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Database: UniProt
Entry: A0A1D6F447_MAIZE
LinkDB: A0A1D6F447_MAIZE
Original site: A0A1D6F447_MAIZE 
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
//
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