TRUB_TROWT
ID TRUB_TROWT Reviewed; 377 AA.
AC Q820Y5;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 102.
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=TWT_087;
OS Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX NCBI_TaxID=203267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Twist;
RX PubMed=12902375; DOI=10.1101/gr.1474603;
RA Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA Claverie J.-M.;
RT "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT reduced genome.";
RL Genome Res. 13:1800-1809(2003).
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; AE014184; AAO44184.1; -; Genomic_DNA.
DR AlphaFoldDB; Q820Y5; -.
DR SMR; Q820Y5; -.
DR STRING; 203267.TWT_087; -.
DR EnsemblBacteria; AAO44184; AAO44184; TWT_087.
DR KEGG; twh:TWT_087; -.
DR eggNOG; COG0130; Bacteria.
DR HOGENOM; CLU_032087_0_0_11; -.
DR OMA; KVERSEM; -.
DR Proteomes; UP000002200; 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; Reference proteome; tRNA processing.
FT CHAIN 1..377
FT /note="tRNA pseudouridine synthase B"
FT /id="PRO_0000121936"
FT ACT_SITE 53
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ SEQUENCE 377 AA; 41136 MW; 9CF022715712E927 CRC64;
MLGKVERSEM YILFAMTQVL LVDKISGITS HTAVAKIRHL TGIKKIGHCG TLDPAACGLL
IMGCGTATRL IRYMSNLDKR YIATITLGTQ TTTDDSEGEI IYSAPKPSLD KITLESIGRA
AEKLSGTIKQ IPSAYSAIKV SGNRAYNLAR QGIIPKLNAR EVRVHWKFLG DFENNQVHVQ
ITCSSGTYVR ALARDMGKFL GVGGHLSYLK RLSIGPFHLH EIYREINKKE ATMSERTPSG
NTQGLTDNMA ISESDKHDCT EPGINCTELG IKDTCTALRE VHYTQGDTLS FTRLTALQAL
SRIYKPIEVS QKQADDLSCG RYISLGIDSK GPVCAVCKEN LIAVIQPVSA GLWRPETVLS
DNRKLNSNAA QDASGST