PRMB_BURPS
ID PRMB_BURPS Reviewed; 307 AA.
AC Q63SZ9;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=BPSL2172;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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; BX571965; CAH36174.1; -; Genomic_DNA.
DR RefSeq; WP_004192731.1; NZ_CP009538.1.
DR RefSeq; YP_108767.1; NC_006350.1.
DR AlphaFoldDB; Q63SZ9; -.
DR SMR; Q63SZ9; -.
DR STRING; 272560.BPSL2172; -.
DR EnsemblBacteria; CAH36174; CAH36174; BPSL2172.
DR GeneID; 56595956; -.
DR KEGG; bps:BPSL2172; -.
DR PATRIC; fig|272560.51.peg.3278; -.
DR eggNOG; COG2890; Bacteria.
DR OMA; IYYGHGT; -.
DR Proteomes; UP000000605; Chromosome 1.
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..307
FT /note="50S ribosomal protein L3 glutamine
FT methyltransferase"
FT /id="PRO_0000414178"
SQ SEQUENCE 307 AA; 33508 MW; C05E7C949A479586 CRC64;
MTTSPTPFKT VRDLVRHAVS RFSQAKLAFG HGSDNAFDEA VYLVLHTLHL PLDTLEPFLD
ARLAPDEIDA VLAVIERRAT ERVPAAYLTR EAWMHGHRFY VDERVIVPRS FIGELLDDGL
QPYVEDPELV GSVLELCTGS GCLAILAALA FPNASVDAVD LSADALAVAK INRDNYGLDE
RIALYHGDLY APLPQFKWID PAQRYDVIIA NPPYVNAGSM AELPAEYRHE PEMALAGGAD
GMDIVRRIIG EARRWLQDDG VLVVEIGNER ANVEAAFGGL ELVWLPTSAG DGSVFLIHAS
ELPAVAG