ID   ANM7_CAEBR              Reviewed;         656 AA.
AC   A8XFF4;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Protein arginine N-methyltransferase 7;
DE            EC=2.1.1.-;
GN   Name=prmt-7; ORFNames=CBG12433;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Arginine methyltransferase that can both catalyze the
CC       formation of omega-N monomethylarginine (MMA) and symmetrical
CC       dimethylarginine (sDMA). {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; HE600913; CAP31415.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8XFF4; -.
DR   SMR; A8XFF4; -.
DR   STRING; 6238.CBG12433; -.
DR   WormBase; CBG12433; CBP09075; WBGene00033385; Cbr-prmt-7.
DR   eggNOG; KOG1501; Eukaryota.
DR   HOGENOM; CLU_015180_0_0_1; -.
DR   InParanoid; A8XFF4; -.
DR   OMA; LPMANCA; -.
DR   OrthoDB; 408622at2759; -.
DR   Proteomes; UP000008549; Chromosome I.
DR   GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IBA:GO_Central.
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..656
FT                   /note="Protein arginine N-methyltransferase 7"
FT                   /id="PRO_0000373906"
FT   DOMAIN          12..338
FT                   /note="SAM-dependent MTase PRMT-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT   DOMAIN          343..656
FT                   /note="SAM-dependent MTase PRMT-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
SQ   SEQUENCE   656 AA;  74267 MW;  74AE7A8E94661F61 CRC64;
     MFLERVNQKT GEREWVVAQE DYDMAQELAR SRFGDMILDF DRNDKFLEGL KTTIPEKKKE
     NGDGLVHVLD IANITFPGTG TGLLSLMAAR EGADKVTALE VFKPMGDCAR HITGCSPWAE
     KITVISERST DVSQIGGTAA DIIVAEVFDT ELIGEGALRT FKEALQRLAK PGCRVVPSSG
     NVYIVPVESH LLKMFNTIPR INGGEDEHPL GTCSGTASVF DVQLSELETH EFRELAEPIV
     AFKFDFENEE KIIYNESFVR EAIAHTSGTI DAIMMWWDID MDGKGETFID MAPRWKNPKH
     YAWRDHWMQA VYYLPDKKCV EKAQKFEIIC NHDEFSIWFS DVGKDSTRSY CVCGLHSMLS
     RQTVYHINEM FEDQSFRAEV DRLSSGLNVV TVGEGSFVGL LAAKTAKTVT IIEPNERFRD
     IFHKYVLYYN MKNVHIVEKV THLIEKPDIV IAEPFYMSAM NPWNHLRFLY DVEILKMLHG
     DDLKVEPHLG TLKAIPECFE DLHKIAADVN TVNGFDLSYF DRISTKARAA TDAIVDEQSL
     WEYAGTVKGE PVELLTFPVD GRILSRKCVG KMDNMQSSNG IPIWMEWQFG DLTLSTGLLS
     TSESRKPCWN KGYKQGVYFP ITNLQNESSI NLNALFDKSS GDITFQFKKF DVQSGN