ID   PRMB_XYLFT              Reviewed;         312 AA.
AC   Q87DS5;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=PD_0606;
OS   Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=183190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Temecula1 / ATCC 700964;
RX   PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA   Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA   Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA   Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA   Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA   Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA   Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA   Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA   Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA   Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA   Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA   Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA   Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT   "Comparative analyses of the complete genome sequences of Pierce's disease
RT   and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL   J. Bacteriol. 185:1018-1026(2003).
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; AE009442; AAO28478.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q87DS5; -.
DR   SMR; Q87DS5; -.
DR   EnsemblBacteria; AAO28478; AAO28478; PD_0606.
DR   KEGG; xft:PD_0606; -.
DR   HOGENOM; CLU_018398_5_1_6; -.
DR   OMA; IYYGHGT; -.
DR   Proteomes; UP000002516; 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; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..312
FT                   /note="50S ribosomal protein L3 glutamine
FT                   methyltransferase"
FT                   /id="PRO_0000088014"
SQ   SEQUENCE   312 AA;  34236 MW;  EEDA62A92B06E75A CRC64;
     MAVAMTPAAA DELHTIVDLI RYGASRFSEA GLTFGHSYDN ALDEATQLVL HALHLPPDLG
     PAYGQARLLR TEKECVLALF ERRVTERVPV AYLTGDAWFA GLNFKSDARA LVPRSPIAEL
     IQAGFEPWLA GRDVRHALDL CTGSGCIAIA MGHYNPHWRV DGSDISEDAL SLALENKVRL
     LAHNVELIKS DVFAGLVGRR YQLIVSNPPY VTDAETDALP QEYGYEPELG LRAGPDGLNL
     VLKILRDAPA HLDEEGLLIC EVGESEQQLV QLLPQVDFAW VEFKVGQMGV FAVECRELIA
     HHDRIAALAA ER