(data stored in SCRATCH zone)

SWISSPROT: D3UY65_XENBS

ID   D3UY65_XENBS            Unreviewed;       247 AA.
AC   D3UY65;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 52.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase J {ECO:0000256|HAMAP-Rule:MF_01523, ECO:0000256|SAAS:SAAS01088954};
DE            EC=2.1.1.242 {ECO:0000256|HAMAP-Rule:MF_01523, ECO:0000256|SAAS:SAAS01088959};
DE   AltName: Full=16S rRNA m2G1516 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01523};
DE   AltName: Full=rRNA (guanine-N(2)-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01523};
GN   Name=yhiQ {ECO:0000313|EMBL:CBJ79243.1};
GN   Synonyms=rsmJ {ECO:0000256|HAMAP-Rule:MF_01523};
GN   OrderedLocusNames=XBJ1_0092 {ECO:0000313|EMBL:CBJ79243.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79243.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|Proteomes:UP000002045};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ79243.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79243.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Specifically methylates the guanosine in position 1516
CC       of 16S rRNA. {ECO:0000256|HAMAP-Rule:MF_01523,
CC       ECO:0000256|SAAS:SAAS01088957}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine =
CC         H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:43220, Rhea:RHEA-COMP:10412,
CC         Rhea:RHEA-COMP:10413, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, ChEBI:CHEBI:74481;
CC         EC=2.1.1.242; Evidence={ECO:0000256|HAMAP-Rule:MF_01523,
CC         ECO:0000256|SAAS:SAAS01123258};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01523,
CC       ECO:0000256|SAAS:SAAS01088952}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmJ
CC       family. {ECO:0000256|HAMAP-Rule:MF_01523,
CC       ECO:0000256|SAAS:SAAS01088950}.
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DR   EMBL; FN667741; CBJ79243.1; -; Genomic_DNA.
DR   RefSeq; WP_012986713.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0092; -.
DR   EnsemblBacteria; CBJ79243; CBJ79243; XBJ1_0092.
DR   GeneID; 8829718; -.
DR   KEGG; xbo:XBJ1_0092; -.
DR   PATRIC; fig|406818.4.peg.82; -.
DR   eggNOG; ENOG4105FFN; Bacteria.
DR   eggNOG; ENOG410XPRJ; LUCA.
DR   HOGENOM; HOG000218236; -.
DR   KO; K15984; -.
DR   OMA; SRYDIYP; -.
DR   BioCyc; XBOV406818:XBJ1_RS00415-MONOMER; -.
DR   Proteomes; UP000002045; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008990; F:rRNA (guanine-N2-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01523; 16SrRNA_methyltr_J; 1.
DR   InterPro; IPR007536; 16SrRNA_methylTrfase_J.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   PANTHER; PTHR36112; PTHR36112; 1.
DR   Pfam; PF04445; SAM_MT; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UY65.
DR   SWISS-2DPAGE; D3UY65.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01523,
KW   ECO:0000256|SAAS:SAAS01088951};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01523,
KW   ECO:0000256|SAAS:SAAS01088953, ECO:0000313|EMBL:CBJ79243.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01523,
KW   ECO:0000256|SAAS:SAAS01088949};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01523,
KW   ECO:0000256|SAAS:SAAS01088958};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01523,
KW   ECO:0000256|SAAS:SAAS01088955, ECO:0000313|EMBL:CBJ79243.1}.
FT   REGION      101    102       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01523}.
FT   REGION      117    118       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01523}.
FT   REGION      153    154       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01523}.
FT   BINDING     171    171       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01523}.
SQ   SEQUENCE   247 AA;  27105 MW;  A9FEA6520E1B87CE CRC64;
     MKICLICEQG ADSSALSQLA ERWNLVHDED SVMALVLTPE RLELRKLDEP KLGGIYVDFV
     AGTMAHRRRF GGGRGEAVAK AVGIKKGYLP TVVDATAGLG RDAFVLASIG CQVRMLERHP
     VVAALLDDGL QRGYQNEEIG SWLKERMTLI HTSSITALTD ITPPPDVVYL DPMYPHRQKS
     ALVKKEMRVF QSLVGADEDA DGLLEPARAL AKRRVVVKRP DYAEPLAGAK ASAAITTKNH
     RFDIYPC
//

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