ID   TRUB_RHOJR              Reviewed;         305 AA.
AC   Q0S212;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 104.
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};
GN   OrderedLocusNames=RHA1_ro06651;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(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; CP000431; ABG98424.1; -; Genomic_DNA.
DR   RefSeq; WP_011598477.1; NC_008268.1.
DR   AlphaFoldDB; Q0S212; -.
DR   SMR; Q0S212; -.
DR   STRING; 101510.RHA1_ro06651; -.
DR   EnsemblBacteria; ABG98424; ABG98424; RHA1_ro06651.
DR   KEGG; rha:RHA1_ro06651; -.
DR   PATRIC; fig|101510.16.peg.6711; -.
DR   eggNOG; COG0130; Bacteria.
DR   HOGENOM; CLU_032087_0_0_11; -.
DR   OMA; ELQFIRW; -.
DR   Proteomes; UP000008710; 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; IPR015225; tRNA_psdUridine_synth_fam2_C.
DR   InterPro; IPR014780; tRNA_psdUridine_synth_TruB.
DR   InterPro; IPR032819; TruB_C.
DR   PANTHER; PTHR13767; PTHR13767; 1.
DR   Pfam; PF09142; TruB_C; 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..305
FT                   /note="tRNA pseudouridine synthase B"
FT                   /id="PRO_1000084658"
FT   ACT_SITE        50
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ   SEQUENCE   305 AA;  32186 MW;  3BE61BFBBC0FC213 CRC64;
     MSAREKPSSG LVGAGLLIVD KDAGVTSHDV VARCRKLLGT RKVGHAGTLD PMATGVLVLG
     VERATKLLGF LALTTKAYTA TIRLGQATTT DDAEGEVVAS ADASGVTDEE IAAQVHTLTG
     DIQQIPSSVS AIKVDGRRAH ALIRAGEEFE LAPRSVTVSR FEVVARRTEG AFVDVDVEVE
     CSSGTYVRAL ARDLGIALIG VGGHLTSLRR TRVGPFTLEH ARTLEQLAEE PGVSLDIDAA
     AQTAFPHRQV DADEAESISQ GRWLEPIGIK GVYAAIDPSG HTIALLQERG RRASSVMVVR
     PATLR