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TRUB_THIDA
ID   TRUB_THIDA              Reviewed;         298 AA.
AC   Q3SKX3;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=tRNA pseudouridine synthase B {ECO:0000255|HAMAP-Rule:MF_01080};
DE            EC=5.4.99.25 {ECO:0000255|HAMAP-Rule:MF_01080};
DE   AltName: Full=tRNA pseudouridine(55) synthase {ECO:0000255|HAMAP-Rule:MF_01080};
DE            Short=Psi55 synthase {ECO:0000255|HAMAP-Rule:MF_01080};
DE   AltName: Full=tRNA pseudouridylate synthase {ECO:0000255|HAMAP-Rule:MF_01080};
DE   AltName: Full=tRNA-uridine isomerase {ECO:0000255|HAMAP-Rule:MF_01080};
GN   Name=truB {ECO:0000255|HAMAP-Rule:MF_01080}; OrderedLocusNames=Tbd_0695;
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=292415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25259;
RX   PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT   anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(2006).
CC   -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-55 in
CC       the psi GC loop of transfer RNAs. {ECO:0000255|HAMAP-Rule:MF_01080}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine(55) in tRNA = pseudouridine(55) in tRNA;
CC         Xref=Rhea:RHEA:42532, Rhea:RHEA-COMP:10101, Rhea:RHEA-COMP:10102,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.25;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01080};
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family. Type 1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01080}.
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DR   EMBL; CP000116; AAZ96648.1; -; Genomic_DNA.
DR   RefSeq; WP_011311207.1; NC_007404.1.
DR   AlphaFoldDB; Q3SKX3; -.
DR   SMR; Q3SKX3; -.
DR   STRING; 292415.Tbd_0695; -.
DR   EnsemblBacteria; AAZ96648; AAZ96648; Tbd_0695.
DR   KEGG; tbd:Tbd_0695; -.
DR   eggNOG; COG0130; Bacteria.
DR   HOGENOM; CLU_032087_0_3_4; -.
DR   OMA; ELQFIRW; -.
DR   OrthoDB; 1166299at2; -.
DR   Proteomes; UP000008291; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-UniRule.
DR   CDD; cd02573; PseudoU_synth_EcTruB; 1.
DR   Gene3D; 2.30.130.10; -; 1.
DR   HAMAP; MF_01080; TruB_bact; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR002501; PsdUridine_synth_N.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR036974; PUA_sf.
DR   InterPro; IPR014780; tRNA_psdUridine_synth_TruB.
DR   InterPro; IPR015240; tRNA_sdUridine_synth_fam1_C.
DR   InterPro; IPR032819; TruB_C.
DR   PANTHER; PTHR13767; PTHR13767; 1.
DR   Pfam; PF09157; TruB-C_2; 1.
DR   Pfam; PF16198; TruB_C_2; 1.
DR   Pfam; PF01509; TruB_N; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   TIGRFAMs; TIGR00431; TruB; 1.
PE   3: Inferred from homology;
KW   Isomerase; Reference proteome; tRNA processing.
FT   CHAIN           1..298
FT                   /note="tRNA pseudouridine synthase B"
FT                   /id="PRO_0000229390"
FT   ACT_SITE        45
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ   SEQUENCE   298 AA;  31607 MW;  9AF3D84CC6383B29 CRC64;
     MKPARQAVDG VLLLNKPVGI TSNAALQKAK WLLNAKKAGH TGTLDPFADG LLPLCFGEAT
     KFSAYLLDAD KRYRAILQLG VTTRTGDPEG EVLATREVRA TCADIRAALP AFVGEIEQIP
     PMHSALKHQG RPLYEYARAG VEIARAPRRV HIRALDLFKC APPRAVVDVQ CSAGTYVRTL
     AEDLGNALGC GAHLTALTRT ASGGFLLEQA HTLAELEATN AGARQALLLP ADCLVAHLPS
     VHLGETAAAS LRQGRSVPDA ADRRGLVRVY DGHGVFVGLA EAEAGKLVPR RLIATVQA
 
 
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