PUS10_THEAC
ID PUS10_THEAC Reviewed; 389 AA.
AC Q9HIN9;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=tRNA pseudouridine synthase Pus10 {ECO:0000255|HAMAP-Rule:MF_01893};
DE EC=5.4.99.25 {ECO:0000255|HAMAP-Rule:MF_01893};
DE AltName: Full=tRNA pseudouridine 54/55 synthase {ECO:0000255|HAMAP-Rule:MF_01893};
DE Short=Psi54/55 synthase {ECO:0000255|HAMAP-Rule:MF_01893};
GN Name=pus10 {ECO:0000255|HAMAP-Rule:MF_01893}; OrderedLocusNames=Ta1296;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-54 and
CC uracil-55 in the psi GC loop of transfer RNAs. {ECO:0000255|HAMAP-
CC Rule:MF_01893}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(54) in tRNA = pseudouridine(54) in tRNA;
CC Xref=Rhea:RHEA:57876, Rhea:RHEA-COMP:10193, Rhea:RHEA-COMP:14141,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01893};
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_01893};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase Pus10 family.
CC {ECO:0000255|HAMAP-Rule:MF_01893}.
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DR EMBL; AL445067; CAC12418.1; -; Genomic_DNA.
DR RefSeq; WP_010901702.1; NC_002578.1.
DR AlphaFoldDB; Q9HIN9; -.
DR SMR; Q9HIN9; -.
DR STRING; 273075.Ta1296; -.
DR EnsemblBacteria; CAC12418; CAC12418; CAC12418.
DR GeneID; 1456775; -.
DR KEGG; tac:Ta1296; -.
DR eggNOG; arCOG01015; Archaea.
DR HOGENOM; CLU_028780_2_0_2; -.
DR OMA; DGGLYIK; -.
DR OrthoDB; 61936at2157; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0000049; F:tRNA 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 HAMAP; MF_01893; Pus10_arch; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR005912; Pus10.
DR InterPro; IPR039894; Pus10-like.
DR InterPro; IPR004114; THUMP_dom.
DR PANTHER; PTHR21568; PTHR21568; 1.
DR Pfam; PF02926; THUMP; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR01213; pseudo_Pus10arc; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome; RNA-binding; tRNA processing.
FT CHAIN 1..389
FT /note="tRNA pseudouridine synthase Pus10"
FT /id="PRO_0000407398"
FT ACT_SITE 213
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
SQ SEQUENCE 389 AA; 44511 MW; 075C1169895E9A5E CRC64;
MFQISELANY RLCKRCSGRI FAYHYHGISN LERGEYLQFA IGCETGNPDF SFVDSKNCDI
CHGIFDRFDD IYDLVAKKVG DAQYSTFLVG SVFPQDTIRM EEDIQKKFGS SGESIKKEFN
REFGKYFSAR TGKEYSQDNP DLTILVNAEY LFVDVKIRSI YIYGKYRKFR RDMPQTRWIH
RPNGDTVESV IGSVFTRYAG GTNYYLHGSG REDVDVRMLG NGREFVLEVE NPRYREFELD
PVVKEINTSG KGVEIFDVKF SSHDAVSEVK LEKHRKVYDA LVVSDRPIDE SRLLEACINL
TGKNIYQRTP LRVAQRRSDL VRTRRIDQVD LVGVSANEAE ILISAEAGTY IKELVNGDGG
RTRPSLSEMY GSPLNVKELD VIKICRGED