ANM7_DROYA
ID ANM7_DROYA Reviewed; 690 AA.
AC B4P925;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Protein arginine N-methyltransferase 7;
DE EC=2.1.1.-;
GN Name=Art7; ORFNames=GE11609;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01;
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; CM000158; EDW92265.1; -; Genomic_DNA.
DR RefSeq; XP_002092553.2; XM_002092517.2.
DR AlphaFoldDB; B4P925; -.
DR SMR; B4P925; -.
DR STRING; 7245.FBpp0256619; -.
DR EnsemblMetazoa; FBtr0258127; FBpp0256619; FBgn0229409.
DR GeneID; 6531766; -.
DR KEGG; dya:Dyak_GE11609; -.
DR eggNOG; KOG1501; Eukaryota.
DR HOGENOM; CLU_015180_0_0_1; -.
DR OMA; LPMANCA; -.
DR OrthoDB; 408622at2759; -.
DR PhylomeDB; B4P925; -.
DR Proteomes; UP000002282; Chromosome 2R.
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_0000373922"
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; 77704 MW; B506CD215688D589 CRC64;
MSCFSHVMNP ITGQNSWQER GDDYDYHLEV ANAGFGDMLH DWERNQKYFA ALKKTIAGMR
EAGREVHVLD IGTGTGILSM MAVEAGADSV TACEAFLPMA NCAERILAAN GAGDKVRLIR
KRSTEIQVGE DMPRKANLLV AELLDTELIG EGAIGIYNHA HAELLTEDAL CIPARARCYA
QVAQSPLAAQ WNSLKTIANL DGEPLLHPPE QLKSCQGEAA LHDVQLSQLP SSAFRPLTDP
VEIFQFDFQR KLEREKQRAQ LLTLQSKQPG AAELVFYWWD IQLDDGGEIL LSCAPYWAHP
QLKELAAEKG KDHPLANVLP WRDHWMQAIY YIPKPLQLVE AGKSFHLSCH HDEYSLWFDA
REEAPTKSVR RHTCTCDLHM TYSRSRIGQI NQSTRNKRYL RYLEENIEAE KSNVLVLGNG
CLLGLASSAL GAASVLLHEP HRFSRRLLES IVTHNQLKNV QFLDKVEELE DSQLSALTHV
FAEPYFLNAI LPWDNFYFGT LLTKIKDRLP ESVKISPCSA RIYALPVEFL DLHKIRAPVG
SCEGFDLRLF DEMVERSAEQ AVSLVEAQPL WEYPCRALSE PQEVLNVEFS SFTQEHSLKG
SIELKHPGTC NGVALWVDWQ LVEENSPRSI VSSGPSEPVV PGEFVKWDMF VRQGVHFPRR
PTGGITHLEW STDFKPVLGE LNFSFGQKKL
