ID   ANM7_DROER              Reviewed;         690 AA.
AC   B3NP10; Q8I1F2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Protein arginine N-methyltransferase 7;
DE            EC=2.1.1.-;
GN   Name=Art7; ORFNames=GG20071;
OS   Drosophila erecta (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7220;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12537575; DOI=10.1186/gb-2002-3-12-research0086;
RA   Bergman C.M., Pfeiffer B.D., Rincon-Limas D.E., Hoskins R.A., Gnirke A.,
RA   Mungall C.J., Wang A.M., Kronmiller B., Pacleb J.M., Park S., Stapleton M.,
RA   Wan K.H., George R.A., de Jong P.J., Botas J., Rubin G.M., Celniker S.E.;
RT   "Assessing the impact of comparative genomic sequence data on the
RT   functional annotation of the Drosophila genome.";
RL   Genome Biol. 3:RESEARCH0086.1-RESEARCH0086.20(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14021-0224.01;
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; AY190941; AAO01020.1; -; Genomic_DNA.
DR   EMBL; CH954179; EDV56743.1; -; Genomic_DNA.
DR   RefSeq; XP_001976343.2; XM_001976307.2.
DR   AlphaFoldDB; B3NP10; -.
DR   SMR; B3NP10; -.
DR   STRING; 7220.FBpp0138617; -.
DR   EnsemblMetazoa; FBtr0140125; FBpp0138617; FBgn0064628.
DR   GeneID; 6547319; -.
DR   KEGG; der:6547319; -.
DR   eggNOG; KOG1501; Eukaryota.
DR   HOGENOM; CLU_015180_0_0_1; -.
DR   OMA; LPMANCA; -.
DR   OrthoDB; 408622at2759; -.
DR   PhylomeDB; B3NP10; -.
DR   Proteomes; UP000008711; 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; Repeat; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..690
FT                   /note="Protein arginine N-methyltransferase 7"
FT                   /id="PRO_0000373912"
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"
FT   CONFLICT        339
FT                   /note="V -> I (in Ref. 1; AAO01020)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        406
FT                   /note="S -> N (in Ref. 1; AAO01020)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        511
FT                   /note="Q -> E (in Ref. 1; AAO01020)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        593
FT                   /note="S -> G (in Ref. 1; AAO01020)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   690 AA;  77838 MW;  B5C22A4B92C841F2 CRC64;
     MSCFSQAINP ITGQNSWQER GDDYDYHLEV ANAGFGDMLH DWERNQKYFA ALKKTIAGMR
     EAGREVHVLD IGTGTGILSM MAVEAGADSV TACEAFLPMA NCAERILAAN GAGDKVRLIR
     KRSTEIQVGE DMPRKANLLV AELLDTELIG EGAIGIYNHA HAELLTEDAL CIPARARCYA
     QVAQSPLAAQ WNSLKTIANL DGEPLLHPPE QLKSCQGEAA LHDVQLSQLP SSAFRPLTDP
     VEIFQFDFQR KQEREKQRAQ LLKLQSKQPG AAELVFYWWD IQLDDGGEIL LSCAPYWAHP
     QLKELAAEKG NDHPLPNVVP WRDHWMQAIY YIPKPLQLVE AGKSFHLSCH HDEYSLWFDA
     REEAPTKSVR RHTCTCDLHM TYSRSRIGQI NQSPRNKRYL RYLEESIEAE KSNVLVLGNG
     CLLGLASSAL GAASVLLHEP HRFSRRLLES IVKHNQLKNV QFLDKVEELE DSQLAALTHI
     FAEPYFLNAI LPWDNFYFGT LLTKIKDRLP QNVKISPCSA RIYALPVEFL DLHKIRAPVG
     SCEGFDLRLF DEMVERSAEQ AVSLVEAQPL WEYPCRALSE PQEVLNVEFS NFSQEHSLKG
     SIELKHSGTC NGVALWVDWQ LVEDNSPRSI VSSGPSEPVV PGEFVKWDMF VRQGVHFPRR
     PKEPITHLEW STAFKPELGE LNFTFGQKKL