ID   PRMB_SHEON              Reviewed;         314 AA.
AC   Q8ECQ4;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   03-AUG-2022, entry version 100.
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=SO_3080;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN56087.2; -; Genomic_DNA.
DR   RefSeq; NP_718643.2; NC_004347.2.
DR   RefSeq; WP_011072977.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8ECQ4; -.
DR   SMR; Q8ECQ4; -.
DR   STRING; 211586.SO_3080; -.
DR   PaxDb; Q8ECQ4; -.
DR   KEGG; son:SO_3080; -.
DR   PATRIC; fig|1028802.3.peg.1451; -.
DR   eggNOG; COG2890; Bacteria.
DR   HOGENOM; CLU_018398_5_1_6; -.
DR   OrthoDB; 1816476at2; -.
DR   PhylomeDB; Q8ECQ4; -.
DR   BioCyc; SONE211586:G1GMP-2851-MON; -.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro.
DR   GO; GO:0018364; P:peptidyl-glutamine methylation; IBA:GO_Central.
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..314
FT                   /note="50S ribosomal protein L3 glutamine
FT                   methyltransferase"
FT                   /id="PRO_0000414181"
SQ   SEQUENCE   314 AA;  35242 MW;  8C2802FC09C15395 CRC64;
     MDKIFVDEAV TELRTIGDML RWAVSRFNDA NVYYGHGTDN AWDEAIALVF HALHLPEEIG
     QQVILSNLTS SEKHKIVELI IRRVRERLPV PYLTNKARFA GLEFYVDERV LVPRSPIAEM
     IANRFGPWLY GKPVNRILDL CTGSGCIAIA CAYEFDEAEV DALDISEDAL DVAQVNVETL
     GVMDRVFPMQ SDLFSAIPEG PQYDLIVSNP PYVDEEDIGD MPDEYHHEPA IGLASGRDGL
     DLTKRILANA AQYLTPTGIL VVEVGNSMVH LMEQFPEVPF TWVNFENGGD GVFVLTRDQL
     IEHQSLFAIY RDAQ