ID N8W3N9_9GAMM Unreviewed; 336 AA.
AC N8W3N9; N9PXU6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=F892_01743 {ECO:0000313|EMBL:ENX22501.1}, F971_02560
GN {ECO:0000313|EMBL:ENU91468.1};
OS Acinetobacter vivianii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1776742 {ECO:0000313|EMBL:ENU91468.1, ECO:0000313|Proteomes:UP000013049};
RN [1] {ECO:0000313|EMBL:ENX22501.1, ECO:0000313|Proteomes:UP000013173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 2168 {ECO:0000313|EMBL:ENX22501.1,
RC ECO:0000313|Proteomes:UP000013173};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. NIPH 2168.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ENU91468.1, ECO:0000313|Proteomes:UP000013049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 758 {ECO:0000313|EMBL:ENU91468.1,
RC ECO:0000313|Proteomes:UP000013049};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. NIPH 758.";
RL Submitted (FEB-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:ENU91468.1}.
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DR EMBL; APPC01000018; ENU91468.1; -; Genomic_DNA.
DR EMBL; APRW01000009; ENX22501.1; -; Genomic_DNA.
DR RefSeq; WP_004772132.1; NZ_KB850134.1.
DR AlphaFoldDB; N8W3N9; -.
DR PATRIC; fig|1217706.3.peg.1684; -.
DR PATRIC; fig|1217712.3.peg.2466; -.
DR eggNOG; COG2890; Bacteria.
DR HOGENOM; CLU_018398_5_1_6; -.
DR OrthoDB; 9800643at2; -.
DR Proteomes; UP000013049; Unassembled WGS sequence.
DR Proteomes; UP000013173; Unassembled WGS sequence.
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:ENU91468.1};
KW Ribonucleoprotein {ECO:0000313|EMBL:ENU91468.1};
KW Ribosomal protein {ECO:0000313|EMBL:ENU91468.1};
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:ENU91468.1}.
FT DOMAIN 145..256
FT /note="Methyltransferase small"
FT /evidence="ECO:0000259|Pfam:PF05175"
SQ SEQUENCE 336 AA; 38042 MW; 6447A435B915D9B1 CRC64;
MERPTISPEH LQEAAENLVT IRDFVRFGVT ALRQYDAHLG QGTQDYFAES SALVLQTLSL
EWKADAEILD AKLLPSEKAE FLSLLERRIN DRIPTSYLLN LAYFFNKPFY VDERVLIPRS
PIAELIEQRF APYCLDENGR MLEALNNLPE NNNPKTPQRI LDMCTGSGCI AIALAYAYPD
AEVDATDISK EALEVASINT EHHDKQYQVA LLESDLFSKI PAENQYDLIV SNPPYVDAED
MADLPEEFLH EPELALAAGQ DGLDLVRKML AQAADYLTED GLIVIEVGNS EWAMRQNFNT
VDFHWLTFQR GGSGIFALTA EQCRRYKELF QQSVQN
//
