TRUB_PYRCJ
ID TRUB_PYRCJ Reviewed; 333 AA.
AC A3MS77;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=Pcal_0054;
OS Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=410359;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21063 / JCM 11548 / VA1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000561; ABO07494.1; -; Genomic_DNA.
DR AlphaFoldDB; A3MS77; -.
DR SMR; A3MS77; -.
DR STRING; 410359.Pcal_0054; -.
DR EnsemblBacteria; ABO07494; ABO07494; Pcal_0054.
DR KEGG; pcl:Pcal_0054; -.
DR eggNOG; arCOG00987; Archaea.
DR HOGENOM; CLU_032087_3_0_2; -.
DR OMA; GPFKEDE; -.
DR Proteomes; UP000001431; 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 Gene3D; 2.30.130.10; -; 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 PANTHER; PTHR23127; PTHR23127; 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; SSF55120; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00425; CBF5; 1.
DR TIGRFAMs; TIGR00451; unchar_dom_2; 1.
DR PROSITE; PS50890; PUA; 1.
PE 3: Inferred from homology;
KW Isomerase; tRNA processing.
FT CHAIN 1..333
FT /note="Probable tRNA pseudouridine synthase B"
FT /id="PRO_1000084725"
FT DOMAIN 238..313
FT /note="PUA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01081"
FT ACT_SITE 71
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01081"
SQ SEQUENCE 333 AA; 37192 MW; BC9B13F5A724DAC1 CRC64;
MKCGSREVFV KLEEGTNPQW GKPPSSRSAE EHIRYSFLIL DKPRGPTSHE VAAWVKKILG
VERAGHSGTL DPKVSGVLPV AVAEGTKVLM ALSRADKVYI AVAKFHGDVD VENLRRVLQE
LQGEIYQKPP LRSAVKRQLR TRRVYSLELL ELDGRYAVLK MHVEAGTYAR KLIHDLGEIL
GVGANMRELR RVAVSCFTED EAVTLQDLAD AYYIWKKYGD DTYLRRVLLP IEEIARPLPK
IWVRDSAVDA LCNGAPLAAP GVAKFEHPFS RGDLVAYFTL KGELIGIGRA LVDSEEVKKM
EKGLVARTDR VVMPRGTYPP MWRRGGKSFK SGT