ID   ANM7_DROSI              Reviewed;         705 AA.
AC   B4QI55;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Protein arginine N-methyltransferase 7;
DE            EC=2.1.1.-;
GN   Name=Art7; ORFNames=GD25084;
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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: 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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Protein arginine N-methyltransferase family. PRMT7
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01015}.
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DR   EMBL; CM000362; EDX08309.1; -; Genomic_DNA.
DR   RefSeq; XP_002082724.1; XM_002082688.2.
DR   AlphaFoldDB; B4QI55; -.
DR   SMR; B4QI55; -.
DR   STRING; 7240.B4QI55; -.
DR   EnsemblMetazoa; FBtr0224994; FBpp0223486; FBgn0196396.
DR   GeneID; 6735814; -.
DR   HOGENOM; CLU_015180_0_0_1; -.
DR   OMA; LPMANCA; -.
DR   PhylomeDB; B4QI55; -.
DR   Proteomes; UP000000304; Chromosome 2r.
DR   Bgee; FBgn0196396; Expressed in male reproductive system and 3 other tissues.
DR   GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0018216; P:peptidyl-arginine methylation; ISS:UniProtKB.
DR   GO; GO:0035247; P:peptidyl-arginine omega-N-methylation; IEA:UniProt.
DR   Gene3D; 3.40.50.150; -; 2.
DR   InterPro; IPR025799; Arg_MeTrfase.
DR   InterPro; IPR014644; MeTrfase_PRMT7.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11006; PTHR11006; 1.
DR   PIRSF; PIRSF036946; Arg_N-mtase; 1.
DR   SUPFAM; SSF53335; SSF53335; 2.
DR   PROSITE; PS51678; SAM_MT_PRMT; 2.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; Repeat; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..705
FT                   /note="Protein arginine N-methyltransferase 7"
FT                   /id="PRO_0000373919"
FT   DOMAIN          29..372
FT                   /note="SAM-dependent MTase PRMT-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT   DOMAIN          381..705
FT                   /note="SAM-dependent MTase PRMT-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
SQ   SEQUENCE   705 AA;  79508 MW;  6893F740F3DAFBA8 CRC64;
     MLRNFLKSRF LAPRGMSCFS QVMNPITGQN SWQERGDDYD YHLEVANAGF GDMLHDWERN
     QKYFAALRKT IAGMREAGRE VHVLDIGTGT GILSMMALAA GADSVTACEA FLPMANCAEK
     ILAANGAGDK VRLIRKRSTE IQVGEDMPRK ANLLVAELLD TELIGEGAIG IYNHAHAELL
     TEDALCIPAR ARCYAQVAQS PLAAQWNSLK TIANLDGEPL LHPPEQLKSC QGEAALHDVQ
     LSQLPSSAFR PLTDPVEIFQ FDFQRKQERE KQRAQLLKLQ SKQPGAAELV FYWWDIQLDD
     GGEILLSCAP YWAHPQLKEL AAEKAKDHPL PNVVPWRDHW MQAIYYIPKP LQLLEAGKSF
     HLSCHHDEYS LWFDAREEAP TKSVRRHTCT CDLHMTYSRS RIGQLNQSPR NKRYLRYLEE
     SIEAEKSNVL VLGNGCLLGL ASSALGAASV LLHEPHRFSR RLLESIVKHN QLKNVHFLDK
     VEELEDSQLA ALTHIFAEPY FLNAILPWDN FYFGTLLTKI KDKLPEGVKI LPCSARIYAL
     PVEFLDLHKI RAPVGSCEGF DLRLFDEMVE RSAEQAVSLV EAQPLWEYPC RALSEPQEVL
     SVDFSNFGQE HSLKGSIELK HTGICNGVAL WVDWKLVEDN SPRSIVSSGP SEPVVPGEFV
     KWDMFVRQGV HFPRKPKDAV THLEWSTDFK PLLGELNFSF GQKKL