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Database: UniProt
Entry: M5D755_STEMA
LinkDB: M5D755_STEMA
Original site: M5D755_STEMA 
ID   M5D755_STEMA            Unreviewed;       258 AA.
AC   M5D755;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase D {ECO:0000256|ARBA:ARBA00013682};
DE            EC=2.1.1.171 {ECO:0000256|ARBA:ARBA00012141};
DE   AltName: Full=16S rRNA m2G966 methyltransferase {ECO:0000256|ARBA:ARBA00031268};
DE   AltName: Full=rRNA (guanine-N(2)-)-methyltransferase {ECO:0000256|ARBA:ARBA00033371};
GN   ORFNames=SMRA8_1959 {ECO:0000313|EMBL:CCP16054.1};
OS   Stenotrophomonas maltophilia RA8.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=1118157 {ECO:0000313|EMBL:CCP16054.1, ECO:0000313|Proteomes:UP000012177};
RN   [1] {ECO:0000313|EMBL:CCP16054.1, ECO:0000313|Proteomes:UP000012177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA8 {ECO:0000313|EMBL:CCP16054.1,
RC   ECO:0000313|Proteomes:UP000012177};
RA   Linke B., Adamek M., Schwartz T.;
RT   "Stenotrophomonas maltophilia SKK35 and RA8 Genome sequencing: Analysis and
RT   Comparison of Viurlence genes.";
RL   Submitted (JUL-2012) 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   -!- 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   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmD family.
CC       {ECO:0000256|ARBA:ARBA00005269}.
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:CCP16054.1}.
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DR   EMBL; CALM01000543; CCP16054.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5D755; -.
DR   Proteomes; UP000012177; 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   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:CCP16054.1};
KW   Transferase {ECO:0000313|EMBL:CCP16054.1}.
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   258 AA;  28287 MW;  BB43B7C1BF2CE008 CRC64;
     MDGATEPPWT DLRRPPQSDP PRHITGSQHL TLLRPLLRPL RVPAAGRPNY NPAHAEILEY
     LPPGAPMSGR GGNDGQVRII GGRWRNTRLP VPTLPGLRPS SDRVRETLFN WLMPRLGGAR
     VLDLFAGSGA LGLEAVSRGA AHATMVERDA QLGRNLTTAV AKLQATDQIT VVQSDAVRWL
     QGAPAQQADL VFIDPPFADG LWQDVLAQLP RHLAADAWLY LESPAGHVPV LPPEWLLHRE
     GSTREVRFAL YRRATATL
//
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