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TRUB_BRUO2
ID   TRUB_BRUO2              Reviewed;         324 AA.
AC   A5VTB4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=BOV_2079;
OS   Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=444178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25840 / 63/290 / NCTC 10512;
RX   PubMed=19436743; DOI=10.1371/journal.pone.0005519;
RA   Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M.,
RA   de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T.,
RA   Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S.,
RA   Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.;
RT   "Genome degradation in Brucella ovis corresponds with narrowing of its host
RT   range and tissue tropism.";
RL   PLoS ONE 4:E5519-E5519(2009).
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; CP000708; ABQ61775.1; -; Genomic_DNA.
DR   RefSeq; WP_002965229.1; NC_009505.1.
DR   AlphaFoldDB; A5VTB4; -.
DR   SMR; A5VTB4; -.
DR   EnsemblBacteria; ABQ61775; ABQ61775; BOV_2079.
DR   GeneID; 45125410; -.
DR   KEGG; bov:BOV_2079; -.
DR   HOGENOM; CLU_032087_0_3_5; -.
DR   OMA; ELQFIRW; -.
DR   PhylomeDB; A5VTB4; -.
DR   Proteomes; UP000006383; Chromosome I.
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   HAMAP; MF_01080; TruB_bact; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR002501; PsdUridine_synth_N.
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   TIGRFAMs; TIGR00431; TruB; 1.
PE   3: Inferred from homology;
KW   Isomerase; tRNA processing.
FT   CHAIN           1..324
FT                   /note="tRNA pseudouridine synthase B"
FT                   /id="PRO_1000084556"
FT   REGION          87..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        49
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ   SEQUENCE   324 AA;  35595 MW;  850AF77186777988 CRC64;
     MARRGKKKGR PISGWVIFDK PKGMGSTEAV SKIKWLFSAE KAGHAGTLDP LASGMLPIAL
     GEATKTVPYV MDGTKVYRFT VTWGEERSTD DLEGQPTKTS DKRPSREEVE ALLPDYTGVI
     SQVPPQFSAI KIDGERAYDL AREGETVEIP AREVEIDRLE IVGFPDADRT EFEVECSKGT
     YVRSLARDMG RDLGCYGHIS DLRRVEVAPF TDEDMVTLAK LEAVWPPLPP KDEDGNVIEP
     APRRDFSALD ALVIDTGAAL DCLPQVPLSD DQAQRVRLGN PVILRGRDAP LEADEACVTT
     RGKLLAIGYI EHGQFKPKRV FTAG
 
 
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