CARM1_AEDAE
ID CARM1_AEDAE Reviewed; 593 AA.
AC Q174R2;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Histone-arginine methyltransferase CARMER {ECO:0000250|UniProtKB:Q7Q2B7};
DE EC=2.1.1.319 {ECO:0000250|UniProtKB:Q7Q2B7};
GN Name=CARM1 {ECO:0000250|UniProtKB:Q7Q2B7}; ORFNames=AAEL006782;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1] {ECO:0000312|EMBL:EAT41589.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(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.
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|UniProtKB:Q7Q2B7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9VH48}. Nucleus
CC {ECO:0000250|UniProtKB:Q9VH48}.
CC -!- PTM: The dimethylated protein is the major form.
CC {ECO:0000250|UniProtKB:Q7Q2B7}.
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; CH477406; EAT41589.1; -; Genomic_DNA.
DR RefSeq; XP_001652238.1; XM_001652188.1.
DR AlphaFoldDB; Q174R2; -.
DR SMR; Q174R2; -.
DR STRING; 7159.AAEL006782-PA; -.
DR GeneID; 5579949; -.
DR KEGG; aag:5579949; -.
DR VEuPathDB; VectorBase:AAEL006782; -.
DR eggNOG; KOG1500; Eukaryota.
DR HOGENOM; CLU_017375_0_1_1; -.
DR InParanoid; Q174R2; -.
DR OMA; KWLKPQG; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; Q174R2; -.
DR Proteomes; UP000008820; Unassembled 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..593
FT /note="Histone-arginine methyltransferase CARMER"
FT /id="PRO_0000399501"
FT DOMAIN 122..429
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 521..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 168
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 190
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 219
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 247
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 482
FT /note="Asymmetric dimethylarginine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q7Q2B7"
SQ SEQUENCE 593 AA; 66391 MW; 3D1808826925D12C CRC64;
MFENQQQLLR LHGCKLFIIG ENDNLVNKYG HSVAIACCYD PQGMSVRVFR EGSQQQLEEY
PVSVKTTHLN HGITSHILIV GGEMIYVKFA SEEDCQSFRM LLQNMSGKVN SVFNLRTEDS
SASQYFQFYG YLSQQQNMMQ DFVRTSTYQR AIYSNSQDFH NKIVLDVGAG SGILSFFAVQ
AGAAKVYAVE ASNMAQYAQQ LVLSNNLDGK IIVIAGKIEE IELPEMVDII ISEPMGYMLY
NERMLETYLH GKKWLRPEGK MFPSRGDLHV APFTDEALYM EQYNKANFWM QTEFHGVNLV
ALRDAAMKEY FRQPIVDTFD IRICMAKSIR HTTNFLTADE KDLHRIQIDV EFHILETGTC
HGLAFWFDVE FAGSCSQVWL STAPTESLTH WYQVRCLLQT PIFVKQGQVL SGKVVLAANQ
RQSYDVEMDL KLEGTMITST NTLDLKNPYF RYTGAPVPAP PGSNTTSPSE AYWGQLDAQG
ARNAVNLVNG ITVNGLGEVD MTMINTNLMP IGNQPNIHPG LISSTGRQQS QQQTTPAQPL
TMNPTIACAA TSTQNVAQQQ LIGGAISPSL FTTPTQQIIN SHHAQPIHGA QFY
