ID   A0A078A0N0_STYLE        Unreviewed;       850 AA.
AC   A0A078A0N0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Trna (Cytosine-c)-methyltransferase {ECO:0000313|EMBL:CDW75761.1};
GN   Name=Contig1876.g2028 {ECO:0000313|EMBL:CDW75761.1};
GN   ORFNames=STYLEM_4756 {ECO:0000313|EMBL:CDW75761.1};
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW75761.1, ECO:0000313|Proteomes:UP000039865};
RN   [1] {ECO:0000313|EMBL:CDW75761.1, ECO:0000313|Proteomes:UP000039865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130c {ECO:0000313|EMBL:CDW75761.1,
RC   ECO:0000313|Proteomes:UP000039865};
RA   Swart Estienne;
RL   Submitted (JUN-2014) 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}.
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DR   EMBL; CCKQ01004598; CDW75761.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078A0N0; -.
DR   EnsemblProtists; CDW75761; CDW75761; STYLEM_4756.
DR   InParanoid; A0A078A0N0; -.
DR   OMA; CRIVICK; -.
DR   OrthoDB; 197651at2759; -.
DR   Proteomes; UP000039865; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
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; 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; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   PRINTS; PR02011; RCMTNCL1.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000039865};
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          199..576
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          213..240
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        449
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         315..321
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         345
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         372
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         396
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   850 AA;  98908 MW;  9C748457E9B55186 CRC64;
     MSNQATKGVS IGAGDSDDDE FGRIPSAADV QKTNTVEIMP NQFGYDDSDE EEETKDMGTD
     YDPPTRTYGI EEYTMSDATM KLFERELGQT SQLRQESKAP AKMMQTFSGQ TTETTTETLT
     VGVEVQINTN KQEKEERKGR KHKKDKKWHD KKVKREDDWA TGTNRKIDPN YILEIKQNQE
     FETYYREANI LPAEEFDKFY QILKEPLDIC FRINSVDKHF EKTQQEIEDL VQKMKGIDEL
     KDKYPKKLLW YPNNLAYTFN ECSRGEMRAN PLLKNFHQFL ILETEMGRIF RQEAVSMIPV
     TLLNIEPHHS VIDVCAAPGS KTIQILEQLH QAHEKIPKGF VIANDTDQKR AYLLTHQARR
     LNSSALFITN NDARFLPYLK IDEHNNNMKF DRILCDVPCS GDGTLRKNLA LWKNFNSHLG
     HSCHPLQLHI LERAFQHLKK GGRLVYSTCS FNPIENEAVV AAALSRHIKQ MELVDVSKEV
     SPHLKYRPGL VNWRVYHRGK GKREGPAWYE TYDKVPNYKR KVIKETMFTD TYTMFNNETD
     RPDDMKSDPL NLRRCLRLFP HDNNQGGFFV AVFTKVLDEH EGFIYDDMYQ MNAWDDPRVK
     QKPILDDIRE FAEEFEKDLK IHEEKNNVPQ ELSQQNQILS IVKDAQDQQK QAMKDSGIVF
     GKMSQIYDNK EHLFPFEKLL ETKQDLWVNL QLFYGINAEF PCENLYFQKD TTNCIAFVSE
     GLSQLMKCQR KHKLKVVNLG VKLFSKNRDI KSPGKYRLLQ EGLELLMPYM NDERKIQVSK
     LLLAQFLDKI NFTFEELRNM GHSQFEGKEP GSAVITSGDL YVTIWIGVNN VSLMIGKEEI
     KSFKFLLINQ
//