TRUD_NITSB
ID TRUD_NITSB Reviewed; 360 AA.
AC A6Q2U7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=tRNA pseudouridine synthase D {ECO:0000255|HAMAP-Rule:MF_01082};
DE EC=5.4.99.27 {ECO:0000255|HAMAP-Rule:MF_01082};
DE AltName: Full=tRNA pseudouridine(13) synthase {ECO:0000255|HAMAP-Rule:MF_01082};
DE AltName: Full=tRNA pseudouridylate synthase D {ECO:0000255|HAMAP-Rule:MF_01082};
DE AltName: Full=tRNA-uridine isomerase D {ECO:0000255|HAMAP-Rule:MF_01082};
GN Name=truD {ECO:0000255|HAMAP-Rule:MF_01082}; OrderedLocusNames=NIS_0692;
OS Nitratiruptor sp. (strain SB155-2).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales;
OC Nitratiruptoraceae; Nitratiruptor; unclassified Nitratiruptor.
OX NCBI_TaxID=387092;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB155-2;
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-13 in
CC transfer RNAs. {ECO:0000255|HAMAP-Rule:MF_01082}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(13) in tRNA = pseudouridine(13) in tRNA;
CC Xref=Rhea:RHEA:42540, Rhea:RHEA-COMP:10105, Rhea:RHEA-COMP:10106,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.27;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01082};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruD family.
CC {ECO:0000255|HAMAP-Rule:MF_01082}.
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DR EMBL; AP009178; BAF69806.1; -; Genomic_DNA.
DR RefSeq; WP_012082069.1; NC_009662.1.
DR AlphaFoldDB; A6Q2U7; -.
DR SMR; A6Q2U7; -.
DR STRING; 387092.NIS_0692; -.
DR EnsemblBacteria; BAF69806; BAF69806; NIS_0692.
DR KEGG; nis:NIS_0692; -.
DR eggNOG; COG0585; Bacteria.
DR HOGENOM; CLU_005281_4_0_7; -.
DR OMA; LWLWVEK; -.
DR OrthoDB; 1490777at2; -.
DR Proteomes; UP000001118; 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; 3.30.2350.20; -; 1.
DR HAMAP; MF_01082; TruD; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR001656; PsdUridine_synth_TruD.
DR InterPro; IPR020119; PsdUridine_synth_TruD_CS.
DR InterPro; IPR011760; PsdUridine_synth_TruD_insert.
DR InterPro; IPR042214; TruD_catalytic.
DR Pfam; PF01142; TruD; 2.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR00094; tRNA_TruD_broad; 1.
DR PROSITE; PS50984; TRUD; 1.
DR PROSITE; PS01268; UPF0024; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome; tRNA processing.
FT CHAIN 1..360
FT /note="tRNA pseudouridine synthase D"
FT /id="PRO_1000084753"
FT DOMAIN 151..332
FT /note="TRUD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01082"
FT ACT_SITE 76
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01082"
SQ SEQUENCE 360 AA; 42180 MW; E4B92AC4FA29F8B8 CRC64;
MDRLFFLDHS PIDFYFKQSP ETFVVEEVPL YPFSGAGEHL IVKVRKKNMT TWQMLQSISE
QVGVKIRDIG YAGLKDKNAL TYQYISLHKK YEEALKKFSH PLIKTIELTY HKNKIRRGHL
KGNRFFIRLK KVKPVDAKKI DEVLKILEEE GMPNFFGYQR FGIDGDNWQL GKEIVEGKRK
ERNKTLKKLL INAYQSHLFN LWLSKRIELS KLLNCFTQNE LSQTLDLPRS IIKELQCQKP
FFKLFPGDIA MHYPNGKIFG VEDVKGESER FFAKAIAPTG LLPGVKTKRC DGLARDIEKD
YDDERISEFG DRRYAWIFPQ ELHGIYKEKN AWYELSFFLP KGSYATVLLE EIAHRKIKGE