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CARM1_DROVI
ID   CARM1_DROVI             Reviewed;         538 AA.
AC   B4LVS8;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=GJ24202;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1] {ECO:0000312|EMBL:EDW67533.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87 {ECO:0000312|EMBL:EDW67533.1};
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; CH940650; EDW67533.1; -; Genomic_DNA.
DR   RefSeq; XP_002054013.1; XM_002053977.2.
DR   AlphaFoldDB; B4LVS8; -.
DR   SMR; B4LVS8; -.
DR   STRING; 7244.FBpp0238619; -.
DR   EnsemblMetazoa; FBtr0240127; FBpp0238619; FBgn0211285.
DR   GeneID; 6630512; -.
DR   KEGG; dvi:6630512; -.
DR   eggNOG; KOG1500; Eukaryota.
DR   HOGENOM; CLU_017375_0_1_1; -.
DR   InParanoid; B4LVS8; -.
DR   OMA; KWLKPQG; -.
DR   OrthoDB; 840669at2759; -.
DR   PhylomeDB; B4LVS8; -.
DR   Proteomes; UP000008792; Unassembled WGS sequence.
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..538
FT                   /note="Histone-arginine methyltransferase CARMER"
FT                   /id="PRO_0000382229"
FT   DOMAIN          148..457
FT                   /note="SAM-dependent MTase PRMT-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT   BINDING         161
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q63009"
FT   BINDING         170
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q63009"
FT   BINDING         194
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q63009"
FT   BINDING         216
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q63009"
FT   BINDING         245
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q63009"
FT   BINDING         273
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         508
FT                   /note="Asymmetric dimethylarginine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Q2B7"
SQ   SEQUENCE   538 AA;  60666 MW;  8C304786F57C2986 CRC64;
     MSTSSSSRIA IEQNNKCVNS VAAALCPLSN CQFSGVVISA ISDEQKLEFN SIYKSSCTLS
     CSYDSQGVLL RIMLDNDQGH VLKEYMISAD TDAAQLGRRC YAVSLESDNL VLRFGSDKDQ
     QLFRKVVENV KHLRPKSVFS QRTEESSASQ YFQFYGYLSQ QQNMMQDYVR TSTYQRAILG
     NSIDFQDKIV LDVGAGSGIL SFFAVQAGAA KVYAIEASNM AQYAQQLVES NNVQHKISVI
     PGKIEEIELP EKVDVIISEP MGYMLYNERM LETYLHARKW LKPHGKMYPT HGDLHIAPFS
     DESLYSEQYN KANFWYQSAF HGVDLTTLHK EGMKEYFRQP IVDTFDIRIC MAKSVRHVCD
     FLNDKEDDLH VIDIPLEFHI LQTGICHGLA FWFDVEFSGS SQNVWLSTSP TAPLTHWYQV
     RCLLPMPIFI KQGQTLTGRV LLEANRRQSY DVTIDLHIEG TLISSSNTLD LKNPYFRYTG
     APVQAPPGTN TQSPSEQYWT QMDTQGNRNS NSMLNGALTV NGMGDGGMDI THGLMHPH
 
 
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