ID   ANM7_DROWI              Reviewed;         685 AA.
AC   B4MNL1;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Protein arginine N-methyltransferase 7;
DE            EC=2.1.1.-;
GN   Name=Art7; ORFNames=GK19600;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24;
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; CH963848; EDW73700.1; -; Genomic_DNA.
DR   RefSeq; XP_002062714.2; XM_002062678.2.
DR   AlphaFoldDB; B4MNL1; -.
DR   SMR; B4MNL1; -.
DR   STRING; 7260.FBpp0248743; -.
DR   PRIDE; B4MNL1; -.
DR   EnsemblMetazoa; FBtr0250251; FBpp0248743; FBgn0221598.
DR   GeneID; 6639894; -.
DR   KEGG; dwi:6639894; -.
DR   eggNOG; KOG1501; Eukaryota.
DR   HOGENOM; CLU_015180_0_0_1; -.
DR   InParanoid; B4MNL1; -.
DR   OMA; LPMANCA; -.
DR   OrthoDB; 408622at2759; -.
DR   PhylomeDB; B4MNL1; -.
DR   Proteomes; UP000007798; 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..685
FT                   /note="Protein arginine N-methyltransferase 7"
FT                   /id="PRO_0000373921"
FT   DOMAIN          14..355
FT                   /note="SAM-dependent MTase PRMT-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT   DOMAIN          364..685
FT                   /note="SAM-dependent MTase PRMT-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
SQ   SEQUENCE   685 AA;  77744 MW;  7BD2ACDFB57A2ABB CRC64;
     MSSFSQVRNP ITGQATWQEN ADDYDYHQEV ANAGFGDMLH DWERNQKYYA AIKKTIKRMQ
     ADGREVHVLD IGTGTGILSM MALKAGADSV TACEAFLPMA NCAAKIMTAN GADKIQLIRK
     RSTEIQIGVD MARRANLLVA ELLDTELIGE GAIGIYNHAH QELLTKDALC IPARARCYAQ
     VATSSLAKQW NGFKLMANLD GETLLRVPPQ LNECKGDAAL HDLQLSQLPT ESFRLFSKPV
     EIFEFDFQQH LEPIQKQRNK VVPLQASQPG SADMVFYWWD IDLDHESEIV LSCAPFWAHP
     DKDKHVAGED KPLANAIPWR DHWMQAIYYI PKPLHLSNTK ETFYLSCHHD EYSLWFDAQL
     KEPAESIERH HCTCDLHLIN PRSRIGQLNQ SPRNKRYLNY LEETTTKDSQ FLVLGNSCFL
     GLATCGLGAA SVEIYDSNSL SRRLLDSFIK FNKLENVSLL EKLEDVQDHS KLTHIFAEPY
     FINSILPWDN FYFGTLLLSL KDKLSEGTQI SPCAARIFAL PMEFLDLHKI RAPVGNCEGF
     DLSLFDEMVK DSADKAVSSV EAQPLWEYPG RALAQPQEIL RVDFANFNQE LHQQGSIELI
     RSKECNGIAL WVDWQLYSSE SPKAFVTSGP SQPIEIGKFV KWDMFVRQGV HFPQTRTTNA
     TQVEWQIDFK PFLGELNFKF DLKSI