PRMB_FRATT
ID PRMB_FRATT Reviewed; 314 AA.
AC Q5NEL0;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=FTT_1617;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(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; AJ749949; CAG46250.1; -; Genomic_DNA.
DR RefSeq; WP_003022542.1; NZ_CP010290.1.
DR RefSeq; YP_170532.1; NC_006570.2.
DR AlphaFoldDB; Q5NEL0; -.
DR SMR; Q5NEL0; -.
DR STRING; 177416.FTT_1617; -.
DR DNASU; 3192421; -.
DR EnsemblBacteria; CAG46250; CAG46250; FTT_1617.
DR KEGG; ftu:FTT_1617; -.
DR eggNOG; COG2890; Bacteria.
DR OMA; IYYGHGT; -.
DR Proteomes; UP000001174; 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; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..314
FT /note="50S ribosomal protein L3 glutamine
FT methyltransferase"
FT /id="PRO_0000414179"
SQ SEQUENCE 314 AA; 35774 MW; 87C11901D226DEA5 CRC64;
MYSQQKQQDI INNLHTIRDY IRWSISEMTA NNVYFGHGSE SIWDEAVHLV LSAINVAHDI
DSNMVGSRLL TEEKKIIIDY VYQRACLRKP LPYILKKAWF AGMEFDIDER VIIPRSPIAE
LIRNEFSPWI NDIDDVTSVL DLCTGSGCIG IACSNVFEDA NITLVDISDD ALAVANHNIK
KHQLSDRVRA IKSDLFDNLH GQKFDLIVSN PPYVDKQDLD TMPHEYHYEP KLALEAGDDG
LDLAKRIILE ADKYMTENGV LIVEVGNSQY ALMEMCPDIP FTWLSFADGG DGVLLLTYDE
LVKYKDAFKK YFQK