ID   A0A1D3JK20_PLAMA        Unreviewed;      1135 AA.
AC   A0A1D3JK20;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=tRNA m5C-methyltransferase, putative {ECO:0000313|EMBL:SBT86868.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:SBT86868.1};
GN   Name=PmUG01_01015700 {ECO:0000313|EMBL:SBT86868.1};
GN   ORFNames=PMUG01_01015700 {ECO:0000313|EMBL:SBT86868.1};
OS   Plasmodium malariae.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=5858 {ECO:0000313|EMBL:SBT86868.1, ECO:0000313|Proteomes:UP000219813};
RN   [1] {ECO:0000313|EMBL:SBT86868.1, ECO:0000313|Proteomes:UP000219813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   EMBL; LT594622; SBT86868.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D3JK20; -.
DR   VEuPathDB; PlasmoDB:PmUG01_01015700; -.
DR   OrthoDB; 197651at2759; -.
DR   Proteomes; UP000219813; Chromosome 1.
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; 2.
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; 2.
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:UP000219813};
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          291..550
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          241..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..266
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        429
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         321
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         376
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   1135 AA;  132961 MW;  F32CFA76B0821A98 CRC64;
     MKGSTKEIPY YDNSVVLEKN EGFFNYYVNQ NIIKKEEIDN FMEIINKELP ITFRVLKNNK
     YSDYIHENIK KKLECICKDN YSIIKLNEED HMYEIYITRS QIKKNENYKN LCSYLINLNE
     SGYIFRQELV SMLPILFLKL KENFFVLDIC AAPGSKTAQI VDYMHLINKK NVKNYLIKKF
     IQKNCSSINN LRENAGNQDS DSCCSDIRDS EGINSIEGSN GYNDDEYAYM CGNRSTKFSG
     RTPVEGNVKT NEHKNVKEND EGERNKTDTE NIYKSYYTIL DNNLYDEKLF EYILNVDNNL
     YNDYKKLISN NNPTGVVVAN DANFKRCCML FHRLKNIHSN CLVVTNNNAI NFPYIYIKNG
     KENKVEKKFF DSVLCDVPCS GDGTLRKDRN IWLNWNPLNA YNLFQVQVNI LKRSIELTKE
     NGVIVYSTCS LNPIENEAVI CEIFNSVENF NCLKLINFEN ELITKLNFKE GITQWRVLID
     DIWFDTYQQF CDYLKNKESS KYKKIYDKIQ NGMFTPPKEF IELINLKYVK RFFPHHYNAG
     GFFIAVIKKC GKLKWKEKAK RENMNKCIVN KNVISNRNKL EKGELRKKYK NRKYKKSNKK
     KKNKNGDLSF NGYNIKQNFS REIENEQRKI LEIKNNSPEQ VIQNGLRKSC SPVNSDGSVM
     DDEHIEKNYN VVNHDLIMKN YKVIDNINDT RNYQVIGDGD ITKNYNNEEN GNVTKNDNLE
     ENDNFEKNYN VIDSDFIISS CPIRRPHETS KGDVIINLIN RKSEEKLNNY SKNEMDSSVE
     YTEQYDILKE NNKTANGYVK PKGSVQTKCK VEDQIYMGNE KLTKQQEYVS LDYYEKLFCI
     NDTLERIKNY FNLNEEFLSI KSNLYIHLKD DSNFCKLSIN ERINSNIKKI NFVSNYTKDI
     LECYTKIKLK IISAGITVIQ IDKNKKNKVE NYYRINYSGC LNFVPFFKDV DAFLLNKIYR
     KEIIKNYFSP IYENKNRVFH FESYMNQLIG ERKSTLSKGT TNNTKVVKNV GENTHPASYV
     NNEKITNSLG GEENLSEEKN KHNKYSDETE KKNMNTIWVK SDVILDLIKV DKSKINNITN
     ETIKQTEKLT KYSPNILLTL NKNKQILAIP SNKGNLYVDI SIDKNSIIML PYILN
//