ID A0A142LL32_9PROT Unreviewed; 307 AA.
AC A0A142LL32;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Ribosomal protein uL3 glutamine methyltransferase {ECO:0000256|HAMAP-Rule:MF_02125};
DE Short=uL3 MTase {ECO:0000256|HAMAP-Rule:MF_02125};
DE EC=2.1.1.298 {ECO:0000256|HAMAP-Rule:MF_02125};
DE AltName: Full=N5-glutamine methyltransferase PrmB {ECO:0000256|HAMAP-Rule:MF_02125};
GN Name=prmB {ECO:0000256|HAMAP-Rule:MF_02125};
GN ORFNames=AEM42_12105 {ECO:0000313|EMBL:AMS32928.1};
OS Betaproteobacteria bacterium UKL13-2.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1690485 {ECO:0000313|EMBL:AMS32928.1, ECO:0000313|Proteomes:UP000075227};
RN [1] {ECO:0000313|Proteomes:UP000075227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Driscoll C.B.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Methylates ribosomal protein uL3 on a specific glutamine
CC residue. {ECO:0000256|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:0000256|HAMAP-Rule:MF_02125};
CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC family. PrmB subfamily. {ECO:0000256|HAMAP-Rule:MF_02125}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP012157; AMS32928.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A142LL32; -.
DR STRING; 1690485.AEM42_12105; -.
DR KEGG; beb:AEM42_12105; -.
DR PATRIC; fig|1690485.4.peg.2758; -.
DR Proteomes; UP000075227; 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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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_uL3_MTase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR NCBIfam; TIGR00536; hemK_fam; 1.
DR NCBIfam; TIGR03533; L3_gln_methyl; 1.
DR PANTHER; PTHR47806; 50S RIBOSOMAL PROTEIN L3 GLUTAMINE METHYLTRANSFERASE; 1.
DR PANTHER; PTHR47806:SF1; 50S RIBOSOMAL PROTEIN L3 GLUTAMINE METHYLTRANSFERASE; 1.
DR Pfam; PF05175; MTS; 1.
DR PIRSF; PIRSF037167; Mtase_YfcB_prd; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_02125,
KW ECO:0000313|EMBL:AMS32928.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075227};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_02125};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02125, ECO:0000313|EMBL:AMS32928.1}.
FT DOMAIN 137..218
FT /note="Methyltransferase small"
FT /evidence="ECO:0000259|Pfam:PF05175"
SQ SEQUENCE 307 AA; 34222 MW; 9F6FE9D8DA39B34E CRC64;
MTGDSGIYDV AQRELTTVRD LLRFAVSQFI EQKLFFGHGS SNAYDEAVYL VLNTLHLPLD
HLEPFLDARL TSVERDALLG VIERRVRERV PAAYLTHQAW LGDYKFYVDK RVLVPRSFIA
ELMRDDLAPW IENPRGVGRV LDLCTGSGCL AILAALSFPH ATVDAVDASL DALEVAKKNV
CDYALDDRIN LIASDMYESL GAKQYDIIIS NPPYVSATSM ERLPEEYRRE PEMALASGED
GLDHVRTIMA DAAKHLYANG LLVVEVGFNR EGVERVFSTL PLIWAETSVG DEVVFIIDRE
SLVAAQS
//