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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
