ID A0A1J0VD94_9GAMM Unreviewed; 318 AA.
AC A0A1J0VD94;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=BOX17_02955 {ECO:0000313|EMBL:APE30003.1};
OS Halomonas aestuarii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1897729 {ECO:0000313|EMBL:APE30003.1, ECO:0000313|Proteomes:UP000181985};
RN [1] {ECO:0000313|Proteomes:UP000181985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hb3 {ECO:0000313|Proteomes:UP000181985};
RA Koh H.-W., Rani S., Park S.-J.;
RT "Halolamina sediminis sp. nov., an extremely halophilic archaeon isolated
RT from solar salt.";
RL Submitted (NOV-2016) 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; CP018139; APE30003.1; -; Genomic_DNA.
DR RefSeq; WP_071941991.1; NZ_CP018139.1.
DR AlphaFoldDB; A0A1J0VD94; -.
DR KEGG; hsi:BOX17_02955; -.
DR Proteomes; UP000181985; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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:APE30003.1};
KW Ribonucleoprotein {ECO:0000313|EMBL:APE30003.1};
KW Ribosomal protein {ECO:0000313|EMBL:APE30003.1};
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:APE30003.1}.
FT DOMAIN 146..229
FT /note="Methyltransferase small"
FT /evidence="ECO:0000259|Pfam:PF05175"
SQ SEQUENCE 318 AA; 34796 MW; A46434416516C893 CRC64;
MAESSPDASS STLVLSDEAL TEGLITLRDC LRWAASEFHL AGLHYGHGTA SAWDEAVALS
LGALHLPWNV DPAVLEARLL PMERTRIVSL VRARIETRRP LPYLLGEAFF AELPFSVDER
VLIPRSPIAE LIEHGFAAWF PGEPPARVLD LCTGSGCIGI ATARYLPTCE VDLADISPEA
LEVARLNITR HDVGDRVRAV ESDLFAGLVG RRYDLIVSNP PYVDTRDLTT MPAEFRHEPA
LALGAGRDGL DIVRRILREA RDHLTDEGVL IVEVGNSDHH LEAAFPEVPF LWLEFERGGQ
GVFALTADEL DAHAASFA
//
