(data stored in SCRATCH zone)

SWISSPROT: D4YYJ4_SPHJU

ID   D4YYJ4_SPHJU            Unreviewed;       215 AA.
AC   D4YYJ4;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   08-MAY-2019, entry version 53.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase E {ECO:0000256|HAMAP-Rule:MF_01547};
DE            EC=2.1.1.166 {ECO:0000256|HAMAP-Rule:MF_01547};
DE   AltName: Full=23S rRNA Um2552 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01547};
DE   AltName: Full=rRNA (uridine-2'-O-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01547};
GN   Name=rlmE {ECO:0000256|HAMAP-Rule:MF_01547};
GN   Synonyms=ftsJ {ECO:0000256|HAMAP-Rule:MF_01547,
GN   ECO:0000313|EMBL:BAI95426.1}, rrmJ {ECO:0000256|HAMAP-Rule:MF_01547};
GN   OrderedLocusNames=SJA_C1-05920 {ECO:0000313|EMBL:BAI95426.1};
OS   Sphingobium japonicum (strain DSM 16413 / CCM 7287 / MTCC 6362 / UT26
OS   / NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95426.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95426.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S
RC   {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- FUNCTION: Specifically methylates the uridine in position 2552 of
CC       23S rRNA at the 2'-O position of the ribose in the fully assembled
CC       50S ribosomal subunit. {ECO:0000256|HAMAP-Rule:MF_01547}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-
CC         O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:42720, Rhea:RHEA-COMP:10202,
CC         Rhea:RHEA-COMP:10203, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:65315, ChEBI:CHEBI:74478;
CC         EC=2.1.1.166; Evidence={ECO:0000256|HAMAP-Rule:MF_01547};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01547}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RNA methyltransferase RlmE family.
CC       {ECO:0000256|HAMAP-Rule:MF_01547}.
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DR   EMBL; AP010803; BAI95426.1; -; Genomic_DNA.
DR   STRING; 452662.SJA_C1-05920; -.
DR   EnsemblBacteria; BAI95426; BAI95426; SJA_C1-05920.
DR   KEGG; sjp:SJA_C1-05920; -.
DR   eggNOG; ENOG4105F7M; Bacteria.
DR   eggNOG; COG0293; LUCA.
DR   HOGENOM; HOG000162366; -.
DR   KO; K02427; -.
DR   OMA; HRQTDHL; -.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   HAMAP; MF_01547; RNA_methyltr_E; 1.
DR   InterPro; IPR015507; rRNA-MeTfrase_E.
DR   InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF01728; FtsJ; 1.
DR   PIRSF; PIRSF005461; 23S_rRNA_mtase; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YYJ4.
DR   SWISS-2DPAGE; D4YYJ4.
KW   Cell cycle {ECO:0000313|EMBL:BAI95426.1};
KW   Cell division {ECO:0000313|EMBL:BAI95426.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01547};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01547,
KW   ECO:0000313|EMBL:BAI95426.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01547,
KW   ECO:0000256|SAAS:SAAS00319237};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01547,
KW   ECO:0000256|PIRSR:PIRSR005461-1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01547,
KW   ECO:0000313|EMBL:BAI95426.1}.
FT   DOMAIN       34    208       FtsJ. {ECO:0000259|Pfam:PF01728}.
FT   ACT_SITE    165    165       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01547, ECO:0000256|PIRSR:PIRSR005461-
FT                                1}.
FT   BINDING      66     66       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01547}.
FT   BINDING      68     68       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01547}.
FT   BINDING      85     85       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01547}.
FT   BINDING     101    101       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01547}.
FT   BINDING     125    125       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01547}.
SQ   SEQUENCE   215 AA;  23390 MW;  30C89B67C4076AF5 CRC64;
     MRVKTAKGRT AQSTRWLERQ LNDPYVRRAK AEGWRSRAAF KLIELDEKFH FLKGSRAVVD
     LGVAPGGWAQ VVRKLCPKAK VVGIDLLPTD PIPGVTLFQM DFMDDKAPAL LAEALGDAPD
     LVISDMAANT VGHAATDHLR TMGLVEAAAM FAVENLRKGG TFVAKVFAGG TDADLLAILK
     RHFTTIKHAK PPASRKGSVE WYVVAQGFKG RPEEG
//

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