ID N9GKH0_ACIHA Unreviewed; 182 AA.
AC N9GKH0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase D {ECO:0000256|ARBA:ARBA00013682, ECO:0000256|PIRNR:PIRNR004553};
DE EC=2.1.1.171 {ECO:0000256|ARBA:ARBA00012141, ECO:0000256|PIRNR:PIRNR004553};
GN ORFNames=F927_01938 {ECO:0000313|EMBL:ENW17584.1};
OS Acinetobacter haemolyticus CIP 64.3 = MTCC 9819.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217659 {ECO:0000313|EMBL:ENW17584.1, ECO:0000313|Proteomes:UP000017667};
RN [1] {ECO:0000313|EMBL:ENW17584.1, ECO:0000313|Proteomes:UP000017667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 64.3 {ECO:0000313|EMBL:ENW17584.1,
RC ECO:0000313|Proteomes:UP000017667};
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 haemolyticus CIP 64.3.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically methylates the guanine in position 966 of 16S
CC rRNA in the assembled 30S particle. {ECO:0000256|ARBA:ARBA00002649,
CC ECO:0000256|PIRNR:PIRNR004553}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(966) in 16S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(2)-methylguanosine(966) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:23548, Rhea:RHEA-COMP:10211, Rhea:RHEA-COMP:10212,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.171;
CC Evidence={ECO:0000256|ARBA:ARBA00000252,
CC ECO:0000256|PIRNR:PIRNR004553};
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmD family.
CC {ECO:0000256|ARBA:ARBA00005269, ECO:0000256|PIRNR:PIRNR004553}.
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:ENW17584.1}.
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DR EMBL; APQQ01000022; ENW17584.1; -; Genomic_DNA.
DR RefSeq; WP_005081910.1; NZ_KB849800.1.
DR AlphaFoldDB; N9GKH0; -.
DR GeneID; 56329766; -.
DR PATRIC; fig|1217659.3.peg.1903; -.
DR HOGENOM; CLU_075826_2_2_6; -.
DR Proteomes; UP000017667; Unassembled WGS sequence.
DR GO; GO:0052913; F:16S rRNA (guanine(966)-N(2))-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004398; RNA_MeTrfase_RsmD.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00095; 16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; 1.
DR PANTHER; PTHR43542; METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43542:SF1; METHYLTRANSFERASE; 1.
DR Pfam; PF03602; Cons_hypoth95; 1.
DR PIRSF; PIRSF004553; CHP00095; 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|PIRNR:PIRNR004553,
KW ECO:0000313|EMBL:ENW17584.1};
KW rRNA processing {ECO:0000256|PIRNR:PIRNR004553};
KW S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR004553};
KW Transferase {ECO:0000256|PIRNR:PIRNR004553, ECO:0000313|EMBL:ENW17584.1}.
SQ SEQUENCE 182 AA; 20806 MW; 0765B99574D337B2 CRC64;
MKNQLRIIGG EWKRRVLPFA SIEGLRPTPD RVRETLFNWL MWDIQNAQVL DLCSGSGALG
FEALSRGAAQ VVMIEPNTTQ ARYLKDNLQL LKAQNCRLII STAQQALNKL TEQFDVVFLD
PPYSLDLWQE LSTLADRLIK DNAYIYVEAD RELSQIQLPA SWQKIKETKA GQVRAALYQK
KI
//
