ID   ANM7_DROAN              Reviewed;         690 AA.
AC   B3MF31;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Protein arginine N-methyltransferase 7;
DE            EC=2.1.1.-;
GN   Name=Art7; ORFNames=GF11303;
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13;
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; CH902619; EDV37659.1; -; Genomic_DNA.
DR   RefSeq; XP_001960837.2; XM_001960801.2.
DR   AlphaFoldDB; B3MF31; -.
DR   SMR; B3MF31; -.
DR   STRING; 7217.FBpp0114495; -.
DR   EnsemblMetazoa; FBtr0116003; FBpp0114495; FBgn0088343.
DR   GeneID; 6494167; -.
DR   KEGG; dan:6494167; -.
DR   eggNOG; KOG1501; Eukaryota.
DR   HOGENOM; CLU_015180_0_0_1; -.
DR   InParanoid; B3MF31; -.
DR   OMA; LPMANCA; -.
DR   OrthoDB; 408622at2759; -.
DR   PhylomeDB; B3MF31; -.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
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..690
FT                   /note="Protein arginine N-methyltransferase 7"
FT                   /id="PRO_0000373911"
FT   DOMAIN          14..357
FT                   /note="SAM-dependent MTase PRMT-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT   DOMAIN          366..690
FT                   /note="SAM-dependent MTase PRMT-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
SQ   SEQUENCE   690 AA;  77860 MW;  E70B48D6422D9296 CRC64;
     MSCFSQVLNP ITGENSWQER EDDYDYHQEV ANAGFGDMLH DWERNQKYFA ALRKTIAEMR
     TAGKEVHVLD IGTGTGILSM MALEAGADSV TACEAFLPMA NCAEKILAAN GAADKVRLIR
     KRSTDIQIGE DMPRKANLLV AELLDTELIG EGAIGIYNHA HDELLTEDAL CIPARARCYA
     QVAQSPLAAQ WNSLKSLANL DGEPLLQPPA QLKGCKGEAG LHDVQLSQLP SHTFRPLTDP
     VEIFQFDFQR KKQREKKRDQ LLKVQSNQPG SAELVFYWWD IQLDDGGEIL LSCAPYWAHP
     EIHELSGKKG KDLPLPNVVP WRDHWMQAIY YIPKPLQLLE AGKSFHLSCH HDEYSLWFDA
     REEAPAKSVS RHTCTCDLHM TYSRSRIGQM NQSTRNKRYL RYLEENIEAE KSKVLVLGNG
     CLLGLASSAL GATSVQLHEP HRFSRRLLES IVQHNQLKNV EFVDKVEEVE DSQLAGLTHV
     FAEPYFLNAI LPWDNFYFGT LLAKIKDKLP EDVKISPCSA RIYALPVEFL DLHKIRAPVV
     SCEGFDLRLF DEMVERSAEQ AVTLVEAQPL WEYPCRALSE PQEILNVDFN KFSEEHHLKG
     TIDLKHPGTC NGVALWVDWQ LINDSSPRSI VSTGPSEAVT PGEFVKWDMF VRQGVHFPQK
     TNQTISSLAW STDFKPLLGQ LSFTFGQKKP