CARM1_DROSI
ID CARM1_DROSI Reviewed; 530 AA.
AC B4QVW6;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Histone-arginine methyltransferase CARMER {ECO:0000250|UniProtKB:Q7Q2B7};
DE EC=2.1.1.319 {ECO:0000250|UniProtKB:Q7Q2B7};
GN Name=Art4; ORFNames=GD20747;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1] {ECO:0000312|EMBL:EDX13546.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Methylates (mono- and asymmetric dimethylation) the guanidino
CC nitrogens of arginyl residues in proteins. May methylate histone H3 at
CC 'Arg-17' and activate transcription via chromatin remodeling (By
CC similarity). {ECO:0000250|UniProtKB:Q7Q2B7}.
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:0000250|UniProtKB:Q7Q2B7};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9VH48}. Nucleus
CC {ECO:0000250|UniProtKB:Q9VH48}.
CC -!- PTM: The dimethylated protein is the major form. {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; CM000364; EDX13546.1; -; Genomic_DNA.
DR RefSeq; XP_002104043.1; XM_002104007.2.
DR AlphaFoldDB; B4QVW6; -.
DR SMR; B4QVW6; -.
DR STRING; 7240.B4QVW6; -.
DR EnsemblMetazoa; FBtr0220657; FBpp0219149; FBgn0192213.
DR GeneID; 6728707; -.
DR HOGENOM; CLU_017375_0_1_1; -.
DR OMA; KWLKPQG; -.
DR PhylomeDB; B4QVW6; -.
DR Proteomes; UP000000304; Chromosome 3r.
DR Bgee; FBgn0192213; Expressed in embryo and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR GO; GO:0035097; C:histone methyltransferase complex; IEA:EnsemblMetazoa.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042054; F:histone methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0034969; P:histone arginine methylation; ISS:UniProtKB.
DR GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; ISS:UniProtKB.
DR GO; GO:0120142; P:positive regulation of ecdysone receptor-mediated signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblMetazoa.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR011993; PH-like_dom_sf.
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; Methylation; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..530
FT /note="Histone-arginine methyltransferase CARMER"
FT /id="PRO_0000382228"
FT DOMAIN 141..450
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT BINDING 154
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 187
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 209
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 238
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 266
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 501
FT /note="Asymmetric dimethylarginine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q7Q2B7"
SQ SEQUENCE 530 AA; 59685 MW; 449CCE09B98B6608 CRC64;
MSSLRPDEAR KLATAASVSP LSNCQFCGVV ISSIADEQKL EFTNKYKGSC TLLCSYDSQG
VVLRVVSDDD RSHVLKEYMI AADTDAAQMG RRSYAVSLDA DNLVLRFGSE QDQQLFRKVV
ENVKHLRPKS VFSQRTEESS ASQYFQFYGY LSQQQNMMQD YVRTSTYQRA ILGNAVDFQD
KIVLDVGAGS GILSFFAVQA GAAKVYAIEA SNMAQYAQQL VESNNVQHKI SVIPGKIEEI
ELPEKVDVII SEPMGYMLYN ERMLETYLHA RKWLKPQGKM YPTHGDLHIA PFSDESLYSE
QYNKANFWYQ SAFHGVDLTT LHKEGMKEYF RQPIVDTFDI RICMAKSVRH VCDFLNDKED
DLHLISIPLE FHILQTGICH GLAFWFDVEF SGSSQNVWLS TSPTAPLTHW YQVRCLLPMP
IFIKQGQTLT GRVLLEANRR QSYDVTIDLH IEGTLISSSN TLDLKNPYFR YTGAPVQAPP
GTSTQSPSEQ YWTQVDTQGS RNSSSMLNGG LSVNGIGDGM DITHGLMHPH
