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Database: UniProt
Entry: C5BLM5_TERTT
LinkDB: C5BLM5_TERTT
Original site: C5BLM5_TERTT 
ID   C5BLM5_TERTT            Unreviewed;       191 AA.
AC   C5BLM5;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
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   Name=rsmD {ECO:0000313|EMBL:ACR13223.1};
GN   OrderedLocusNames=TERTU_0247 {ECO:0000313|EMBL:ACR13223.1};
OS   Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Teredinibacter.
OX   NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR13223.1, ECO:0000313|Proteomes:UP000009080};
RN   [1] {ECO:0000313|EMBL:ACR13223.1, ECO:0000313|Proteomes:UP000009080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080};
RX   PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA   Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA   Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA   Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA   Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA   Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA   Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA   Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT   "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT   endosymbiont of marine wood-boring bivalves (shipworms).";
RL   PLoS ONE 4:E6085-E6085(2009).
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}.
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DR   EMBL; CP001614; ACR13223.1; -; Genomic_DNA.
DR   RefSeq; WP_015819336.1; NC_012997.1.
DR   AlphaFoldDB; C5BLM5; -.
DR   STRING; 377629.TERTU_0247; -.
DR   KEGG; ttu:TERTU_0247; -.
DR   eggNOG; COG0742; Bacteria.
DR   HOGENOM; CLU_075826_2_2_6; -.
DR   OrthoDB; 9803017at2; -.
DR   Proteomes; UP000009080; Chromosome.
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:ACR13223.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009080};
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:ACR13223.1}.
SQ   SEQUENCE   191 AA;  20983 MW;  98CF027E9EFD5E1B CRC64;
     MQRQSKNSQK SSLRIIGGQW RGRKLSIADA EGLRPTGDRV RETLFNWLAP WLPGARCLDL
     FAGTGALGLE ALSRGAAHTT FIETNPHAAA TLCEHLNTLD CKQADVLRND GIAWLNSAAH
     TPYDIIFVDP PFAKDLWEQA LTSIERCAVA SAQALVYIET PVDHALNTPP NWQPLKSKTA
     GKVRFGLWQV A
//
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