CARM1_DROMO
ID CARM1_DROMO Reviewed; 539 AA.
AC B4KA23;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=GI22087;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1] {ECO:0000312|EMBL:EDW16698.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22 {ECO:0000312|EMBL:EDW16698.1};
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; CH933806; EDW16698.1; -; Genomic_DNA.
DR RefSeq; XP_002001237.1; XM_002001201.2.
DR AlphaFoldDB; B4KA23; -.
DR SMR; B4KA23; -.
DR STRING; 7230.FBpp0171304; -.
DR EnsemblMetazoa; FBtr0172812; FBpp0171304; FBgn0144816.
DR GeneID; 6575223; -.
DR eggNOG; KOG1500; Eukaryota.
DR HOGENOM; CLU_017375_0_1_1; -.
DR InParanoid; B4KA23; -.
DR OMA; KWLKPQG; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; B4KA23; -.
DR Proteomes; UP000009192; 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..539
FT /note="Histone-arginine methyltransferase CARMER"
FT /id="PRO_0000382224"
FT DOMAIN 149..458
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT BINDING 162
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 171
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 195
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 217
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 246
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 274
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 509
FT /note="Asymmetric dimethylarginine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q7Q2B7"
SQ SEQUENCE 539 AA; 60750 MW; DEDD7554348A7EB3 CRC64;
MSTTSSSGRI AADQNNKCVN SVAAALCPLS NCQFSGVVIS AITDEQKLEF SNKYNSSCTL
SCSYDSQGVL LRIMLDNDQG HVLKEYMISA DTDAAQLGRR CYAISLESDN LVLRFVSDKD
QQLFRKVVEN VKHLRPKSVF SQRTEESSAS QYFQFYGYLS QQQNMMQDYV RTSTYQRAIL
GNAIDFQDKV VLDVGAGSGI LSFFAVQAGA AKVYAIEASN MAQYAQQLVE SNNVQHKISV
IPGKIEEIEL PEKVDVIISE PMGYMLYNER MLETYLHARK WLKPHGKMYP THGDLHIAPF
SDESLYSEQY NKANFWYQSA FHGVDLTTLH KEGMKEYFRQ PIVDTFDIRI CMAKSVRHVC
DFLNDKEDDL HVIDIPLEFH ILQTGICHGL AFWFDVEFSG SSQNVWLSTS PTAPLTHWYQ
VRCLLPMPIF IKQGQTLTGR VLLEANRRQS YDVTIDLHIE GTLISSSNTL DLKNPYFRYT
GAPVQAPPGT NTQSPSEQYW TQMDTQGNRN SNSMLNGTLS VNGMGDGSMD ITHGLLHPH
