CARM1_CULQU
ID CARM1_CULQU Reviewed; 599 AA.
AC B0W3L6;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=CPIJ001402;
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000312|EMBL:EDS31802.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000312|EMBL:EDS31802.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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.
CC {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; DS231832; EDS31802.1; -; Genomic_DNA.
DR RefSeq; XP_001843300.1; XM_001843248.1.
DR AlphaFoldDB; B0W3L6; -.
DR SMR; B0W3L6; -.
DR STRING; 7176.CPIJ001402-PA; -.
DR EnsemblMetazoa; XM_001843248.2; XP_001843300.1; LOC6032759.
DR GeneID; 6032759; -.
DR KEGG; cqu:CpipJ_CPIJ001402; -.
DR VEuPathDB; VectorBase:CPIJ001402; -.
DR VEuPathDB; VectorBase:CQUJHB011210; -.
DR eggNOG; KOG1500; Eukaryota.
DR HOGENOM; CLU_017375_0_1_1; -.
DR InParanoid; B0W3L6; -.
DR OMA; VEFHMLE; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; B0W3L6; -.
DR Proteomes; UP000002320; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0006355; P:regulation of transcription, DNA-templated; 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; Methylation; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..599
FT /note="Histone-arginine methyltransferase CARMER"
FT /id="PRO_0000382220"
FT DOMAIN 127..434
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT BINDING 140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 149
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 173
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 224
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 252
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 487
FT /note="Asymmetric dimethylarginine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q7Q2B7"
SQ SEQUENCE 599 AA; 66118 MW; 43F875A3AD7B2FF8 CRC64;
MCEQLARLHG CNILIIGDND CLVNKYGHSV TIACGYDPQG MSVRILKEGG GGGGGGGGGQ
QLEEYPVNAK TTHLNHGHTS HVVVAGGEML YLKFASKADC QLFRSLLQKM SGKVNSVFNL
RTEDSSASQY FQFYGYLSQQ QNMMQDFVRT STYQRAIYSN SQDFHNKIVL DVGAGSGILS
FFAVQAGAAK VYAVEASNMA QYAQQLVHSN NLNGKITVIA GKIEEIELPE MVDVIISEPM
GYMLYNERML ETYLHGKKWL KPEGKMFPSR GDLHVAPFTD EALYMEQYNK ANFWMQSEFH
GVNLVSLRDA AMKEYFRQPI VDTFDIRICM AKSIRHTTNF LTADEKDLHR IQIDVEFHIL
ETGTCHGLAF WFDVEFAGSC SQIWLSTAPT ESLTHWYQVR CLLQTPIFVK QGQVLSGKVV
LAANQRQSYD VEIDLKLEGT MITSCNTLDL KNPYFRYTGA PVPAPPGSNT TSPSEAYWGQ
LDAQGARNAV NLVNGITVNG LGEVDMSIIN SNMMPMGNQP NIHPGLISST GRQQSAQQQV
TPSQQLTMNP TIACAATSTQ NVAQQQLIGG AISPSLFTTP TQQIINSHHA QPIHGGQFY
