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Database: UniProt
Entry: S3PMB9_9GAMM
LinkDB: S3PMB9_9GAMM
Original site: S3PMB9_9GAMM 
ID   S3PMB9_9GAMM            Unreviewed;       191 AA.
AC   S3PMB9;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=F945_00847 {ECO:0000313|EMBL:EPF79956.1};
OS   Acinetobacter rudis CIP 110305.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=421052 {ECO:0000313|EMBL:EPF79956.1, ECO:0000313|Proteomes:UP000014568};
RN   [1] {ECO:0000313|EMBL:EPF79956.1, ECO:0000313|Proteomes:UP000014568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 110305 {ECO:0000313|EMBL:EPF79956.1,
RC   ECO:0000313|Proteomes:UP000014568};
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   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter rudis CIP 110305.";
RL   Submitted (JUN-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:EPF79956.1}.
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DR   EMBL; ATGI01000006; EPF79956.1; -; Genomic_DNA.
DR   RefSeq; WP_016655274.1; NZ_KE340351.1.
DR   AlphaFoldDB; S3PMB9; -.
DR   STRING; 632955.GCA_000829675_02111; -.
DR   PATRIC; fig|421052.3.peg.839; -.
DR   eggNOG; COG0742; Bacteria.
DR   HOGENOM; CLU_075826_2_2_6; -.
DR   OrthoDB; 9803017at2; -.
DR   Proteomes; UP000014568; 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:EPF79956.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014568};
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:EPF79956.1}.
SQ   SEQUENCE   191 AA;  21528 MW;  EB0900827A4E5457 CRC64;
     MTKPSVSKST NQLRIIGGEW KRRQLPFASI EGLRPTPDRI RETLFNWLMW DIQQSQVLDL
     CAGSGALGFE ALSRGAAHVT MIEPNSSQCQ FLKQNISLLK TEQCEVMHST AEQALTRLTD
     NQFDLVFLDP PYSLDLWSTL ASNVDPMIKK QGLIYVEADR DLSQLQLPAH WNLLKQTKAG
     VVRAGLYQKA I
//
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