ID   PRMB_PASMU              Reviewed;         313 AA.
AC   Q9CNN7;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=50S ribosomal protein L3 glutamine methyltransferase {ECO:0000255|HAMAP-Rule:MF_02125};
DE            Short=L3 MTase {ECO:0000255|HAMAP-Rule:MF_02125};
DE            EC=2.1.1.298 {ECO:0000255|HAMAP-Rule:MF_02125};
DE   AltName: Full=N5-glutamine methyltransferase PrmB {ECO:0000255|HAMAP-Rule:MF_02125};
GN   Name=prmB {ECO:0000255|HAMAP-Rule:MF_02125}; OrderedLocusNames=PM0390;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Specifically methylates the 50S ribosomal protein L3 on a
CC       specific glutamine residue. {ECO:0000255|HAMAP-Rule:MF_02125}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutaminyl-[ribosomal protein uL3] + S-adenosyl-L-methionine
CC         = H(+) + N(5)-methyl-L-glutaminyl-[ribosomal protein uL3] + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:45020, Rhea:RHEA-COMP:11063,
CC         Rhea:RHEA-COMP:11064, ChEBI:CHEBI:15378, ChEBI:CHEBI:30011,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61891;
CC         EC=2.1.1.298; Evidence={ECO:0000255|HAMAP-Rule:MF_02125};
CC   -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC       family. PrmB subfamily. {ECO:0000255|HAMAP-Rule:MF_02125}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK02474.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE004439; AAK02474.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_005753769.1; NC_002663.1.
DR   AlphaFoldDB; Q9CNN7; -.
DR   SMR; Q9CNN7; -.
DR   STRING; 747.DR93_1165; -.
DR   EnsemblBacteria; AAK02474; AAK02474; PM0390.
DR   KEGG; pmu:PM0390; -.
DR   PATRIC; fig|272843.6.peg.403; -.
DR   HOGENOM; CLU_018398_5_1_6; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro.
DR   GO; GO:0018364; P:peptidyl-glutamine methylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_02125; L3_methyltr_PrmB; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR004556; HemK-like.
DR   InterPro; IPR017127; Ribosome_L3_Gln-N5_MeTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   Pfam; PF05175; MTS; 1.
DR   PIRSF; PIRSF037167; Mtase_YfcB_prd; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00536; hemK_fam; 1.
DR   TIGRFAMs; TIGR03533; L3_gln_methyl; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..313
FT                   /note="50S ribosomal protein L3 glutamine
FT                   methyltransferase"
FT                   /id="PRO_0000088009"
SQ   SEQUENCE   313 AA;  35735 MW;  348DC1D22C5C2046 CRC64;
     MTHNQELIET IIADQVHQEL HSIQDFLRWT YSTFNRSDIY YGHGYNNAWD EALQLILTTL
     ALPIDFPNEY YAAHLTRSEK EVLLRLIIQR LEKRIPVAYL THQAWFCGLN FYVDERVIVP
     RSPISALIQE GFAPLLPQEP KRILDMCTGS GCIAIACAER FPEAEVDAVD LSSDALDVAQ
     INIERHNMLD RVYPIQSDLF HDLAKDQYDL IVANPPYVDL EDLSDMPAEF HHEPEMALGS
     GVDGLEITKK ILYAAPDYLT EQGVLVCEVG NSMVHLIEQY PDVPFNWVEL KNGGVGVFAL
     TQAELMQYRH LFQ