ID   PUS5_DEBHA              Reviewed;         339 AA.
AC   Q6BNX8;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=21S rRNA pseudouridine(2819) synthase;
DE            EC=5.4.99.43 {ECO:0000250|UniProtKB:Q06244};
DE   AltName: Full=Pseudouridine synthase 5;
DE   AltName: Full=Pseudouridylate synthase PUS5;
DE   AltName: Full=Uracil hydrolyase PUS5;
GN   Name=PUS5; OrderedLocusNames=DEHA2E18216g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Pseudouridylate synthase responsible for the pseudouridine-
CC       2819 formation in mitochondrial 21S rRNA. May modulate the efficiency
CC       or the fidelity of the mitochondrial translation machinery.
CC       {ECO:0000250|UniProtKB:Q06244}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine(2819) in 21S rRNA = pseudouridine(2819) in 21S rRNA;
CC         Xref=Rhea:RHEA:42556, Rhea:RHEA-COMP:10113, Rhea:RHEA-COMP:10114,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.43;
CC         Evidence={ECO:0000250|UniProtKB:Q06244};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q06244}.
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC       {ECO:0000305}.
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DR   EMBL; CR382137; CAG88356.2; -; Genomic_DNA.
DR   RefSeq; XP_460092.2; XM_460092.1.
DR   AlphaFoldDB; Q6BNX8; -.
DR   STRING; 4959.XP_460092.2; -.
DR   EnsemblFungi; CAG88356; CAG88356; DEHA2E18216g.
DR   GeneID; 2901954; -.
DR   KEGG; dha:DEHA2E18216g; -.
DR   eggNOG; KOG1919; Eukaryota.
DR   HOGENOM; CLU_998077_0_0_1; -.
DR   InParanoid; Q6BNX8; -.
DR   OMA; ACIITKI; -.
DR   OrthoDB; 1378690at2759; -.
DR   Proteomes; UP000000599; Chromosome E.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0120159; F:rRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd02869; PseudoU_synth_RluA_like; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR006224; PsdUridine_synth_RluC/D_CS.
DR   InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR   Pfam; PF00849; PseudoU_synth_2; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
DR   PROSITE; PS01129; PSI_RLU; 1.
PE   3: Inferred from homology;
KW   Isomerase; Mitochondrion; Reference proteome; rRNA processing.
FT   CHAIN           1..339
FT                   /note="21S rRNA pseudouridine(2819) synthase"
FT                   /id="PRO_0000162752"
FT   ACT_SITE        84
FT                   /evidence="ECO:0000250|UniProtKB:P0AA37"
SQ   SEQUENCE   339 AA;  39114 MW;  1289EC0F73B29218 CRC64;
     MKPTFLKCLQ GIDKNHAYRQ INIIDIHSRY LIINKPSGIQ CNGTKSHSNY LLPQLYKQLK
     AHFSANNPNY KLNPDQYKVV HRLDKYVSGG LIIARGKNAN AFRKSFSNQN TNLSVKRKYI
     GLVPIPNTVS FKQHLHEFGD LKVQHENEVR YLNRPESVTD KKGLIFKDDS LTEGIINFDI
     VALPKDDRRN KNTGELVTYS ALTKFKILHS MSQVPTNEQI SRFPKLYKNK TIYPIIIELE
     TGRKNQIRDH ILQAFKVSLL NDDKFIDFKM VQKSNTANIN SEVYNSNQIG LHSAYISISK
     SSFANEYVIP IPEGDEYLWK GFLDENSFIK TINRELITF