ID   A0A183M2M0_9TREM        Unreviewed;       593 AA.
AC   A0A183M2M0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=SAM_MT_RSMB_NOP domain-containing protein {ECO:0000313|WBParaSite:SMRZ_0001029601-mRNA-1};
GN   ORFNames=SMRZ_LOCUS10295 {ECO:0000313|EMBL:VDO89740.1};
OS   Schistosoma margrebowiei.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=48269 {ECO:0000313|WBParaSite:SMRZ_0001029601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMRZ_0001029601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO89740.1, ECO:0000313|Proteomes:UP000277204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zambia {ECO:0000313|EMBL:VDO89740.1,
RC   ECO:0000313|Proteomes:UP000277204};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC       ECO:0000256|PROSITE-ProRule:PRU01023}.
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; UZAI01005243; VDO89740.1; -; Genomic_DNA.
DR   STRING; 48269.A0A183M2M0; -.
DR   WBParaSite; SMRZ_0001029601-mRNA-1; SMRZ_0001029601-mRNA-1; SMRZ_0001029601.
DR   Proteomes; UP000277204; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22808:SF1; RNA CYTOSINE C(5)-METHYLTRANSFERASE NSUN2; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000277204};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}.
FT   DOMAIN          1..303
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          317..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        183
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         19..25
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         63
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         90
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         123
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   593 AA;  67339 MW;  24AD705DD400D679 CRC64;
     MLPPLLLDVR SHHTILDLCA APGSKSAQLV ELLHSDAEAV QSRIGVENAP KYVEPTGMVI
     ANDFDQKRCY MMVHQVKRLQ SPCVVITQED ATCFPRLYVT LSPDEKTSQK DLRQLMFDRI
     LADVPCSGDG TLRKNPDLWL RWSPNLGIGE HPLQCRILKR GLELLRDPVG DSTSYPRLVY
     STCSFNPVEN EAVVASVLHA CRGAVRLIEP DLLERILPDS SENKDSVRQK FKFRSGLSNW
     RIMDKKGVWF TSYDEVPTGQ RNYICPSLFP PSNVSDLHLE HCKRVLPHDQ NTGGFFIAVL
     EKIAPLPWMN ATKREVSVSS NQINQTDKQL EPKDDSRPPC VAKKSRIFHE NGLTYIDSTL
     DPIWLTIRDY YKIKDKSSYN GESSLISFCA DNLLSRSGGE GNRCRLLYYT NSLIKNMVST
     NKERGLKIVN TGVRIFSSVE DKQFEGYRLL QDGIEVADAF IPLSSDRRVR LTSNEYCDLV
     LLLKYEMPLL SLMTESTRRQ CENLSPGPIL IDYTPNVTEF TSDDESWTCD SLPRCRLVFS
     GWRGAKSIRH YIGRFERLHF MRLANIEPSP CIMGHTAKEL VAHVNSESNE DVE
//