CARM1_ORYSI
ID CARM1_ORYSI Reviewed; 528 AA.
AC A2YPT7; B8B5U5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Probable histone-arginine methyltransferase CARM1;
DE EC=2.1.1.319;
DE AltName: Full=Protein arginine N-methyltransferase 4;
GN Name=CARM1; Synonyms=PRMT4; ORFNames=OsI_27289;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: Methylates (mono- and asymmetric dimethylation) the guanidino
CC nitrogens of arginyl residues in several proteins involved in DNA
CC packaging, transcription regulation, and mRNA stability. Recruited to
CC promoters upon gene activation, methylates histone H3 and activates
CC transcription via chromatin remodeling. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01015}.
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DR EMBL; CM000132; EEC82664.1; -; Genomic_DNA.
DR AlphaFoldDB; A2YPT7; -.
DR SMR; A2YPT7; -.
DR STRING; 39946.A2YPT7; -.
DR EnsemblPlants; BGIOSGA026368-TA; BGIOSGA026368-PA; BGIOSGA026368.
DR Gramene; BGIOSGA026368-TA; BGIOSGA026368-PA; BGIOSGA026368.
DR HOGENOM; CLU_017375_0_2_1; -.
DR OMA; KWLKPQG; -.
DR Proteomes; UP000007015; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042054; F:histone methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0034969; P:histone arginine methylation; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Cytoplasm; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..528
FT /note="Probable histone-arginine methyltransferase CARM1"
FT /id="PRO_0000294006"
FT DOMAIN 149..464
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 500..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 166
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 528 AA; 58580 MW; 06043252B82901AD CRC64;
MASPDLFPNV SFSHVSVPAA AGASTEVTGG ATAVFGGDAS TGAPRLSLVW SGETQAKHTL
EIDLSDAQIF KLGPTEWLCV SGESEAKDGV EEKSYSRAIK VVLRTEAESK AFYLAFQQWK
HRVISGKAGE PLENGLIIGS KSKFDTKIEA SSAKMYFHYY GQLLHQQNML QDFVRTGTYY
AAVMENRSDF EGRVVVDVGA GSGILSLFAA QAGARHVYAV EASEMAEHAQ RLISGNPSLG
QRITVIKGKV EEVELPEKAD ILISEPMGTL LVNERMLESY VIARDRFLVP GGKMFPTTGR
IHMAPFSDEY LYVEMANKAL FWQQHNFFGV DLTPLHGSAF QGYFSQPVVD AFDPRLLVSP
PTFHTLDFTT MKEEELYEID IPLNFVASVG TRVHGLACWF DVLFNGSTVQ RWLTTAPGSP
TTHWYQLRCI LSQPLYVMAG QEITGRLHLV AHSAQSYTIY LTMSAKMWGE GAEQGGILQT
STAKLELKEP YYRLSQPQPY VMQQDQQQQQ LPSLQPQSPL WDYHYGQD
