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Database: UniProt
Entry: L0ECT1_THECK
LinkDB: L0ECT1_THECK
Original site: L0ECT1_THECK 
ID   L0ECT1_THECK            Unreviewed;       521 AA.
AC   L0ECT1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=tRNA/rRNA cytosine-C5-methylase {ECO:0000313|EMBL:AGA57607.1};
GN   OrderedLocusNames=Theco_1452 {ECO:0000313|EMBL:AGA57607.1};
OS   Thermobacillus composti (strain DSM 18247 / JCM 13945 / KWC4).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Thermobacillus.
OX   NCBI_TaxID=717605 {ECO:0000313|EMBL:AGA57607.1, ECO:0000313|Proteomes:UP000010795};
RN   [1] {ECO:0000313|Proteomes:UP000010795}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18247 / JCM 13945 / KWC4
RC   {ECO:0000313|Proteomes:UP000010795};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Anderson I.,
RA   Woyke T.;
RT   "Complete sequence of chromosome of Thermobacillus composti KWC4.";
RL   Submitted (JAN-2012) 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; CP003255; AGA57607.1; -; Genomic_DNA.
DR   RefSeq; WP_015254362.1; NC_019897.1.
DR   AlphaFoldDB; L0ECT1; -.
DR   STRING; 717605.Theco_1452; -.
DR   KEGG; tco:Theco_1452; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG3270; Bacteria.
DR   HOGENOM; CLU_005316_6_1_9; -.
DR   OMA; PQDNDTE; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000010795; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd21147; RsmF_methylt_CTD1; 1.
DR   Gene3D; 2.30.130.60; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR031341; Methyltr_RsmF_N.
DR   InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR   InterPro; IPR027391; Nol1_Nop2_Fmu_2.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR031340; RsmF_methylt_CI.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807:SF30; 28S RRNA (CYTOSINE(4447)-C(5))-METHYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF17125; Methyltr_RsmF_N; 1.
DR   Pfam; PF13636; Methyltranf_PUA; 1.
DR   Pfam; PF17126; RsmF_methylt_CI; 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}; Reference proteome {ECO:0000313|Proteomes:UP000010795};
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..312
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          316..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        235
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         113..119
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         182
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   521 AA;  57376 MW;  8D20B1FD2CC412DB CRC64;
     MTVRLPELFV ARMRTLLGDE FDDWLASYAA PRRYGLRVNT LKTDGESYRM RSPLSAGLKP
     VPWAEAGYYY SEEDRPGKHP HYHAGLYYIQ EPSAMAPAEL LNVQPGHRVL DLCAAPGGKS
     SQIAAKLKGH GLLVANDNAR ERTKALARNL ELAGVRNAVV LNEEPERLVP VFRAFFDRIL
     VDAPCSGEGM FRKDESMIAD WLRHPAAHWT SMQREILRHA AEMLAPGGVL VYSTCTFSPE
     ENEERIAELL AERPDFEVVP VPPAHGWAPG RPDWVSLEGI EHRHVEAVAG TVRLWPHRIE
     GEGHYAAVLR RQGGDSPGLN VGVAPQDPAE TSGSGKPDRP RLKTRPNAGR RGNGGKAGKR
     GHAMSGQEAD PTEVWRSFRA EVLPGLGDLP GRLIAVGEKL YAQPAGVPDL SGLRVVRHGW
     LLGEARRGRF APSQALAMGL AAEDAARRVE YGADEPEALK YLKGETLPLE PERLNLRPVE
     DGRQPDEAGY ALVCIDGYPV GWGKLRDGLL INERAPGWRW M
//
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