RLUF_ECOL6
ID RLUF_ECOL6 Reviewed; 290 AA.
AC Q8FB47;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=c4988;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN83414.1; -; Genomic_DNA.
DR RefSeq; WP_000936385.1; NC_004431.1.
DR AlphaFoldDB; Q8FB47; -.
DR SMR; Q8FB47; -.
DR STRING; 199310.c4988; -.
DR EnsemblBacteria; AAN83414; AAN83414; c4988.
DR KEGG; ecc:c4988; -.
DR eggNOG; COG1187; Bacteria.
DR HOGENOM; CLU_024979_6_1_6; -.
DR OMA; NAHDKEY; -.
DR BioCyc; ECOL199310:C4988-MON; -.
DR Proteomes; UP000001410; 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; RNA-binding; rRNA processing; tRNA processing.
FT CHAIN 1..290
FT /note="Dual-specificity RNA pseudouridine synthase RluF"
FT /id="PRO_0000100017"
FT DOMAIN 7..74
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; 32449 MW; 478D69FB767E4B44 CRC64;
MLPDSSVRLN KYISESGICS RREADRYIEQ GNVFLNGKRA TIGDQVKPGD VVKVNGQLIE
PRESEDLVLI ALNKPVGIVS TTEDGERDNI VDFVNHSKRV FPIGRLDKDS QGLIFLTNHG
DLVNKILRAG NDHEKEYLVT VDKPITDEFI RGMGAGVPIL GTVTKKCKVK KEAPFVFRIT
LVQGLNRQIR RMCEHFGYEV KKLERTRIMN VSLSGIPLGE WRDLTDDELI DLFKLIENSS
SEAKPKAKAK PKTVGIKRPV VKMEKTAEKG GRPASNGKRF TSPGRKKKGR
