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ANM7_DROPE
ID   ANM7_DROPE              Reviewed;         692 AA.
AC   B4GA28;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Protein arginine N-methyltransferase 7;
DE            EC=2.1.1.-;
GN   Name=Art7; ORFNames=GL11301;
OS   Drosophila persimilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSH-3 / Tucson 14011-0111.49;
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; CH479181; EDW31780.1; -; Genomic_DNA.
DR   RefSeq; XP_002015890.1; XM_002015854.1.
DR   AlphaFoldDB; B4GA28; -.
DR   SMR; B4GA28; -.
DR   STRING; 7234.FBpp0175408; -.
DR   EnsemblMetazoa; FBtr0176916; FBpp0175408; FBgn0148910.
DR   GeneID; 6590260; -.
DR   KEGG; dpe:6590260; -.
DR   eggNOG; KOG1501; Eukaryota.
DR   HOGENOM; CLU_015180_0_0_1; -.
DR   OMA; LPMANCA; -.
DR   PhylomeDB; B4GA28; -.
DR   Proteomes; UP000008744; 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..692
FT                   /note="Protein arginine N-methyltransferase 7"
FT                   /id="PRO_0000373916"
FT   DOMAIN          14..359
FT                   /note="SAM-dependent MTase PRMT-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT   DOMAIN          368..692
FT                   /note="SAM-dependent MTase PRMT-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
SQ   SEQUENCE   692 AA;  78064 MW;  1A8C6E96DA470E71 CRC64;
     MSCFSHVMNP ITGENSWQER EDDYDYHQEV ANAGFGDMLH DWERNQKYFA ALRKTIKGMR
     AAGREVHVLD IGTGTGILSM MALKAGADSV TACEAFLPMA NCAAKIFTDN GVGDKVQLIR
     KRSTDIKIGA DLDMPQRANL LVAELLDTEL IGEGAISIYN HAHAELLTDD ALCIPARARC
     YAQVAQSPLA SQWNSLKILP SLDGEALLRP PEQLKSCKGE AALHDVQLSQ LPAGTFRLLT
     EPIEIFQLDF QRKEKREKQR EKLVQLQASQ PGAAELVFYW WDIQLDDQGE ILLSCAPYWA
     HPELNELSAS KEERVPVANV VPWRDHWMQA IYYVPKPPQL ATAGQDFYLS CHHDEYSLWF
     DAMLEAPAKT VRRHTCSCDL HMTYSRSRIG QLNQAIRNKR YLRYLEATIV PKQSNVLVLG
     NGCMLGLASA ALGAASVQLH EPHRFSRRLI DSIVQHNELK NVKYVENVEQ LEDTELIALS
     HVFAEPYFLN AILPWDNFYF GTLLMKLKDK LPEKVEISPC EARIFALPVE FLDLHKIRAP
     VGSCEGFDLR LFDEMVERSA EQAVSLVEAQ PLWEYPSRAL AEPQQLLSVD FANFNVEHHL
     QGSIELTQSG VCNGIALWVD WHLDKTNNPK SIVSTGPSEA VVPGEFVKWD MFVRQGVHFP
     RKPTDLSGRV AWSTDFKPLL GQLNFGFSQE KR
 
 
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