ID   ANM7_DROGR              Reviewed;         704 AA.
AC   B4JWL5;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Protein arginine N-methyltransferase 7;
DE            EC=2.1.1.-;
GN   Name=Art7; ORFNames=GH23070;
OS   Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Hawaiian Drosophila.
OX   NCBI_TaxID=7222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15287-2541.00;
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; CH916375; EDV98353.1; -; Genomic_DNA.
DR   RefSeq; XP_001995281.1; XM_001995245.1.
DR   AlphaFoldDB; B4JWL5; -.
DR   SMR; B4JWL5; -.
DR   STRING; 7222.FBpp0156976; -.
DR   EnsemblMetazoa; FBtr0460746; FBpp0411166; FBgn0130527.
DR   GeneID; 6569154; -.
DR   KEGG; dgr:6569154; -.
DR   eggNOG; KOG1501; Eukaryota.
DR   HOGENOM; CLU_015180_0_0_1; -.
DR   InParanoid; B4JWL5; -.
DR   OMA; LPMANCA; -.
DR   OrthoDB; 408622at2759; -.
DR   PhylomeDB; B4JWL5; -.
DR   Proteomes; UP000001070; 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..704
FT                   /note="Protein arginine N-methyltransferase 7"
FT                   /id="PRO_0000373913"
FT   DOMAIN          14..356
FT                   /note="SAM-dependent MTase PRMT-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT   DOMAIN          366..704
FT                   /note="SAM-dependent MTase PRMT-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
SQ   SEQUENCE   704 AA;  79440 MW;  88BF9B3BB437BDE0 CRC64;
     MASFGQVINP MTGENTWQER DENYDYHQEV ANAGFGDMLH DWERNQKYDA ALRKTIAAMR
     EAGREVHVLD IGTGTGILAM MALRAGADTV TACEAFMPMA NCAQRILNAN GYGDRVRLIR
     KRSTDIEMGV DMPHRANLLV AELLDTELIG EGAIGIYNHA HNELLTADAL CIPARATCYA
     QAAQSALATQ WNSLKMLASL DGDILLKPPA QLLQCSGEAA LHDVQLSQLP IDSFHVLTAP
     TPIFQFDFQR KQAREQQREN ILRLQIVRPG SVELIFYWWQ IELDDRGEQL LSCAPYWAHP
     ELAQLQRSNS SKPLANVVPW RDHWMQAIYY IPKPLQLHTA GEQFYLRCYH DEYSLWFDAH
     QTEPPSQPAR RHCCTCDLHM TYTRNRIGQL NQGTRNKRYL RYLEQAVHAK ESAHLLVLGD
     GCLLGLASSA LGAGSVRCLE PHRFSRRLLG AIAKHNQLKN VSFVESVQQL QPIELAAITH
     IFAEPYFLNS ILPWDNFYFG TLLLQLLEQI PALSVQISPC AARIYALPVE FLDLHKIRTP
     IGSCEGFDLR LFDDMVQRSA EQAVALVEAQ PLWEYPCRAL AQPQQLLNVN FDNFGEDKHS
     HGCLQLTASG DCNGVALWVD WQLAADESPR SIVSSGPSET VVPGQLVKWD MFVRQGVHFI
     SQPTKDRRQT DAGKRQLDWS INFKPRLGEL NFNFSLRSSS EKSE