TRUB_RICAH
ID TRUB_RICAH Reviewed; 293 AA.
AC A8GNM0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=A1C_03570;
OS Rickettsia akari (strain Hartford).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=293614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hartford;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia akari.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000847; ABV74995.1; -; Genomic_DNA.
DR RefSeq; WP_012149627.1; NC_009881.1.
DR AlphaFoldDB; A8GNM0; -.
DR SMR; A8GNM0; -.
DR STRING; 293614.A1C_03570; -.
DR EnsemblBacteria; ABV74995; ABV74995; A1C_03570.
DR KEGG; rak:A1C_03570; -.
DR eggNOG; COG0130; Bacteria.
DR HOGENOM; CLU_032087_0_3_5; -.
DR OMA; ELQFIRW; -.
DR Proteomes; UP000006830; 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 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; IPR032819; TruB_C.
DR PANTHER; PTHR13767; PTHR13767; 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..293
FT /note="tRNA pseudouridine synthase B"
FT /id="PRO_1000084659"
FT ACT_SITE 40
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ SEQUENCE 293 AA; 32752 MW; 5FDE417B0B27AEBB CRC64;
MSNYWLNIYK PGGISSAKLV SMVKQILGKK VKVGHAGTLD VEAEGILPIA VGEATKLIQL
LIDSRKTYIF TIKFGLQTDS GDYTGTVIAT KNYIPSQEEA YTVCSKFIGK VTQIPPAFSA
LKVNGVRAYK FAREGKEVEL KPRNITIYNL KCLNFDKKNA IAIYYTECSK GTYIRTLAED
LALSLQSLGF VIELRRTQVG IFKAENAIRI KSPDEITKSF LEEKSIKIEA ILDDILVLDA
TDSQAQQIKY GQKCIFDYED DISLLWVRYK GTLLAIGSLN KNCFNSLRVF NVL