ID   PUS10_ARCFU             Reviewed;         357 AA.
AC   O29113;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=AF_1152;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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; AE000782; AAB90092.1; -; Genomic_DNA.
DR   PIR; G69393; G69393.
DR   RefSeq; WP_010878649.1; NC_000917.1.
DR   AlphaFoldDB; O29113; -.
DR   SMR; O29113; -.
DR   STRING; 224325.AF_1152; -.
DR   DNASU; 1484376; -.
DR   EnsemblBacteria; AAB90092; AAB90092; AF_1152.
DR   GeneID; 1484376; -.
DR   KEGG; afu:AF_1152; -.
DR   eggNOG; arCOG01015; Archaea.
DR   HOGENOM; CLU_028780_2_0_2; -.
DR   OMA; DGGLYIK; -.
DR   OrthoDB; 61936at2157; -.
DR   PhylomeDB; O29113; -.
DR   Proteomes; UP000002199; 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.
DR   PROSITE; PS51165; THUMP; 1.
PE   3: Inferred from homology;
KW   Isomerase; Reference proteome; RNA-binding; tRNA processing.
FT   CHAIN           1..357
FT                   /note="tRNA pseudouridine synthase Pus10"
FT                   /id="PRO_0000407382"
FT   DOMAIN          1..118
FT                   /note="THUMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
FT   ACT_SITE        187
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
FT   BINDING         251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
FT   BINDING         322
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
SQ   SEQUENCE   357 AA;  41287 MW;  63F8EE984337FEE1 CRC64;
     MNLCRECYGI IGEGVVAEKC EACCNAFDRV EEFAEEIVKK MSEYEFETFN VGSRVWGSLK
     ALQEYLSLKG IEYEIKQRFN TKLARAIEEK TGSKRTLNPD ITVLFDLETF TFELQIRPVF
     IYGRYLKRVR NISQTRWLCG YCNGEGCEVC NFTGKKYVSS VEELIAMPAV RLFKARDAKL
     HGAGREDVDA RMLGTGRPFV LEVIEPRKRF VDLKELEEAI NSQKWVAVRD LEYTDAEKVR
     EVKTERHRKT YRAKVVFEEK VERERLIEAL ESLKGEIRQR TPMRVSHRRA DRVRVRRLYD
     ARLIHHTGRV AVVEFEAEAG LYIKELVSGD NGRTRPSLAE KVGVNARVDR LDVIAVS