TRUB_RICRS
ID TRUB_RICRS Reviewed; 345 AA.
AC A8GS98;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=A1G_03780;
OS Rickettsia rickettsii (strain Sheila Smith).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=392021;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheila Smith;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia rickettsii.";
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; CP000848; ABV76273.1; -; Genomic_DNA.
DR RefSeq; WP_012150854.1; NC_009882.1.
DR AlphaFoldDB; A8GS98; -.
DR SMR; A8GS98; -.
DR EnsemblBacteria; ABV76273; ABV76273; A1G_03780.
DR GeneID; 45539236; -.
DR KEGG; rri:A1G_03780; -.
DR HOGENOM; CLU_032087_0_3_5; -.
DR OMA; ELQFIRW; -.
DR Proteomes; UP000006832; 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; IPR005728; Rickett_RPE.
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; TIGR01045; RPE1; 1.
DR TIGRFAMs; TIGR00431; TruB; 1.
PE 3: Inferred from homology;
KW Isomerase; tRNA processing.
FT CHAIN 1..345
FT /note="tRNA pseudouridine synthase B"
FT /id="PRO_1000084663"
FT ACT_SITE 39
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ SEQUENCE 345 AA; 38754 MW; 707238F81AC4CE01 CRC64;
MSNYWLNIYK PRGISSAQLV SIVKKILGKT KIGHAGTLDV EAEGILPFAV GEATKLIRLL
IDARKTYIFT VKFGMQTNSG DCAGKVIATK DCVPSQEEAY AVCSKFIGSV TQIPPAFSAL
KVNGVRAYKL AREEKKVELK PRNITIYDLK CLNFDEKNAT ATYYTECSKG TYIRTLAEDL
ALSLQSLGFV IELRRTQVGI FKEENAIRIK SPDEITKNAL EAKSIKIEAI LDDILVLDAT
DSQAQQIKYG QKCLFNYEKD FRHLAKFAYR EEFKGNTERS TTAYTLVRED ASTGLTYKLP
LEVEFGKMSI DLLWVRYKGT LLAIGSLNKS CFNSLRVFNL TQDFF