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Database: UniProt
Entry: Q5JJE8
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ID   TRUB_THEKO              Reviewed;         338 AA.
AC   Q5JJE8;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Probable tRNA pseudouridine synthase B {ECO:0000255|HAMAP-Rule:MF_01081};
DE            EC=5.4.99.25 {ECO:0000255|HAMAP-Rule:MF_01081};
DE   AltName: Full=tRNA pseudouridine(55) synthase {ECO:0000255|HAMAP-Rule:MF_01081};
DE            Short=Psi55 synthase {ECO:0000255|HAMAP-Rule:MF_01081};
DE   AltName: Full=tRNA pseudouridylate synthase {ECO:0000255|HAMAP-Rule:MF_01081};
DE   AltName: Full=tRNA-uridine isomerase {ECO:0000255|HAMAP-Rule:MF_01081};
GN   Name=truB {ECO:0000255|HAMAP-Rule:MF_01081}; OrderedLocusNames=TK1509;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- FUNCTION: Could be responsible for synthesis of pseudouridine from
CC       uracil-55 in the psi GC loop of transfer RNAs. {ECO:0000255|HAMAP-
CC       Rule:MF_01081}.
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_01081};
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family. Type 2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01081}.
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DR   EMBL; AP006878; BAD85698.1; -; Genomic_DNA.
DR   RefSeq; WP_011250460.1; NC_006624.1.
DR   AlphaFoldDB; Q5JJE8; -.
DR   SMR; Q5JJE8; -.
DR   STRING; 69014.TK1509; -.
DR   EnsemblBacteria; BAD85698; BAD85698; TK1509.
DR   GeneID; 78448037; -.
DR   KEGG; tko:TK1509; -.
DR   PATRIC; fig|69014.16.peg.1469; -.
DR   eggNOG; arCOG00987; Archaea.
DR   HOGENOM; CLU_032087_3_0_2; -.
DR   InParanoid; Q5JJE8; -.
DR   OrthoDB; 35866at2157; -.
DR   PhylomeDB; Q5JJE8; -.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000495; P:box H/ACA RNA 3'-end processing; IBA:GO_Central.
DR   GO; GO:1990481; P:mRNA pseudouridine synthesis; IBA:GO_Central.
DR   GO; GO:0031118; P:rRNA pseudouridine synthesis; IBA:GO_Central.
DR   GO; GO:0031120; P:snRNA pseudouridine synthesis; IBA:GO_Central.
DR   GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-UniRule.
DR   CDD; cd02572; PseudoU_synth_hDyskerin; 1.
DR   CDD; cd21148; PUA_Cbf5; 1.
DR   Gene3D; 3.30.2350.10; Pseudouridine synthase; 1.
DR   Gene3D; 2.30.130.10; PUA domain; 1.
DR   HAMAP; MF_01081; TruB_arch; 1.
DR   InterPro; IPR012960; Dyskerin-like.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR002501; PsdUridine_synth_N.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR036974; PUA_sf.
DR   InterPro; IPR004802; tRNA_PsdUridine_synth_B_fam.
DR   InterPro; IPR026326; TruB_arch.
DR   InterPro; IPR032819; TruB_C.
DR   InterPro; IPR004521; Uncharacterised_CHP00451.
DR   NCBIfam; TIGR00425; CBF5; 1.
DR   NCBIfam; TIGR00451; unchar_dom_2; 1.
DR   PANTHER; PTHR23127; CENTROMERE/MICROTUBULE BINDING PROTEIN CBF5; 1.
DR   PANTHER; PTHR23127:SF0; H_ACA RIBONUCLEOPROTEIN COMPLEX SUBUNIT DKC1; 1.
DR   Pfam; PF08068; DKCLD; 1.
DR   Pfam; PF01472; PUA; 1.
DR   Pfam; PF16198; TruB_C_2; 1.
DR   Pfam; PF01509; TruB_N; 1.
DR   SMART; SM01136; DKCLD; 1.
DR   SMART; SM00359; PUA; 1.
DR   SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   PROSITE; PS50890; PUA; 1.
PE   3: Inferred from homology;
KW   Isomerase; Reference proteome; tRNA processing.
FT   CHAIN           1..338
FT                   /note="Probable tRNA pseudouridine synthase B"
FT                   /id="PRO_0000121970"
FT   DOMAIN          250..325
FT                   /note="PUA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01081"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01081"
SQ   SEQUENCE   338 AA;  38215 MW;  96230D6C1D75EC23 CRC64;
     MARDEVRRIL PADIKREVVV KDEKAETNPK WGFPPEKRPI EMHIQFGIIN LDKPPGPTSH
     EVVAWVKRIL NLNKAGHGGT LDPKVSGVLP VALERATRVV QALLPAGKEY VALMHLHGDV
     PEDKILAVMR EFQGEIIQRP PLRSAVKRRL RTRKVYYIDV LEIEGRDVLF RVGVEAGTYI
     RSLIHHIGLA LGVGAHMAEL RRTRSGPFKE DETLVTLHDL VDYYHFWKED GVEEYFRKAI
     QPMEKAVEHL PKVWIRDSAV AAVTHGADLA VPGVVKLHKG IKKGDLVAIM TLKDELVALG
     KAMMTTGEML QKSKGIAVDV DKVFMPRDWY PKLWKEKE
//
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