ID A0A166WQF6_9GAMM Unreviewed; 311 AA.
AC A0A166WQF6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=N475_02745 {ECO:0000313|EMBL:KZN37751.1};
OS Pseudoalteromonas luteoviolacea DSM 6061.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1365250 {ECO:0000313|EMBL:KZN37751.1, ECO:0000313|Proteomes:UP000076643};
RN [1] {ECO:0000313|EMBL:KZN37751.1, ECO:0000313|Proteomes:UP000076643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6061 {ECO:0000313|EMBL:KZN37751.1,
RC ECO:0000313|Proteomes:UP000076643};
RA Vynne N.G., Mansson M., Gram L.;
RT "Comparative Genomic and Metabolomic Analysis of Twelve Strains of
RT Pseudoalteromonas luteoviolacea.";
RL Submitted (JUL-2013) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZN37751.1}.
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DR EMBL; AUYB01000103; KZN37751.1; -; Genomic_DNA.
DR RefSeq; WP_063355188.1; NZ_AUYB01000103.1.
DR AlphaFoldDB; A0A166WQF6; -.
DR STRING; 43657.S4054249_15735; -.
DR PATRIC; fig|1365250.3.peg.2772; -.
DR Proteomes; UP000076643; Unassembled WGS sequence.
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; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 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:KZN37751.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076643};
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:KZN37751.1}.
FT DOMAIN 140..222
FT /note="Methyltransferase small"
FT /evidence="ECO:0000259|Pfam:PF05175"
SQ SEQUENCE 311 AA; 34934 MW; 655CE968184AF350 CRC64;
MSELAITNEI AEEAYRDLVT MQDWLRWTTS QFVANGLFYG HGTDNPWDEA VNLLLPTLNL
PVDAPKDLMQ SRLTGTEKKR LVEVIKLRIE QRIPVPYLTN QAWFAGMPFY VDERVLVPRS
PFAELITKQF TPWVQSPNEV TRILDMCTGS ACIAIALAKY FDNAQVDAVD ISFDALAVAE
MNIHDHMMDE RVFAIQSDVF SGVPGQKYDL IVANPPYVDA EDMADLPDEF HHEPELGLAS
GDDGLDVTRV LLRDAAEHLT DNGILFVEVG NSMVHMDALY PGAPFTWLEF EKGGLGVFMI
SKQELVAYFN D
//
