSEQ QMQEGLSPAF
TIDQDCLN
//