ID   A0A182UXJ6_ANOME        Unreviewed;       690 AA.
AC   A0A182UXJ6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Protein arginine N-methyltransferase {ECO:0000256|PIRNR:PIRNR036946};
DE            EC=2.1.1.- {ECO:0000256|PIRNR:PIRNR036946};
OS   Anopheles merus (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=30066 {ECO:0000313|EnsemblMetazoa:AMEM005368-PA, ECO:0000313|Proteomes:UP000075903};
RN   [1] {ECO:0000313|Proteomes:UP000075903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAF {ECO:0000313|Proteomes:UP000075903};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles merus MAF (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMEM005368-PA}
RP   IDENTIFICATION.
RC   STRAIN=MAF {ECO:0000313|EnsemblMetazoa:AMEM005368-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- FUNCTION: Arginine methyltransferase that can both catalyze the
CC       formation of omega-N monomethylarginine (MMA) and symmetrical
CC       dimethylarginine (sDMA). {ECO:0000256|PIRNR:PIRNR036946}.
CC   -!- FUNCTION: Essential arginine methyltransferase that can both catalyze
CC       the formation of omega-N monomethylarginine (MMA) and symmetrical
CC       dimethylarginine (sDMA). Specifically mediates the symmetrical
CC       dimethylation of arginine residues in the small nuclear
CC       ribonucleoproteins SmD1 and SmD3. {ECO:0000256|ARBA:ARBA00025081}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Protein arginine N-methyltransferase family. PRMT7
CC       subfamily. {ECO:0000256|PIRNR:PIRNR036946}.
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DR   AlphaFoldDB; A0A182UXJ6; -.
DR   STRING; 30066.A0A182UXJ6; -.
DR   EnsemblMetazoa; AMEM005368-RA; AMEM005368-PA; AMEM005368.
DR   VEuPathDB; VectorBase:AMEM005368; -.
DR   VEuPathDB; VectorBase:AMEM21_015101; -.
DR   Proteomes; UP000075903; Unassembled WGS sequence.
DR   GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 2.70.160.11; Hnrnp arginine n-methyltransferase1; 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR   InterPro; IPR025799; Arg_MeTrfase.
DR   InterPro; IPR014644; MeTrfase_PRMT7.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11006; PROTEIN ARGININE N-METHYLTRANSFERASE; 1.
DR   Pfam; PF06325; PrmA; 1.
DR   PIRSF; PIRSF036946; Arg_N-mtase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR   PROSITE; PS51678; SAM_MT_PRMT; 2.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01015};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01015};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU01015}.
SQ   SEQUENCE   690 AA;  77721 MW;  B41C7C3BBB720128 CRC64;
     MEDTFQDSAS EDGGFDLRQE IARSAFADMC HDWERNQKYD RALQLTIARL HAAGHQAHVL
     DIGTGSGLLS MMAIRAGADS VVACEAFRPM ADCAERIIAA NGMQDRIRLV KKRSTKVTVG
     PGQDMERRAN VLVTELFDTE LIGEGALGTY RHALQHLLTE DVLTIPHQAT VYAQVVECPL
     ALSWQQLKTL SNADGDILLR VPPEVATCRG SSAVFDIQLS QLPAGSFNVL TDPVPVFKFA
     WSKHQELIND RCEQSVCHAR TAGFPQAVFM WWDLTMDCEG DVLLSCAPYW AHPEHEALKK
     KHSDNGSKRR LPEGNYIPWR DHWMQAVYFL PPLKIPLQRG QQFVLQSYHD EFSLWFGVGE
     QSVKDPLTAP HCTCGWHIAQ SRSRIGQLND SLRNKRYLNY FERVFSSDSV VLVLSEGSLL
     GLAAARMGVK QVLLYEPNAI SRRCMEAFVE HNSVVNVRFL PSADALEPEQ AVTITHVFAE
     PHFPSAILPW DNLHYGDLLK NLRPLLPANV TVIPASGTLY ALPVEFVDLY KINAPLGSCE
     GFDLTLMDQL IDQHSTFADS PVEAQPLWEY PSFPLAGTTR LIEINFVQDF EQSKLERGEL
     FVSEAERLNG IAIWIDWHLD GSHSPKTTIS SGPLVPVEES SDEPTRWNTN WRQGVHLLRK
     TPNRKRTIPW SVKFNPVLSN VYFRFDEEEQ
//