ID   PRMB_VIBA7              Reviewed;         310 AA.
AC   P39200; F7YND5;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 2.
DT   03-AUG-2022, entry version 103.
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}; Synonyms=yfcB;
GN   OrderedLocusNames=VAA_03441;
OS   Vibrio anguillarum (strain ATCC 68554 / 775) (Listonella anguillarum).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=882102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 68554 / 775;
RX   PubMed=21576332; DOI=10.1128/iai.05138-11;
RA   Naka H., Dias G.M., Thompson C.C., Dubay C., Thompson F.L., Crosa J.H.;
RT   "Complete genome sequence of the marine fish pathogen Vibrio anguillarum
RT   harboring the pJM1 virulence plasmid and genomic comparison with other
RT   virulent strains of V. anguillarum and V. ordalii.";
RL   Infect. Immun. 79:2889-2900(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 163-310.
RC   STRAIN=ATCC 68554 / 775;
RX   PubMed=8021209; DOI=10.1128/jb.176.14.4226-4234.1994;
RA   Chen Q., Actis L.A., Tolmasky M.E., Crosa J.H.;
RT   "Chromosome-mediated 2,3-dihydroxybenzoic acid is a precursor in the
RT   biosynthesis of the plasmid-mediated siderophore anguibactin in Vibrio
RT   anguillarum.";
RL   J. Bacteriol. 176:4226-4234(1994).
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA   Borodovsky M., Rudd K.E., Koonin E.V.;
RT   "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT   genome.";
RL   Nucleic Acids Res. 22:4756-4767(1994).
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}.
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DR   EMBL; CP002284; AEH32634.1; -; Genomic_DNA.
DR   EMBL; L29562; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; WP_013856325.1; NC_015633.1.
DR   AlphaFoldDB; P39200; -.
DR   SMR; P39200; -.
DR   EnsemblBacteria; AEH32634; AEH32634; VAA_03441.
DR   GeneID; 63946427; -.
DR   KEGG; van:VAA_03441; -.
DR   eggNOG; COG2890; Bacteria.
DR   HOGENOM; CLU_018398_5_1_6; -.
DR   OMA; IYYGHGT; -.
DR   Proteomes; UP000006800; Chromosome I.
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; IPR019874; Release_fac_Glu-N5_MeTfrase.
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.
DR   TIGRFAMs; TIGR03534; RF_mod_PrmC; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..310
FT                   /note="50S ribosomal protein L3 glutamine
FT                   methyltransferase"
FT                   /id="PRO_0000088011"
SQ   SEQUENCE   310 AA;  35164 MW;  2965B031A877CEF5 CRC64;
     MDKIFVEEAV SELHTLQDMI RWTVSRFNAA NLFYGHGTDN AWDEAVQLIL PTLYLPIDVP
     PHVLNSRLTG SERLRIVERV IKRINERTPI AYLTNKAWFC GLEFYVDERV LVPRSPIGEL
     IEAQFQPWLI DEPVRIMDLC TGSGCIAIAC AHAFPDAEVD AIDISTDALQ VAEQNIQDHG
     MEQQVFPIRS DLFRDLPKEK YDLIVSNPPY VDQEDMNSLP KEFKHEPELG LAAGTDGLKL
     VRRILANAAG YLTDNGILIC EVGNSMVHMM NQYDHIPFTW LEFENGGHGV FMLTRQQLVD
     CASDFALYID