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Database: UniProt
Entry: A0A142LL32_9PROT
LinkDB: A0A142LL32_9PROT
Original site: A0A142LL32_9PROT 
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}.
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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
//
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