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Database: UniProt
Entry: M2RUT3_ENTHI
LinkDB: M2RUT3_ENTHI
Original site: M2RUT3_ENTHI 
ID   M2RUT3_ENTHI            Unreviewed;       630 AA.
AC   M2RUT3;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=tRNA (Cytosine5)-methyltransferase, putative {ECO:0000313|EMBL:EMD42741.1};
GN   ORFNames=EHI5A_096670 {ECO:0000313|EMBL:EMD42741.1};
OS   Entamoeba histolytica KU27.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=885311 {ECO:0000313|EMBL:EMD42741.1, ECO:0000313|Proteomes:UP000011755};
RN   [1] {ECO:0000313|EMBL:EMD42741.1, ECO:0000313|Proteomes:UP000011755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KU27 {ECO:0000313|EMBL:EMD42741.1,
RC   ECO:0000313|Proteomes:UP000011755};
RA   Hannick L., Zafar N., Lorenzi H., Ali I.A., Petri W.P., Caler E.;
RL   Submitted (FEB-2013) 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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   EMBL; KB445450; EMD42741.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2RUT3; -.
DR   EnsemblProtists; EMD42741; EMD42741; EHI5A_096670.
DR   VEuPathDB; AmoebaDB:EHI5A_096670; -.
DR   Proteomes; UP000011755; 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   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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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          55..402
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        295
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         165..171
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         194
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         242
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   630 AA;  72226 MW;  9949E29F5E93CD5D CRC64;
     MEGEKKEEIQ QEEIKKDDGR KPSKKDYHYI TENPEMEKFY SQQTSIMNNE EFKEYIETMH
     KTLPTTFRLT RNEQTPIIKE ELKRLINNIE NEQERPIELS WYPGGIAYQL NASRGEIQKN
     KSLEELRKFI IVQTEAGVIS RQEAVSMIPP LFLNVKPYHD VLDLCAAPGS KTTQILEMIH
     SGPEEATGIV IANDSDYKRC ELLDHQTKRL QSPNIIITNH LAQNYPVKIG DQFMKFDRVL
     CDVPCSGDGT LRKNPDAWGK WNIMRGINLH KTQCTIMRRA VRLVKSCGRF VYSTCSLNPY
     EDEAVVAFIL RNYPQIRLVD VSTELPTLKR CKGVSSWKVF NKEGEELTIK PDSKEDGSSK
     IPSTLFPPTE EEAKRFRLDR CMRFLPQLQN TGGFFVAVLE KVGDLDNDFK EEKQKRKKAP
     KPIKTRKGDS RLMPLNMTEG YETITQTIKN FYGLEGSGFD FECLGFKGDG KGTLHYLIKK
     AMDLVRINEL KIVGGGLKLF RKHSVGSNSS FRLSNEGLSA VAHLFGERRK LEIKHEEFVK
     MLVSESPVQL GNEVMERAKD MEVGCVIFQI KDANSPINKQ YFSGWKSKGL SLFVSKVDKK
     ALCQNLKIEL PKNELHEDSD SEKKEKKDEN
//
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