ID   ANM7_DROVI              Reviewed;         697 AA.
AC   B4LPB6;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-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=GJ20986;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87;
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; CH940648; EDW60225.1; -; Genomic_DNA.
DR   RefSeq; XP_002049032.2; XM_002048996.2.
DR   RefSeq; XP_015029517.1; XM_015174031.1.
DR   AlphaFoldDB; B4LPB6; -.
DR   SMR; B4LPB6; -.
DR   STRING; 7244.FBpp0235403; -.
DR   EnsemblMetazoa; FBtr0442993; FBpp0399429; FBgn0208121.
DR   GeneID; 6626596; -.
DR   KEGG; dvi:6626596; -.
DR   eggNOG; KOG1501; Eukaryota.
DR   HOGENOM; CLU_015180_0_0_1; -.
DR   InParanoid; B4LPB6; -.
DR   OMA; LPMANCA; -.
DR   OrthoDB; 408622at2759; -.
DR   PhylomeDB; B4LPB6; -.
DR   Proteomes; UP000008792; 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..697
FT                   /note="Protein arginine N-methyltransferase 7"
FT                   /id="PRO_0000373920"
FT   DOMAIN          14..357
FT                   /note="SAM-dependent MTase PRMT-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT   DOMAIN          366..697
FT                   /note="SAM-dependent MTase PRMT-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
SQ   SEQUENCE   697 AA;  79055 MW;  559F535E6C005572 CRC64;
     MASFSQVINP MTGQNTWQER GDDYDYHQEV ANAGFGDMLH DWERNQKYYA ALRKTIAAMR
     KAGKEVHALD IGTGTGILAM MALRAGADTV TACEAFMPMA NCAARILAAN DAAQVRLIRK
     RSTDIQMGID MPHRANLLVA ELLDTELIGE GAISIYNHAH QELLTDDALC IPARATCYAQ
     VAQSPLATQW NSLKVLPSLD GDILLRPPAQ LMECSGEAAL HDVQLSQLPP NSFHTLTEPA
     QIFQFDFQRK QPREQQREHV LRLQLSKPGS VELVFYWWQI ELDDAGEQLL SCAPYWAHPE
     LQQLQKSFKD ADRPLPNIVP WRDHWMQAIY YIPKPLQLHQ AGEQFWLRCY HDEYSLWFDA
     HKEQPEQPAR RHSCSCDLHL TYTRNRIGQL NQGTRNKRYL AYLEQAVQQA KPAHVLVIGD
     GCLLGLASSA LGACSVRCLE PHRFSRRLLE SVAKHNKLKN VRFLESLQQL EPEELNTLTH
     IFAEPYFLNA ILPWDNFYFG TLLLQLQQQQ KLSESVEISP CAARIYALPV QFLDLHKIRT
     PIISCEGFDL TLFDEMVQRS AKQALSQVEA QPLWEYPCRA LAEPQLLLSV NFANFGVEQH
     NQGCLELTAK GNCNGVALWV DWQLAANNSS KSIVSTGPLE PIVPGQFVKW DMFVRQGVHF
     PSQTDDQTHL KWSTTLRPLL GELTFNFSLQ ASHEETK