GenomeNet

Database: UniProt
Entry: A0A0F2NUY5_9GAMM
LinkDB: A0A0F2NUY5_9GAMM
Original site: A0A0F2NUY5_9GAMM 
ID   A0A0F2NUY5_9GAMM        Unreviewed;       195 AA.
AC   A0A0F2NUY5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=VR73_13300 {ECO:0000313|EMBL:KJS04950.1};
OS   Gammaproteobacteria bacterium BRH_c0.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1629722 {ECO:0000313|EMBL:KJS04950.1, ECO:0000313|Proteomes:UP000033581};
RN   [1] {ECO:0000313|EMBL:KJS04950.1, ECO:0000313|Proteomes:UP000033581}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c0 {ECO:0000313|EMBL:KJS04950.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-2015) 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:KJS04950.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LADM01000120; KJS04950.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2NUY5; -.
DR   STRING; 1629722.VR73_13300; -.
DR   PATRIC; fig|1629722.3.peg.354; -.
DR   Proteomes; UP000033581; 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   rRNA processing {ECO:0000256|PIRNR:PIRNR004553};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR004553};
KW   Transferase {ECO:0000256|PIRNR:PIRNR004553}.
SQ   SEQUENCE   195 AA;  21270 MW;  A920EE7BEE7ADF11 CRC64;
     MKATRNPPAD SSRNQLRIIA GKWRSRRLAF PDVEGLRPTG DRIRETLFNW IGPRIVDSRC
     LDAFAGSGAL GFEALSRGAA EVLLIENNAT AFRQLEASRQ LLDATGATLL RANTLTWLES
     ATANSSFDIV FLDPPFGSNL LDKILPLVVS KQLVAGDGLI YVETATDTSL SVPDGWCIRK
     EKRTGGIVCR LIGRT
//
DBGET integrated database retrieval system