ID   PRMB_ALIF1              Reviewed;         310 AA.
AC   Q5E3U5;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=VF_1806;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW86301.1; -; Genomic_DNA.
DR   RefSeq; WP_005420259.1; NC_006840.2.
DR   RefSeq; YP_205189.1; NC_006840.2.
DR   AlphaFoldDB; Q5E3U5; -.
DR   SMR; Q5E3U5; -.
DR   STRING; 312309.VF_1806; -.
DR   EnsemblBacteria; AAW86301; AAW86301; VF_1806.
DR   GeneID; 64242092; -.
DR   KEGG; vfi:VF_1806; -.
DR   PATRIC; fig|312309.11.peg.1834; -.
DR   eggNOG; COG2890; Bacteria.
DR   HOGENOM; CLU_018398_5_1_6; -.
DR   OMA; IYYGHGT; -.
DR   OrthoDB; 1816476at2; -.
DR   Proteomes; UP000000537; 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; 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..310
FT                   /note="50S ribosomal protein L3 glutamine
FT                   methyltransferase"
FT                   /id="PRO_0000414183"
SQ   SEQUENCE   310 AA;  35327 MW;  B749C669EF501446 CRC64;
     MDKIFVEEAV AELHTLQDML RWTVSRFNAA GLFYGHGTDN AWDEAVQLVL PTLYLPIDVP
     AHVRESRLTS TERLRIVERV VRRINERIPT AYLTNKAWFC GLEFFVDERV LVPRSPIAEL
     IETQFEPWLT EEPTRIMDLC TGSGCIAIAC AHAFPNAEVD AIDISTDALM VAEQNVQDHG
     MEQQVFPIRS DLLRDIPKDQ YNFIVSNPPY VDEEDMNSLP EEFEHEPELG LAAGTDGLKL
     VRRILANAPD YLMDNGFLIC EVGNSMVHMM EQYPDIPFTW IEFAEGGHGV FMLTKQQLLD
     CADEFALYRD