GenomeNet

Database: UniProt
Entry: A0A0D0QQU4_9FIRM
LinkDB: A0A0D0QQU4_9FIRM
Original site: A0A0D0QQU4_9FIRM 
ID   A0A0D0QQU4_9FIRM        Unreviewed;       413 AA.
AC   A0A0D0QQU4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Ribosomal RNA small subunit methyltransferase B {ECO:0000313|EMBL:KIR03423.1};
GN   ORFNames=P261_02238 {ECO:0000313|EMBL:KIR03423.1};
OS   Lachnospiraceae bacterium TWA4.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1392836 {ECO:0000313|EMBL:KIR03423.1, ECO:0000313|Proteomes:UP000032079};
RN   [1] {ECO:0000313|EMBL:KIR03423.1, ECO:0000313|Proteomes:UP000032079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TWA4 {ECO:0000313|EMBL:KIR03423.1,
RC   ECO:0000313|Proteomes:UP000032079};
RX   PubMed=25495654;
RA   Gagen E.J., Wang J., Padmanabha J., Liu J., de Carvalho I., Liu J.,
RA   Webb R.I., Al Jassim R., Morrison M., Denman S.E., McSweeney C.S.;
RT   "Investigation of a new acetogen isolated from an enrichment of the tammar
RT   wallaby forestomach.";
RL   BMC Microbiol. 14:314-314(2014).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {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:KIR03423.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JPZU01000001; KIR03423.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0QQU4; -.
DR   STRING; 1392836.P261_02238; -.
DR   PATRIC; fig|1392836.3.peg.2527; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000032079; 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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.940.10; NusB-like; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR035926; NusB-like_sf.
DR   InterPro; IPR006027; NusB_RsmB_TIM44.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807:SF61; NOL1_NOP2_SUN FAMILY PROTEIN _ ANTITERMINATION NUSB DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF01029; NusB; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF48013; NusB-like; 1.
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:UP000032079};
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          132..412
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        349
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         227..233
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         251
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         278
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         296
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   413 AA;  46661 MW;  0E1D41A03E0EA2E3 CRC64;
     MINVRLIACN SIYEVLEEGK FSHLVMGRVT LDGQDRSFYT RLVKGTIERM ITLDYLINSY
     SKTKVHKMKP YIRTILRMSA YQIYYMDQIP DHAVCNEAVK LTVKKGYAGL KGFVNGVLRT
     LSRQKESVKL PDDLSIQYSI PKWLVDYMIK SFGLEIATKM CKASLEEEKL SVWSPNKHLE
     GEPLPYGLNG AYVTSLENQD VLVQDVSSMI AGEITSPKEG DVILDVCAAP GGKAVHAALS
     LNGTGKVIAC DLTSDKTALI EENKKRLKVE NLVTKVHDAR KLNEEWIEKA DIVIADLPCS
     GLGIIGRKPE IKYRMSFEQV EELAKLQREI LDVVWQYVKP GGRLVYSTCT WTPLENIKNY
     EWFLDNHPFI AESVNLYLPE ELHSNTTTHG YLNLFAGVHK CDGFFISLAV RNK
//
DBGET integrated database retrieval system