ID   A0A914SBG0_9BILA        Unreviewed;       881 AA.
AC   A0A914SBG0;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   18-JUN-2025, entry version 13.
DE   RecName: Full=tRNA (cytosine(34)-C(5))-methyltransferase {ECO:0000256|ARBA:ARBA00012629};
DE            EC=2.1.1.203 {ECO:0000256|ARBA:ARBA00012629};
OS   Panagrolaimus sp. PS1159.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Panagrolaimoidea; Panagrolaimidae;
OC   Panagrolaimus.
OX   NCBI_TaxID=55785 {ECO:0000313|WBParaSite:PS1159_v2.g11323.t1};
RN   [1] {ECO:0000313|WBParaSite:PS1159_v2.g11323.t1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2022) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   WBParaSite; PS1159_v2.g11323.t1; PS1159_v2.g11323.t1; PS1159_v2.g11323.
DR   Proteomes; UP000887580; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016428; F:tRNA (cytidine-5-)-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030488; P:tRNA methylation; IEA:TreeGrafter.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR023270; RCMT_NCL1.
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-RELATED; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF25376; Pre-PUA_NSUN2; 1.
DR   Pfam; PF25378; PUA_NSUN2; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   PRINTS; PR02011; RCMTNCL1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000887580};
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}; tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT   DOMAIN          248..605
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          198..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          829..858
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..213
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        834..858
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        497
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         364..370
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         393
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         421
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         444
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   881 AA;  100665 MW;  758CA883BC4F4221 CRC64;
     MATKNEFLFL KNKSFANSQT VSEKQYSNLN LNQNQKCSDI SLFQSFSKSS NTNNYVSDNC
     KEKSQLWNKS SKISNIVTPN AEAQKEDFNK CLKEEDYPNT NNSTLFLHIE ADTAFDSFNG
     KNSIKNEATK QDFNTSTFFI ENLFEFPRQQ SNEVSEPEVS QFKASQQLLN FNEVSNNDPQ
     DFKPSRATKM AAALDAEKMD TTNAEEEKPK VDNRSPNYQL DPIIKKNEKL FSYYKAQPVI
     PPSEYDAYVE TIKVDLPSSF RVQMSLPEAK LVEKYLREHF FDKISQIADL NGVISVPTPI
     KFVPYGYQAV MPRSVMRSHP LLRDLHQFLV SETEIGVLSR QEAVSMVPPL LLDIKPEHFV
     LDMCAAPGSK TMQLIELMHK DEPNPSGLLV ANDIDYARCY LLVHQTLKRM PTANCIVVNQ
     DGSQIPTVID ENQKPILFDR ILCDVICTGD GTFRKNPELW KTWDPQKGLN LHRIQIHIAR
     RGLELLKVGG RMVYSTCSLN PIEDEAVICH LLRKFEGKVR LVDVSKELPD LIRSPGISSW
     KVIDKTMTEY QNIDAVPEGL RRAILPSMFP PTSQEASKFH LEHGFRILPH QQNSGGFYVA
     VLEKVEAFDS DSKVWKPSFF GPPDRKRKRR MVREDPFNFL TEKESADVKA DLEEHYGLQS
     NFAYDNLLIR SAETEKKKVI YFTNDNLRKF MKYNETRFKI VNAGVGVLRR CDKVSVSKYR
     LMQDGLPHMT PYVKKRIVSI GIEDAIKILE GSNDNHFANI QELSEPGELK TLPCGSVILK
     LKNGDFQKEI VCWLGQHTVT AFITKEEKIH CLTMLGHDAA KLRQQVQSTR QKKALGDRQP
     RKNDDETAKA KIENVKEEKP NEEDFVIIDE TVAADVKEEQ N
//