CARM1_ANOGA
ID CARM1_ANOGA Reviewed; 622 AA.
AC Q7Q2B7; B7TWH1;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 5.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Histone-arginine methyltransferase CARMER {ECO:0000303|PubMed:19472346};
DE EC=2.1.1.319 {ECO:0000269|PubMed:19472346};
DE AltName: Full=Coactivator-associated arginine methyltransferase 1 {ECO:0000303|PubMed:19472346};
DE Short=AgCARM1 {ECO:0000303|PubMed:19472346};
GN Name=CARM1 {ECO:0000312|EMBL:ACJ24894.1}; ORFNames=AGAP003923;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP IDENTIFICATION BY MASS SPECTROMETRY, METHYLATION AT ARG-478, AND
RP MUTAGENESIS OF ARG-478.
RC STRAIN=G3 {ECO:0000269|PubMed:19472346};
RX PubMed=19472346; DOI=10.1002/pro.139;
RA Kuhn P., Xu Q., Cline E., Zhang D., Ge Y., Xu W.;
RT "Delineating Anopheles gambiae coactivator associated arginine
RT methyltransferase 1 automethylation using top-down high resolution tandem
RT mass spectrometry.";
RL Protein Sci. 18:1272-1280(2009).
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:0000269|PubMed:19472346}.
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:0000269|PubMed:19472346};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19472346}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9VH48}. Nucleus
CC {ECO:0000250|UniProtKB:Q9VH48}.
CC -!- PTM: The dimethylated protein is the major form.
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; AAAB01008978; EAA13615.4; -; Genomic_DNA.
DR EMBL; FJ391182; ACJ24894.1; -; mRNA.
DR RefSeq; XP_318375.4; XM_318375.4.
DR AlphaFoldDB; Q7Q2B7; -.
DR SMR; Q7Q2B7; -.
DR STRING; 7165.AGAP003923-PA; -.
DR iPTMnet; Q7Q2B7; -.
DR PaxDb; Q7Q2B7; -.
DR PRIDE; Q7Q2B7; -.
DR GeneID; 1278750; -.
DR KEGG; aga:AgaP_AGAP003923; -.
DR CTD; 1278750; -.
DR VEuPathDB; VectorBase:AGAP003923; -.
DR eggNOG; KOG1500; Eukaryota.
DR HOGENOM; CLU_017375_0_1_1; -.
DR InParanoid; Q7Q2B7; -.
DR OMA; VEFHMLE; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; Q7Q2B7; -.
DR Proteomes; UP000007062; Chromosome 2R.
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; IDA:UniProtKB.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0034969; P:histone arginine methylation; ISS:UniProtKB.
DR GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA: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 1: Evidence at protein level;
KW Chromatin regulator; Cytoplasm; Methylation; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..622
FT /note="Histone-arginine methyltransferase CARMER"
FT /id="PRO_0000382219"
FT DOMAIN 118..425
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 513..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 478
FT /note="Asymmetric dimethylarginine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:19472346"
FT MUTAGEN 478
FT /note="R->K: Destroys the dimethylation site."
FT /evidence="ECO:0000269|PubMed:19472346"
SQ SEQUENCE 622 AA; 68822 MW; F3519221E86C3355 CRC64;
MARMQGCSVL VLDDSDKLVN KYDHKVTVVC SYDPQGMAVR LLQEGATPPK QLEEYLVSGA
GTTHLSRGHT SHMLVVGGEL VLFRFASRGD CQQFRSLLHK LSGKVNSVFN LRTEDSSASQ
YFQFYGYLSQ QQNMMQDFVR TSTYQRAIYN NAQDFQNKIV LDVGAGSGIL SFFAVQAGAA
KVYAVEASNM AQYAQQLVSS NNLTDRIIVI AGKIEEIDLP ERVDVIISEP MGYMLYNERM
LETYLHGKKW LKPDGKMYPS RGDLHVAPFT DEALYMEQYN KANFWMQTEF HGVNLVALRD
AAMKEYFRQP IVDTFDIRIC MAKSIRHTTN FLTADEKDLH RIQIDVEFHM LETGTCHGLA
FWFDVEFAGT CSQIWLSTSP TEPLTHWYQV RCLLQTPIFV KQGQVLSGKV VLAANQRQSY
DVEIDLKLEG TMISSSNTLD LKNPYFRYTG APVAAPPGSN TTSPSEAFWS QLDAQGARNA
VNLVNGITVN GLGEVDMSST IINTNLMAIG GGANGGGPGG HQPNIHPGLI SSTGRQQQQQ
QQQQQQQAAV GPQQQQQQQS TTAQQLAMTP PIGCAATSTQ NVAQHQLIGG AISPSLFTSP
AQPILNSHHH HPGQPIHGNQ FY
