ID   ANM7_ANOGA              Reviewed;         690 AA.
AC   Q7QIL2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 4.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Protein arginine N-methyltransferase 7;
DE            EC=2.1.1.-;
GN   Name=Art7; ORFNames=AGAP006938;
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST;
RX   PubMed=12364791; DOI=10.1126/science.1076181;
RA   Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA   Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA   Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA   Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA   Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA   Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA   Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA   Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA   Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA   Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA   Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA   Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA   McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA   O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA   Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA   Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA   Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA   Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA   Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA   Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA   Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA   Collins F.H., Hoffman S.L.;
RT   "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL   Science 298:129-149(2002).
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; AAAB01008807; EAA04124.4; -; Genomic_DNA.
DR   RefSeq; XP_308819.4; XM_308819.4.
DR   AlphaFoldDB; Q7QIL2; -.
DR   SMR; Q7QIL2; -.
DR   STRING; 7165.AGAP006938-PA; -.
DR   PaxDb; Q7QIL2; -.
DR   GeneID; 1270147; -.
DR   KEGG; aga:AgaP_AGAP006938; -.
DR   CTD; 1270147; -.
DR   VEuPathDB; VectorBase:AGAP006938; -.
DR   eggNOG; KOG1501; Eukaryota.
DR   HOGENOM; CLU_015180_0_0_1; -.
DR   InParanoid; Q7QIL2; -.
DR   OMA; LPMANCA; -.
DR   OrthoDB; 408622at2759; -.
DR   PhylomeDB; Q7QIL2; -.
DR   Proteomes; UP000007062; Chromosome 2L.
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; 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_0000373909"
FT   DOMAIN          5..355
FT                   /note="SAM-dependent MTase PRMT-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT   DOMAIN          364..690
FT                   /note="SAM-dependent MTase PRMT-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
SQ   SEQUENCE   690 AA;  77580 MW;  4FD6CB2F635C395E CRC64;
     MEDTFQDSAS EDGGFDLRQE IARSAFADMC HDWERNQKYD RALQLTIARL HAAGQQAHVL
     DIGTGSGLLS MMAIRAGADS VVACEAFRPM ADCAELIIAA NGMQDRIRLV KKRSTKVTVG
     PGQDMERRAN VLVTELFDTE LIGEGALGTY RHALQHLLTE DVLTIPHQAT VYAQVVECPL
     ALSWQQLKTL SNADGDILLR VPPEVATCRG SSAVFDIQLS QLPAGSFNVL TDPVPVFKFA
     WSKHQELIND RCEQSVCHAR TAGFPQAVFM WWDLTMDREG DVLLSCAPYW AHPEHEALKK
     KHSDNGSKRR LPEGNYIPWR DHWMQAVYFL PPLKIPLQRG QQFVLQSYHD EFSLWFGVGE
     QSVKEPLTAP HCTCGWHIAQ SRSRIGQLND SLRNKRYLNY FERVFSSDSV VLVLSEGSLL
     GLAAARMGVK QVLLYEPNAI SRRCMEAFVE HNSVANVRFL PSADALEPEQ AATITHVFAE
     PHFPSAILPW DNLHYGDLLK NLRPLLPASV TVIPASGTLY ALPVEFVDLY KINAPLGSCE
     GFDLTLMDQL IDQHSTFADS PVEAQPLWEY PSFPLAGTTR LIEINFVKDF EQSKLERGEL
     FVSEPERLNG IAIWIDWHLD GSHSPKTTIS SGPLVPVEES SDEPTRWNTN WRQGVHLLRK
     TPNRKGTIPW SVKFNPVLSN VYFRFDEEEQ