PUS10_PYRAR
ID PUS10_PYRAR Reviewed; 411 AA.
AC A4WLQ5;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=Pars_1771;
OS Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=340102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700994 / DSM 13514 / JCM 11321 / PZ6;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum arsenaticum DSM 13514.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000660; ABP51322.1; -; Genomic_DNA.
DR AlphaFoldDB; A4WLQ5; -.
DR SMR; A4WLQ5; -.
DR STRING; 340102.Pars_1771; -.
DR EnsemblBacteria; ABP51322; ABP51322; Pars_1771.
DR KEGG; pas:Pars_1771; -.
DR HOGENOM; CLU_028780_2_0_2; -.
DR OMA; DGGLYIK; -.
DR PhylomeDB; A4WLQ5; -.
DR Proteomes; UP000001567; 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; 2.
DR Pfam; PF02926; THUMP; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR01213; pseudo_Pus10arc; 1.
DR PROSITE; PS51165; THUMP; 1.
PE 3: Inferred from homology;
KW Isomerase; RNA-binding; tRNA processing.
FT CHAIN 1..411
FT /note="tRNA pseudouridine synthase Pus10"
FT /id="PRO_0000407395"
FT DOMAIN 65..192
FT /note="THUMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
FT ACT_SITE 244
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
FT BINDING 376
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
SQ SEQUENCE 411 AA; 46535 MW; E375CF2D71A3F510 CRC64;
MELISKALEA VRRYPLCDSC LGRLFALMGY GIENRERGQA IKTILHMAAV SDYRKGKDVT
ADLIALAKCH LPTRRFLAGV GIRVDEERCY ICGDLMEGVE KYAEMAVEQL RGLDFVSFAV
GSTLPEELLE KEAEVVKSLL VTTGESVKHE VNRRIGKELL RRLSDKRVDK LRPNVVVNVD
LVSGQVKVVR NPILIGGRYL KLGRKIAQAK RFGNVRTTLL EKLAYLRDTF GGEDHVIHVS
GREDSDARML GSGRPLVVEV KQPLRYTAQV APFRDKDVIF LPVGFTDRNE VRRLKEKAKT
DIKLYRVLVL SESPLKQDDL SKLSALSGAT VTQYTPRRIK RLHPRKKRVR MVYDVAWRLV
SPHVFELYIR CQGGLYVKEF VHGDGGRTAP NVAELLNTRL EVLELDVLYI E