RLUF_SHIFL
ID RLUF_SHIFL Reviewed; 290 AA.
AC Q83IR6;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Dual-specificity RNA pseudouridine synthase RluF {ECO:0000250|UniProtKB:P32684};
DE EC=5.4.99.- {ECO:0000250|UniProtKB:P32684};
DE EC=5.4.99.21 {ECO:0000250|UniProtKB:P32684};
DE AltName: Full=23S rRNA pseudouridine(2604) synthase {ECO:0000250|UniProtKB:P32684};
DE AltName: Full=Ribosomal large subunit pseudouridine synthase F {ECO:0000250|UniProtKB:P32684};
DE AltName: Full=rRNA pseudouridylate synthase F {ECO:0000250|UniProtKB:P32684};
DE AltName: Full=rRNA-uridine isomerase F {ECO:0000250|UniProtKB:P32684};
DE AltName: Full=tRNA(Tyr) pseudouridine(35) synthase {ECO:0000250|UniProtKB:P32684};
GN Name=rluF; OrderedLocusNames=SF4095, S3635;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Dual specificity enzyme that catalyzes the synthesis of
CC pseudouridine from uracil-2604 in 23S ribosomal RNA and from uracil-35
CC in the anticodon of tRNA(Tyr). {ECO:0000250|UniProtKB:P32684}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(2604) in 23S rRNA = pseudouridine(2604) in 23S rRNA;
CC Xref=Rhea:RHEA:38875, Rhea:RHEA-COMP:10093, Rhea:RHEA-COMP:10094,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.21;
CC Evidence={ECO:0000250|UniProtKB:P32684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(35) in tRNA(Tyr) = pseudouridine(35) in tRNA(Tyr);
CC Xref=Rhea:RHEA:60556, Rhea:RHEA-COMP:15607, Rhea:RHEA-COMP:15608,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000250|UniProtKB:P32684};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P32684}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family.
CC {ECO:0000305}.
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DR EMBL; AE005674; AAN45520.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18679.1; -; Genomic_DNA.
DR RefSeq; NP_709813.1; NC_004337.2.
DR RefSeq; WP_000936346.1; NZ_WPGW01000087.1.
DR AlphaFoldDB; Q83IR6; -.
DR SMR; Q83IR6; -.
DR STRING; 198214.SF4095; -.
DR PRIDE; Q83IR6; -.
DR EnsemblBacteria; AAN45520; AAN45520; SF4095.
DR EnsemblBacteria; AAP18679; AAP18679; S3635.
DR GeneID; 1027595; -.
DR GeneID; 58460517; -.
DR KEGG; sfl:SF4095; -.
DR KEGG; sfx:S3635; -.
DR PATRIC; fig|198214.7.peg.4826; -.
DR HOGENOM; CLU_024979_6_1_6; -.
DR OMA; NAHDKEY; -.
DR OrthoDB; 1037615at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0120159; F:rRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IEA:UniProt.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR Gene3D; 3.30.70.1560; -; 1.
DR Gene3D; 3.30.70.580; -; 1.
DR InterPro; IPR042092; PsdUridine_s_RsuA/RluB/E/F_cat.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR InterPro; IPR000748; PsdUridine_synth_RsuA/RluB/E/F.
DR InterPro; IPR018496; PsdUridine_synth_RsuA/RluB_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR InterPro; IPR020094; TruA/RsuA/RluB/E/F_N.
DR Pfam; PF00849; PseudoU_synth_2; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM00363; S4; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR00093; TIGR00093; 1.
DR PROSITE; PS01149; PSI_RSU; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome; RNA-binding; rRNA processing;
KW tRNA processing.
FT CHAIN 1..290
FT /note="Dual-specificity RNA pseudouridine synthase RluF"
FT /id="PRO_0000100021"
FT DOMAIN 7..72
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00182"
FT REGION 105..108
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:P32684"
FT REGION 187..190
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:P32684"
FT REGION 241..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 107
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P32684"
SQ SEQUENCE 290 AA; 32418 MW; 39B58C7CD3EAE3B6 CRC64;
MLPDSSVRLN KYISESGICS RREADRYIEQ GNVFLNGKRA TIGDQVKPGD IVKVNGQLIE
PREAEDLVLI ALNKPVGIVS TTEDGERDNI VDFVNHSKRV FPIGRLDKDS QGLIFLTNHG
DLVNKILRAG NDHEKEYLVT VDKPITDEFI RGMGAGVPIL GTVTKKCKVK KEAPFVFRIT
LVQGLNRQIR RMCEHFGYEV KKLERTRIMN VSLSGIPLGE WRDLTDDELI DLFKLIENSS
SEAKPKAKAK PKTAGIKRPV VKMEKTAEKG GRPASNGKRF TSPGRKKKGR
