PUS5_YEAST
ID PUS5_YEAST Reviewed; 254 AA.
AC Q06244; D6VYH1;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=21S rRNA pseudouridine(2819) synthase;
DE EC=5.4.99.43 {ECO:0000269|PubMed:10756195, ECO:0000269|PubMed:25219674};
DE AltName: Full=Pseudouridine synthase 5;
DE AltName: Full=Pseudouridylate synthase PUS5;
DE AltName: Full=Uracil hydrolyase PUS5;
GN Name=PUS5; OrderedLocusNames=YLR165C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=10756195; DOI=10.1093/nar/28.9.1941;
RA Ansmant I., Massenet S., Grosjean H., Motorin Y., Branlant C.;
RT "Identification of the Saccharomyces cerevisiae RNA:pseudouridine synthase
RT responsible for formation of psi(2819) in 21S mitochondrial ribosomal
RT RNA.";
RL Nucleic Acids Res. 28:1941-1946(2000).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25219674; DOI=10.1016/j.cell.2014.08.028;
RA Schwartz S., Bernstein D.A., Mumbach M.R., Jovanovic M., Herbst R.H.,
RA Leon-Ricardo B.X., Engreitz J.M., Guttman M., Satija R., Lander E.S.,
RA Fink G., Regev A.;
RT "Transcriptome-wide mapping reveals widespread dynamic-regulated
RT pseudouridylation of ncRNA and mRNA.";
RL Cell 159:148-162(2014).
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:0000269|PubMed:10756195, ECO:0000269|PubMed:25219674}.
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:0000269|PubMed:10756195, ECO:0000269|PubMed:25219674};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10756195}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U51921; AAB67489.1; -; Genomic_DNA.
DR EMBL; AY557942; AAS56268.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09487.1; -; Genomic_DNA.
DR PIR; S68481; S68481.
DR RefSeq; NP_013266.1; NM_001182052.1.
DR AlphaFoldDB; Q06244; -.
DR SMR; Q06244; -.
DR BioGRID; 31438; 77.
DR STRING; 4932.YLR165C; -.
DR PaxDb; Q06244; -.
DR EnsemblFungi; YLR165C_mRNA; YLR165C; YLR165C.
DR GeneID; 850862; -.
DR KEGG; sce:YLR165C; -.
DR SGD; S000004155; PUS5.
DR VEuPathDB; FungiDB:YLR165C; -.
DR eggNOG; KOG1919; Eukaryota.
DR HOGENOM; CLU_081037_0_0_1; -.
DR InParanoid; Q06244; -.
DR OMA; ACIITKI; -.
DR BioCyc; MetaCyc:G3O-32295-MON; -.
DR BioCyc; YEAST:G3O-32295-MON; -.
DR BRENDA; 4.2.1.70; 984.
DR BRENDA; 5.4.99.43; 984.
DR ChiTaRS; PUS5; yeast.
DR PRO; PR:Q06244; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06244; protein.
DR GO; GO:0005739; C:mitochondrion; IMP:SGD.
DR GO; GO:0009982; F:pseudouridine synthase activity; IDA:UniProtKB.
DR GO; GO:0004730; F:pseudouridylate synthase activity; IMP:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0120159; F:rRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IDA:UniProtKB.
DR GO; GO:0001522; P:pseudouridine synthesis; IMP:SGD.
DR GO; GO:0000154; P:rRNA modification; IMP:SGD.
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 1: Evidence at protein level;
KW Isomerase; Mitochondrion; Reference proteome; rRNA processing.
FT CHAIN 1..254
FT /note="21S rRNA pseudouridine(2819) synthase"
FT /id="PRO_0000162754"
FT ACT_SITE 71
FT /evidence="ECO:0000250|UniProtKB:P0AA37"
SQ SEQUENCE 254 AA; 29359 MW; 7404383DCD726369 CRC64;
MSLKKQIPII FENTHYFIVN KPPGIPSQPP DCRTWGRTHP NLDPTPLLER FKAIYYSHRE
VELCRTVHRL DHCVTGGMLI AKTKDGSVKF SRFLQKGGNN GYKLQRKYVA IVESSGRFNK
PNNYEIKYGP KYNFLISHGG REITKFKEVD ENCIVLQLVT GKKHQIRNHV SQILNQPILN
DKRHGSTVNF PELFNDQIAL HSACIITKIG LQTKTHLIPM EHNNTGQLWS RKYVNEEGEF
TLPIKEVLLE NWDQ
