ID A0A183MZB7_9TREM Unreviewed; 755 AA.
AC A0A183MZB7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Protein arginine N-methyltransferase {ECO:0000256|PIRNR:PIRNR036946};
DE EC=2.1.1.- {ECO:0000256|PIRNR:PIRNR036946};
GN ORFNames=SMRZ_LOCUS21392 {ECO:0000313|EMBL:VDP39364.1};
OS Schistosoma margrebowiei.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=48269 {ECO:0000313|WBParaSite:SMRZ_0002139301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMRZ_0002139301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP39364.1, ECO:0000313|Proteomes:UP000277204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zambia {ECO:0000313|EMBL:VDP39364.1,
RC ECO:0000313|Proteomes:UP000277204};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Arginine methyltransferase that can both catalyze the
CC formation of omega-N monomethylarginine (MMA) and symmetrical
CC dimethylarginine (sDMA). {ECO:0000256|PIRNR:PIRNR036946}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family. PRMT7
CC subfamily. {ECO:0000256|PIRNR:PIRNR036946}.
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DR EMBL; UZAI01018689; VDP39364.1; -; Genomic_DNA.
DR STRING; 48269.A0A183MZB7; -.
DR WBParaSite; SMRZ_0002139301-mRNA-1; SMRZ_0002139301-mRNA-1; SMRZ_0002139301.
DR Proteomes; UP000277204; Unassembled WGS sequence.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.70.160.11; Hnrnp arginine n-methyltransferase1; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR014644; MeTrfase_PRMT7.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PROTEIN ARGININE N-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11006:SF4; PROTEIN ARGININE N-METHYLTRANSFERASE 7; 1.
DR PIRSF; PIRSF036946; Arg_N-mtase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01015};
KW Reference proteome {ECO:0000313|Proteomes:UP000277204};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01015};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU01015}.
SQ SEQUENCE 755 AA; 85779 MW; 877039E915AD9B67 CRC64;
MKTEHIFIPQ FNPVVGRMQW KDVDPDYEFN QEIARSGYGD MLHDYDRNHK YRLAIEHTIK
RLKQQYPQNP VHVLDIGTGT GLLSMMAVNA GADLVTACES FIPMATCALN ILRNNGFSDK
INIIPKRSTD LIVGVDMPCK ANVLVAELFD TELIGEGALE TYRHAAEHLL TLDASLIPCA
AQVYLQVVES QFLWSHHRLF PFQYKIGDTT IDINEFQHAE IESCSGLPST FDIQVSEIQL
EGSQLVSCDR QLRCLLKSPR LVKRFNFGPP ADLIKLNDVL DLECTTFESG IAHAFIVWWS
LQMEPTNSVP PISVAPTWAG DPNSAWRDHW MQAVYFPKTA HYLIKNESFM VRYLHDSLSM
RFDILPAPNF NAKPDTSSLD VRNEMSCLSC SCDLHRVWPR TRISELNSSD YKTFSTKIIN
SLITVSQKYP ASLFNVLVVS DCTYLPFLLG KSLAKHVKQF QLVHLDTSPS SCLLLDRIYK
SFSSSRSIIE SCQSIEEVFS RMTPNMFTKT NPTESTLILI SEPYISSSIL PWDSLYFWYA
FQNLLSHNPA YSSLYLFSPV RLRIYAILVD FKNLWRIRSP VGFTCESFDL RPFDDLVLDA
SAKSDELIEP HPLWEYPNTA RSDACVIFDM VLPNSSDLGS DFQYADSKKL IHCKQNTLTT
SSSSVNGIAL WCEWLYNTPA THHSNETWWY APAGPNKITT LNEPISWKSR GTQQGVFLFP
SEWKAKILPN DLLRISACMD FDISTGVLSP SFKII
//
