ID   PUS10_PYRFU             Reviewed;         388 AA.
AC   Q8U1R6;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=tRNA pseudouridine synthase Pus10;
DE            EC=5.4.99.25 {ECO:0000269|PubMed:16920741, ECO:0000269|PubMed:18952823};
DE   AltName: Full=tRNA pseudouridine 54/55 synthase;
DE            Short=Psi54/55 synthase;
GN   Name=pus10; Synonyms=psuX; OrderedLocusNames=PF1139;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND TEMPERATURE DEPENDENCE.
RX   PubMed=16920741; DOI=10.1093/nar/gkl530;
RA   Roovers M., Hale C., Tricot C., Terns M.P., Terns R.M., Grosjean H.,
RA   Droogmans L.;
RT   "Formation of the conserved pseudouridine at position 55 in archaeal
RT   tRNA.";
RL   Nucleic Acids Res. 34:4293-4301(2006).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=18952823; DOI=10.1261/rna.1276508;
RA   Gurha P., Gupta R.;
RT   "Archaeal Pus10 proteins can produce both pseudouridine 54 and 55 in
RT   tRNA.";
RL   RNA 14:2521-2527(2008).
CC   -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-54 and
CC       uracil-55 in the psi GC loop of transfer RNAs.
CC       {ECO:0000269|PubMed:16920741, ECO:0000269|PubMed:18952823}.
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;
CC         Evidence={ECO:0000269|PubMed:18952823};
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:0000269|PubMed:16920741, ECO:0000269|PubMed:18952823};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius.
CC         {ECO:0000269|PubMed:16920741};
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase Pus10 family.
CC       {ECO:0000305}.
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DR   EMBL; AE009950; AAL81263.1; -; Genomic_DNA.
DR   RefSeq; WP_011012279.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U1R6; -.
DR   SMR; Q8U1R6; -.
DR   STRING; 186497.PF1139; -.
DR   PRIDE; Q8U1R6; -.
DR   EnsemblBacteria; AAL81263; AAL81263; PF1139.
DR   GeneID; 41712948; -.
DR   KEGG; pfu:PF1139; -.
DR   PATRIC; fig|186497.12.peg.1200; -.
DR   eggNOG; arCOG01015; Archaea.
DR   HOGENOM; CLU_028780_2_0_2; -.
DR   OMA; DGGLYIK; -.
DR   OrthoDB; 61936at2157; -.
DR   PhylomeDB; Q8U1R6; -.
DR   BioCyc; MetaCyc:MON-16703; -.
DR   BRENDA; 5.4.99.B22; 5243.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
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.
DR   PROSITE; PS51165; THUMP; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Reference proteome; RNA-binding; tRNA processing.
FT   CHAIN           1..388
FT                   /note="tRNA pseudouridine synthase Pus10"
FT                   /id="PRO_0000407396"
FT   DOMAIN          35..159
FT                   /note="THUMP"
FT   ACT_SITE        210
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   BINDING         274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         346
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   388 AA;  44680 MW;  2AFC8BF8BA3B7529 CRC64;
     MILEKAREIL EEHQLCNHCL GRLFGKLGKG TNEERGRAIR LLLSMETGKE YKEPEKCELC
     GGVFNNLDKF AELCIKAAEG IEFETFWVGS RFPEEIEKKE EEIWRKFRVV SGEKITKEFN
     RELGKVIAVR YGKTPVKERP DVVFIVEPFS EKVELQVNPI YVAGRYRKLI RGIPQTPAPG
     FKESIATIIC RAFKKHFHGK CIFKGAGRED VDVRMLGNGR PFVVEIKRPR KRKVNLKDIE
     EEINQSGKVE VLNLRFITPE EAERILTTRH RKVYEAIVYV KDGITKEEVE KVVKSLKNAE
     IKQRTPRRVL NSRADLVRVR KVYDVKGELI DDKHFKLRLV TDGGLYIKEL ISGDRGRTTP
     SVSEILGKEA WCEILDVLEV LDDVEGDN