ID T0MKM1_9MICR Unreviewed; 486 AA.
AC T0MKM1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Putative methyltransferase {ECO:0000313|EMBL:EQB61520.1};
GN ORFNames=NAPIS_ORF00906 {ECO:0000313|EMBL:EQB61520.1};
OS Vairimorpha apis BRL 01.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae;
OC Vairimorpha.
OX NCBI_TaxID=1037528 {ECO:0000313|EMBL:EQB61520.1, ECO:0000313|Proteomes:UP000053780};
RN [1] {ECO:0000313|EMBL:EQB61520.1, ECO:0000313|Proteomes:UP000053780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRL 01 {ECO:0000313|EMBL:EQB61520.1,
RC ECO:0000313|Proteomes:UP000053780};
RX PubMed=23829473; DOI=10.1186/1471-2164-14-451;
RA Chen Yp., Pettis J.S., Zhao Y., Liu X., Tallon L.J., Sadzewicz L.D., Li R.,
RA Zheng H., Huang S., Zhang X., Hamilton M.C., Pernal S.F.,
RA Melathopoulos A.P., Yan X., Evans J.D.;
RT "Genome sequencing and comparative genomics of honey bee microsporidia,
RT Nosema apis reveal novel insights into host-parasite interactions.";
RL BMC Genomics 14:451-451(2013).
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}.
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DR EMBL; KE647131; EQB61520.1; -; Genomic_DNA.
DR AlphaFoldDB; T0MKM1; -.
DR VEuPathDB; MicrosporidiaDB:NAPIS_ORF00906; -.
DR HOGENOM; CLU_005316_4_3_1; -.
DR Proteomes; UP000053780; 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:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProt.
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:UP000053780};
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 24..325
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 233
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 112..118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 136
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 180
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 486 AA; 56280 MW; 0DAF50E077C293EA CRC64;
MGLEDFIKFY KKNLNLCDND FNNLLETLQK PLMSAFRITN TVVKEFILKK LSNLNESKVF
PNVYEVNKRK MPFRNFIVTQ TSVGNIQRQE VVSMLPVFLM NLKKCHSVLD MCAAPGSKTK
QLLEIVGDDG LVVANEVKSK RLEILVSECC KLPSKSLLVI KHDASKMPIF KNDFDRVLCD
VPCSGDATAR KNLEVLPKWN LQNALSLIEL QFKILKHSLN FVKDDGLIIY STCSLNIMEN
ECIIQKAVLE ENLEIVDLRE NINEEYISKD FKIRNGITNW HFDLKKYNNI NLEPIDKDIG
LSKCLRVYPH DQNTGGFFIV GLKKISKKTK QLKSFKPRFN IYEIDEELKK ILQKNYKLEN
NIYIQRWKNA KSIYEVNDEI LKILKTSPLN VAYFGKKVFV KSTDIELNWI RKVSFNKESL
LHDIELDEEK SNNFINKKEI LFRFKKGPII VLCNNLKIKI GALSDGEKIV ALLDDKLQKA
LKQLLF
//
