PUS10_PICTO
ID PUS10_PICTO Reviewed; 377 AA.
AC Q6L227;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=PTO0390;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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; AE017261; AAT42975.1; -; Genomic_DNA.
DR RefSeq; WP_011177191.1; NC_005877.1.
DR AlphaFoldDB; Q6L227; -.
DR SMR; Q6L227; -.
DR STRING; 263820.PTO0390; -.
DR EnsemblBacteria; AAT42975; AAT42975; PTO0390.
DR GeneID; 2843974; -.
DR KEGG; pto:PTO0390; -.
DR PATRIC; fig|263820.9.peg.414; -.
DR eggNOG; arCOG01015; Archaea.
DR HOGENOM; CLU_028780_2_0_2; -.
DR OMA; DGGLYIK; -.
DR OrthoDB; 61936at2157; -.
DR Proteomes; UP000000438; 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 PANTHER; PTHR21568; PTHR21568; 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..377
FT /note="tRNA pseudouridine synthase Pus10"
FT /id="PRO_0000407394"
FT ACT_SITE 206
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
SQ SEQUENCE 377 AA; 43311 MW; 866DC153D19386C4 CRC64;
MDLKELFDLN LCLRCTGRIF AAVDTGLTNE ERGARLYFAY KSIYGERDVP ESCYLCNGVF
KKFDEFFNIL MSKLNNYEFN SILVGSTFDE NIIEMEKDIQ SRFGSKGESI KKEFNREFGK
YLSKRLGKPF SKDADLTIEV DALYENVNII VKPVYIYGVY IKKSRDISQT RWIHKTGESI
ESIIGNELRS MTGCENYYLH GSGREDVDVM MLGNGREFVI EAAMPKRRYI DLYELQLRVN
ASGILFIYNL SYSSKATVRR IKSELHEKLY IAEVTGDLNK DIKKACSKFN NLIIEQRTPL
RVINHRSDLV RRKKINYINI ISIMNGRALL KICAEAGTYI KELVNGDNGR TVPSLSSVYG
SQLQVSSLDV VKIYRDD