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RLUF_SALTY
ID   RLUF_SALTY              Reviewed;         289 AA.
AC   Q8ZKL1;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=STM4193;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AE006468; AAL23017.1; -; Genomic_DNA.
DR   RefSeq; NP_463058.1; NC_003197.2.
DR   RefSeq; WP_000954611.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZKL1; -.
DR   SMR; Q8ZKL1; -.
DR   STRING; 99287.STM4193; -.
DR   PaxDb; Q8ZKL1; -.
DR   EnsemblBacteria; AAL23017; AAL23017; STM4193.
DR   GeneID; 1255719; -.
DR   KEGG; stm:STM4193; -.
DR   PATRIC; fig|99287.12.peg.4407; -.
DR   HOGENOM; CLU_024979_6_1_6; -.
DR   OMA; NAHDKEY; -.
DR   PhylomeDB; Q8ZKL1; -.
DR   BioCyc; SENT99287:STM4193-MON; -.
DR   Proteomes; UP000001014; 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..289
FT                   /note="Dual-specificity RNA pseudouridine synthase RluF"
FT                   /id="PRO_0000100020"
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..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        107
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P32684"
SQ   SEQUENCE   289 AA;  32350 MW;  DEBD4688994A615E CRC64;
     MLTDTSTRLN KYISESGICS RREADRFIEQ GNVFINGKRA AIGDQVVAGD IVKVNGRLIE
     PREADDLVLI ALNKPVGIVS TTEDGERDNI VDFVNHSKRI FPIGRLDKDS QGLIFLTNHG
     DLVNKILRAG NDHEKEYLVT VDKPITDEFI RGMGAGVPIL GTVTKKCKVK KEAPFVFRIT
     LVQGLNRQIR RMCEYFGYEV TKLERTRIMN VSLSGIPLGE WRDLTDDELI DLFKLIERSS
     SEAKPKAKAK PKTTGIKRPV VAIEKSNEKA RPTSSGKRFT SPGRKKKGR
 
 
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