ANM7_DROMO
ID ANM7_DROMO Reviewed; 698 AA.
AC B4KSL6;
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=GI21139;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22;
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; CH933808; EDW10515.1; -; Genomic_DNA.
DR RefSeq; XP_002006580.1; XM_002006544.2.
DR RefSeq; XP_015019889.1; XM_015164403.1.
DR RefSeq; XP_015019890.1; XM_015164404.1.
DR AlphaFoldDB; B4KSL6; -.
DR SMR; B4KSL6; -.
DR STRING; 7230.FBpp0170356; -.
DR EnsemblMetazoa; FBtr0171864; FBpp0170356; FBgn0143871.
DR EnsemblMetazoa; FBtr0422443; FBpp0380492; FBgn0143871.
DR EnsemblMetazoa; FBtr0424994; FBpp0382787; FBgn0143871.
DR GeneID; 6580777; -.
DR KEGG; dmo:Dmoj_GI21139; -.
DR eggNOG; KOG1501; Eukaryota.
DR HOGENOM; CLU_015180_0_0_1; -.
DR InParanoid; B4KSL6; -.
DR OMA; LPMANCA; -.
DR OrthoDB; 408622at2759; -.
DR PhylomeDB; B4KSL6; -.
DR Proteomes; UP000009192; 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..698
FT /note="Protein arginine N-methyltransferase 7"
FT /id="PRO_0000373915"
FT DOMAIN 14..357
FT /note="SAM-dependent MTase PRMT-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT DOMAIN 366..698
FT /note="SAM-dependent MTase PRMT-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
SQ SEQUENCE 698 AA; 79180 MW; ED9F9A3E8C4DA7BA CRC64;
MASFAQVINP MTGQNTWQER GDDYDYHQEV ANAGFGDMLH DWERNQKYDA AIRKTIAGMR
QAGKQVHVLD IGTGTGILAM MALRAGADTV TACEAFVPMA NCAARILAAN DAAHVRLIRK
RSTDIVMGVD MPHRANLLVA ELLDTELIGE GAIGIYNHAH EELLTDDALC IPARATCYAQ
VAQSPLASQW NSLKILPDLD GDILLRPPTQ LLQCSGEAAL HDVQLSQLPP HSFHVLSEPT
QIFHFDFQRK QPLELMRENV VRVQLSRPGS VELVFYWWQI ELDDAGEQLL SCAPYWAHPE
LEQLKATCKD KQRPLANIVP WRDHWMQAIY YIPKALHLHD AGEEFWLRCY HDEYSLWFDA
HKEQPEKPAR RHSCTCDLHM TYTRNRIGQL NQSIRNKRYL AYLEQAVQSK SAHVLVMGDG
CLLGLASAAL GAASVYCLEP HRFSRRLLES VVKHNQLKNV KFLDSLKQLE PNELDTITHI
FAEPYFLNSI LPWDNFYFGT LLLQLEQLHQ KLPANVEISP CAARIFALPV EFLDLHKIRA
PIVSCEGFDL RLFDDMVQRS AEQALSQVEA QPLWEYPCRA LAQPQQLLSV DFANFGVEQS
NHGSIKLTAE GNCNGIALWV DWQLSPNENP KSIVSSGPLE PVETGQYVKW DMFVRQGVHF
INQTTAEKKY LNWSTQFRPL LGELNFNFSL NANREKSE