ID A0A0R1H123_9LACO Unreviewed; 458 AA.
AC A0A0R1H123;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=tRNA and rRNA cytosine-C5-methylase {ECO:0000313|EMBL:KRK40332.1};
GN ORFNames=FC07_GL000963 {ECO:0000313|EMBL:KRK40332.1};
OS Loigolactobacillus bifermentans DSM 20003.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Loigolactobacillus.
OX NCBI_TaxID=1423726 {ECO:0000313|EMBL:KRK40332.1, ECO:0000313|Proteomes:UP000051461};
RN [1] {ECO:0000313|EMBL:KRK40332.1, ECO:0000313|Proteomes:UP000051461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20003 {ECO:0000313|EMBL:KRK40332.1,
RC ECO:0000313|Proteomes:UP000051461};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRK40332.1}.
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DR EMBL; AZDA01000016; KRK40332.1; -; Genomic_DNA.
DR RefSeq; WP_057903635.1; NZ_AZDA01000016.1.
DR AlphaFoldDB; A0A0R1H123; -.
DR STRING; 1423726.FC07_GL000963; -.
DR PATRIC; fig|1423726.3.peg.996; -.
DR OrthoDB; 9810297at2; -.
DR Proteomes; UP000051461; Unassembled WGS sequence.
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 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; IPR031341; Methyltr_RsmF_N.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
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; 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:UP000051461};
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 10..294
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 299..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 224
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 102..108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 126
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 171
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 458 AA; 51129 MW; 16F7D7DC7A6F8273 CRC64;
MLPEGFVKKY QQLLGAEAPA FFESFQQPRH KGFRINPLKP NPTEVALDLS RPVPYAKWGY
YGAVNGRQVD HQAGYVYSQE PSAMYVAAIA APQPGERVLD LCAAPGGKTT YLASFMQQQG
LLVSNEIMPK RARILAENVE RFGIQNAVIL NESPAHLAPR FPAFFDTILV DAPCSGEGMF
RKDPAAQAYW TPDYPAKCAT RQREIMTEAL KMVRPGGHLV YSTCTFSPEE DEQMMAWVLA
NYPEFRLQPI KRYPGMTAGR PDWADGNPEL AQAVRLFPHH IDGEGHFMAL LQRAATAEVP
VTKPKKKAKK GKQPRRKTLP DQDQVALWQA FEKNNLNCTL NGDLVVFGDQ LYLSPETLDL
TQLKVVRPGL HLGTLKRQRF EPSYALALAL KATAARHHLA LSAADYRAYV HGDTFKTVET
GKHWVLLTYQ AKTVGFGKLV NGTVKNFFPK GLRFEAAE
//
