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Database: UniProt
Entry: A0A1D9P1S6_9FIRM
LinkDB: A0A1D9P1S6_9FIRM
Original site: A0A1D9P1S6_9FIRM 
ID   A0A1D9P1S6_9FIRM        Unreviewed;       502 AA.
AC   A0A1D9P1S6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=RNA methylase NOL1/NOP2/sun family protein {ECO:0000313|EMBL:AOZ96567.1};
GN   ORFNames=bhn_I1534 {ECO:0000313|EMBL:AOZ96567.1};
OS   Butyrivibrio hungatei.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=185008 {ECO:0000313|EMBL:AOZ96567.1, ECO:0000313|Proteomes:UP000179284};
RN   [1] {ECO:0000313|Proteomes:UP000179284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB2003 {ECO:0000313|Proteomes:UP000179284};
RA   Palevich N., Kelly W.J., Leahy S.C., Altermann E., Rakonjac J.,
RA   Attwood G.T.;
RT   "The complete genome sequence of the rumen bacterium Butyrivibrio hungatei
RT   MB2003.";
RL   Submitted (OCT-2016) 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; CP017831; AOZ96567.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D9P1S6; -.
DR   KEGG; bhu:bhn_I1534; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000179284; Chromosome i.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
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; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
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}; Reference proteome {ECO:0000313|Proteomes:UP000179284};
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          23..323
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        236
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         114..120
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         138
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         165
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         183
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   502 AA;  56286 MW;  4B9D3B5D6055572B CRC64;
     MLPEKFKERM RAYLSEKEYE EFISSFDTDE RYQALRINEL KSDVLSAKEM LSYLGNNVPW
     EKTAFYYNED PANMVTPGKH PYHEAGLYYI QEPSAMSPVC FLDPKPGDKV LDLCAAPGGK
     TTQIASKMKG QGILITNEIN RDRARILSLN VERMGISNAL VTNEDSAKLA SVFEGYFDKI
     LVDAPCSGEG MFRKNDNAAD EWSMENVKTC ALRQEEILDN ASKMLLPGGR LVYSTCTFAA
     DENEESILKF LCAHSDFHVV KVDAFDGMDP GRAELISPEL RASLEAKDKA LFEKSLEQIQ
     YSIRLWPHKL KGEGHFLCVL ERDGELLKES SFVPGGRNIP AKPECIKPFE TFVMESLKFD
     KKTFELKRGN IYCRLESGQE LKGIIFMFGD QMYLAPGDMP SVMGLKCMRP GLHLGTLKKD
     RFEPSHALAL LLKKEDVNIA FDHDADSDDI KAYLNGQTIR AELSGQKGWA LVTASGLSIG
     WAKAAGGMLK NHYPKGLRIN YA
//
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