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Database: UniProt
Entry: C4JBI7_MAIZE
LinkDB: C4JBI7_MAIZE
Original site: C4JBI7_MAIZE 
ID   C4JBI7_MAIZE            Unreviewed;       263 AA.
AC   C4JBI7;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=type I protein arginine methyltransferase {ECO:0000256|ARBA:ARBA00011925};
DE            EC=2.1.1.319 {ECO:0000256|ARBA:ARBA00011925};
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:ACR38537.1};
RN   [1] {ECO:0000313|EMBL:ACR38537.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B73 {ECO:0000313|EMBL:ACR38537.1};
RX   PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA   Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA   Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA   Walbot V., Yu Y.;
RT   "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL   PLoS Genet. 5:E1000740-E1000740(2009).
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; BT088184; ACR38537.1; -; mRNA.
DR   AlphaFoldDB; C4JBI7; -.
DR   ExpressionAtlas; C4JBI7; 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; 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   2: Evidence at transcript level;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01015};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
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}.
SQ   SEQUENCE   263 AA;  28266 MW;  D406AFB840D9CA6B CRC64;
     MASSPDLFPN VAFSDVSAAA PAAEATAAFG LGATTGAPRL CLVKSGKDEA EPTVDIDLAD
     AQVFKLGPME WLCVCDESEA KAGVEEKSFS RAIKVVLRTE AESKAFSLAF QQWKHQVISG
     KAGERLENGS IIASKSKFDT KIEASSAKMY FHYYGQLLHQ QNMLQDFVRT GTYYAAVMEN
     RSDFEGRVVV DVGAGSGILS LFAAQAGARH VYAVEASEMA ENAQRLMSGN PSLGQRITVI
     RGKVEEVELP EKADILISEP MGC
//
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