ANM7_DROSE
ID ANM7_DROSE Reviewed; 690 AA.
AC B4I8G2;
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=GM15586;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25;
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; CH480824; EDW56887.1; -; Genomic_DNA.
DR RefSeq; XP_002040022.1; XM_002039986.1.
DR AlphaFoldDB; B4I8G2; -.
DR SMR; B4I8G2; -.
DR STRING; 7238.B4I8G2; -.
DR EnsemblMetazoa; FBtr0198571; FBpp0197063; FBgn0170504.
DR GeneID; 6615651; -.
DR KEGG; dse:6615651; -.
DR HOGENOM; CLU_015180_0_0_1; -.
DR OMA; LPMANCA; -.
DR PhylomeDB; B4I8G2; -.
DR Proteomes; UP000001292; 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..690
FT /note="Protein arginine N-methyltransferase 7"
FT /id="PRO_0000373918"
FT DOMAIN 14..357
FT /note="SAM-dependent MTase PRMT-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT DOMAIN 366..690
FT /note="SAM-dependent MTase PRMT-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
SQ SEQUENCE 690 AA; 77755 MW; B2B0FA53588D481F CRC64;
MSCFLQVMNP ITGQNSWQER GDDYDYHLEV ANAGFGDMLH DWERNQKYFG ALRKTIAGMR
EAGREVHVLD IGTGTGILSM MALAAGADSV TACEAFLPMA NCAEKILAAN GAGDKVRLIR
KRSTEIQVGE DMPRKANLLV AELLDTELIG EGAIGIYNHA HAELLTEDAL CIPARARCYA
QVAQSPLAAQ WNSLKTIANL DGEPLLHPPE QLKSCQGEAA LHDVQLSQLP ISAFRPLTDP
VEIFQFDFQR KQEREKQRAQ LLKLQSKQPG AAELVFYWWD IQLDDGGEIL LSCAPYWAHP
QLKELAAEKA KDHPLPNVVP WRDHWMQAIY YIPKPLQLLE AGKSFHLSCH HDEYSLWFDA
REEAPTKSVR RHTCTCDLHM TYSRGRIGQL NQSPRNKRYL RYLEESIEAE KSNVLVLGNG
CLLGLASSAL GAASVLLHEP HRFSRRLLES IVKHNQLKNV QFLDKVEELE DSQLAALTHI
FAEPYFLNAI LPWDNFYFGS LLTKIKDRLP EGVKISPCSA RIYALPVEFL DLHKIRAPVG
SCEGFDLRLF DEMVERSAEQ AVSLVEAQPL WEYPCRALSE PQEVLSVDFS NFGQEHSLKG
SIELKHTGIC NGVALWVYWQ LVEDNSPRSI VSSGPSEPVV PGEFVKWDMF VRQGVHFPRK
PKDAVTHLEW STDFKPLLGE LNFSFGQKKL
