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Database: UniProt
Entry: A0A0R1KIU6_9LACO
LinkDB: A0A0R1KIU6_9LACO
Original site: A0A0R1KIU6_9LACO 
ID   A0A0R1KIU6_9LACO        Unreviewed;       450 AA.
AC   A0A0R1KIU6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Fmu (Sun) domain-containing protein {ECO:0000313|EMBL:KRK80497.1};
GN   ORFNames=FD03_GL001921 {ECO:0000313|EMBL:KRK80497.1};
OS   Companilactobacillus nodensis DSM 19682 = JCM 14932 = NBRC 107160.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Companilactobacillus.
OX   NCBI_TaxID=1423775 {ECO:0000313|EMBL:KRK80497.1, ECO:0000313|Proteomes:UP000051248};
RN   [1] {ECO:0000313|EMBL:KRK80497.1, ECO:0000313|Proteomes:UP000051248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19682 {ECO:0000313|EMBL:KRK80497.1,
RC   ECO:0000313|Proteomes:UP000051248};
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|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}.
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:KRK80497.1}.
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DR   EMBL; AZDZ01000003; KRK80497.1; -; Genomic_DNA.
DR   RefSeq; WP_025024453.1; NZ_BCWC01000002.1.
DR   AlphaFoldDB; A0A0R1KIU6; -.
DR   STRING; 1423775.FD03_GL001921; -.
DR   PATRIC; fig|1423775.4.peg.1959; -.
DR   eggNOG; COG0144; Bacteria.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000051248; Unassembled WGS sequence.
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   GO; GO:0006396; P:RNA processing; 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; IPR011023; Nop2p.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR031340; RsmF_methylt_CI.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00446; nop2p; 1.
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};
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          1..297
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        227
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         105..111
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         129
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         174
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   450 AA;  51598 MW;  685E638AFC700735 CRC64;
     MNVELSTDFK DKYRKLMGER ADKFFAAIET DSRNSFRINP LKPNYKNVNV DLSEPIPYSD
     VGYYGDIDGN SIDHQAGYLY SQEPSAMYVA EVLDPQKTDK VLDLCAAPGS KSTYIATKMD
     SQGLLVTNEI NNKRARILSS NIERMGITNA VVTNNSPKDF EKKFEGYFDR ILVDAPCSGE
     GMFRKDPESV KYWSLDYVEQ CANRQRHILD SAFNLLKPGG TLVYSTCTFS PEENEENIDH
     FLSQHEEMSL SEIKKYPGME DGKPEWGNDN QELTKALRMF PDEFEGEGHF MCKMTKSGAA
     AKNREKNVST GIGKEEVKLL DKFAKANLID LAENNWFKVS DFLYQAASLD NRFKSLHVLR
     NGLKLGEFKK NRFEPDIAWI LAIEPTKLKA IYKLNDDQFE TYMYGESIIL TDKPEFDNKW
     IGLSYQDKLF SWGRYSNNQI KNVYPKGLRR
//
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