ANM7_DROME
ID ANM7_DROME Reviewed; 690 AA.
AC Q9W1V1; B5X512; Q8MYV1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 4.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein arginine N-methyltransferase 7;
DE Short=Dart7;
DE EC=2.1.1.-;
GN Name=Art7; ORFNames=CG9882;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=14705965; DOI=10.1042/bj20031176;
RA Boulanger M.-C., Miranda T.B., Clarke S., Di Fruscio M., Suter B.,
RA Lasko P., Richard S.;
RT "Characterization of the Drosophila protein arginine methyltransferases
RT DART1 and DART4.";
RL Biochem. J. 379:283-289(2004).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18369183; DOI=10.1261/rna.940708;
RA Gonsalvez G.B., Praveen K., Hicks A.J., Tian L., Matera A.G.;
RT "Sm protein methylation is dispensable for snRNP assembly in Drosophila
RT melanogaster.";
RL RNA 14:878-887(2008).
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. {ECO:0000269|PubMed:18369183}.
CC -!- TISSUE SPECIFICITY: Expressed at low level in ovary.
CC {ECO:0000269|PubMed:14705965}.
CC -!- DISRUPTION PHENOTYPE: Death at pupal stage.
CC {ECO:0000269|PubMed:18369183}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAM29595.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=ACI46519.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF46952.4; -; Genomic_DNA.
DR EMBL; AY113590; AAM29595.1; ALT_INIT; mRNA.
DR EMBL; BT046131; ACI46519.1; ALT_INIT; mRNA.
DR RefSeq; NP_611753.4; NM_137909.5.
DR AlphaFoldDB; Q9W1V1; -.
DR SMR; Q9W1V1; -.
DR BioGRID; 63270; 4.
DR IntAct; Q9W1V1; 3.
DR STRING; 7227.FBpp0113056; -.
DR PaxDb; Q9W1V1; -.
DR DNASU; 37664; -.
DR EnsemblMetazoa; FBtr0114564; FBpp0113056; FBgn0034817.
DR GeneID; 37664; -.
DR KEGG; dme:Dmel_CG9882; -.
DR CTD; 37664; -.
DR FlyBase; FBgn0034817; Art7.
DR VEuPathDB; VectorBase:FBgn0034817; -.
DR eggNOG; KOG1501; Eukaryota.
DR GeneTree; ENSGT00940000156879; -.
DR HOGENOM; CLU_015180_0_0_1; -.
DR InParanoid; Q9W1V1; -.
DR OMA; LPMANCA; -.
DR OrthoDB; 408622at2759; -.
DR PhylomeDB; Q9W1V1; -.
DR SignaLink; Q9W1V1; -.
DR BioGRID-ORCS; 37664; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37664; -.
DR PRO; PR:Q9W1V1; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034817; Expressed in eye disc (Drosophila) and 24 other tissues.
DR Genevisible; Q9W1V1; DM.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; ISS:FlyBase.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IBA:GO_Central.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IMP:UniProtKB.
DR GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; ISS:FlyBase.
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 2: Evidence at transcript level;
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_0000373914"
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 401
FT /note="R -> C (in Ref. 3; AAM29595)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 690 AA; 77946 MW; 0B0AE55BFD3E2D1C CRC64;
MSCFSHVMNP ITGQNSWQER GDDYDYHLEV ANAGFGDMLH DWERNQKYFA ALRKTIAGMR
EAGREVHVLD IGTGTGILSM MALAAGADSV TACEAFLPMA NCAEKILAAN GAGDKVRLIR
KRSTEIQVGE DMPRKANLLV AELLDTELIG EGAIGIYNHA HAELLTEDAL CIPARARCYA
QVAQSPLAAQ WNSLKTIANL DGEPLLHPPE QLKSCQGEAA LHDVQLSQLP SSAFRPLTDP
VEIFQFDFQR KQEREKQRSQ LLKLQSKQPG AAELVFYWWD IQLDDDGEIL LSCAPYWAHP
QLKELAAEKA KDHPLPNVVP WRDHWMQAIY YIPKPLQLLE AGKSFHLSCH HDEYSLWFDA
REEAPTKSVR RHTCTCDLHM TYSRSRIGQL NQSPRNKRYL RYLEESIEAE KSNVLVLGNG
CLLGLASSAL GAASVLLHEP HRFSRRLIES IVKHNQLKNV QFLDKVEELE DSRLAALTHI
FAEPYFLNAI LPWDNFYFGT LLTKIKDRLP EGVKISPCSA RIYALPVEFL DLHKIRAPVG
SCEGFDLRLF DEMVERSAEQ AVSLVEAQPL WEYPCRALSE PQEVLSVDFS NFGQEHSLKG
SIELKHPRIC NGVALWVDWQ LVEDNSPRSI VSSGPSEPVV PGEFVKWDMF VRQGVHFPRR
PKEAITHLEW STVFKPLLGE LTFSFGQKKL
