PUS2_YEAST
ID PUS2_YEAST Reviewed; 370 AA.
AC P53167; D6VU78; Q06713;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 4.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=tRNA pseudouridine(27/28) synthase;
DE EC=5.4.99.44;
DE AltName: Full=tRNA pseudouridine synthase 2;
DE AltName: Full=tRNA pseudouridylate synthase 2;
DE AltName: Full=tRNA-uridine isomerase 2;
GN Name=PUS2; OrderedLocusNames=YGL063W;
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 [GENOMIC DNA].
RX PubMed=8641292; DOI=10.1002/j.1460-2075.1996.tb00580.x;
RA Simos G., Tekotte H., Grosjean H., Segref A., Sharma K., Tollervey D.,
RA Hurt E.C.;
RT "Nuclear pore proteins are involved in the biogenesis of functional tRNA.";
RL EMBO J. 15:2270-2284(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9234674;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<861::aid-yea125>3.0.co;2-9;
RA Feuermann M., de Montigny J., Potier S., Souciet J.-L.;
RT "The characterization of two new clusters of duplicated genes suggests a
RT 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes.";
RL Yeast 13:861-869(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 136.
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASP-56.
RX PubMed=17684231; DOI=10.1261/rna.605607;
RA Behm-Ansmant I., Branlant C., Motorin Y.;
RT "The Saccharomyces cerevisiae Pus2 protein encoded by YGL063w ORF is a
RT mitochondrial tRNA:Psi27/28-synthase.";
RL RNA 13:1641-1647(2007).
CC -!- FUNCTION: Mitochondrial-specific pseudouridine synthase catalyzing the
CC formation of pseudouridine at positions 27 and 28 in the anticodon stem
CC and loop of mitochondrial transfer RNAs. {ECO:0000269|PubMed:17684231}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(27/28) in mitochondrial tRNA = pseudouridine(27/28) in
CC mitochondrial tRNA; Xref=Rhea:RHEA:42560, Rhea:RHEA-COMP:10115,
CC Rhea:RHEA-COMP:10116, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC EC=5.4.99.44; Evidence={ECO:0000269|PubMed:17684231};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17684231}.
CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC {ECO:0000305}.
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DR EMBL; X80674; CAA56699.1; -; Genomic_DNA.
DR EMBL; Z72585; CAA96766.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08039.2; -; Genomic_DNA.
DR PIR; S64067; S64067.
DR RefSeq; NP_011452.4; NM_001180928.4.
DR AlphaFoldDB; P53167; -.
DR SMR; P53167; -.
DR BioGRID; 33184; 75.
DR DIP; DIP-5022N; -.
DR IntAct; P53167; 1.
DR MINT; P53167; -.
DR STRING; 4932.YGL063W; -.
DR MaxQB; P53167; -.
DR PaxDb; P53167; -.
DR PRIDE; P53167; -.
DR EnsemblFungi; YGL063W_mRNA; YGL063W; YGL063W.
DR GeneID; 852817; -.
DR KEGG; sce:YGL063W; -.
DR SGD; S000003031; PUS2.
DR VEuPathDB; FungiDB:YGL063W; -.
DR eggNOG; KOG2553; Eukaryota.
DR GeneTree; ENSGT00950000183160; -.
DR HOGENOM; CLU_021971_4_0_1; -.
DR InParanoid; P53167; -.
DR OMA; ITLERMC; -.
DR BioCyc; MetaCyc:YGL063W-MON; -.
DR BioCyc; YEAST:YGL063W-MON; -.
DR BRENDA; 5.4.99.44; 984.
DR PRO; PR:P53167; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53167; protein.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009982; F:pseudouridine synthase activity; IMP:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IMP:SGD.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IMP:SGD.
DR CDD; cd02568; PseudoU_synth_PUS1_PUS2; 1.
DR Gene3D; 3.30.70.580; -; 1.
DR Gene3D; 3.30.70.660; -; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR001406; PsdUridine_synth_TruA.
DR InterPro; IPR020097; PsdUridine_synth_TruA_a/b_dom.
DR InterPro; IPR020095; PsdUridine_synth_TruA_C.
DR InterPro; IPR041708; PUS1/PUS2-like.
DR InterPro; IPR020094; TruA/RsuA/RluB/E/F_N.
DR PANTHER; PTHR11142; PTHR11142; 1.
DR Pfam; PF01416; PseudoU_synth_1; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR00071; hisT_truA; 1.
PE 1: Evidence at protein level;
KW Isomerase; Mitochondrion; Reference proteome; tRNA processing.
FT CHAIN 1..370
FT /note="tRNA pseudouridine(27/28) synthase"
FT /id="PRO_0000057532"
FT ACT_SITE 56
FT /note="Nucleophile"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 56
FT /note="D->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:17684231"
FT CONFLICT 136
FT /note="C -> S (in Ref. 2 and 3; CAA96766)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 41891 MW; 776D3A5D8C83EBC3 CRC64;
MLLGYCGSGY YGMQYNPPHK TIEGEILTKL FDVGAISEEN SLAPKKNSFM AAARTDKGVH
AMLNLLSLKI TLREDTVAKL NAALPPEIRV WGIQPVNKKF NARSACDSRW YQYLIPEFIL
IGPPRSSLLH RNVGGCYRED GSQEVWDTFL EQTRGRFSGD ELCRLQDTAQ KLSESDPLVQ
DYVGLLSGTL SGYCLSPSKL DAFEAAMQEY VGTHNFHNFT TGKLWGDPSA QRHIKKVVVS
QASPGWICVR IHGQSFMLHQ IRRMVALAVL AARCQLPPNI VRNYFNAGPR KYIPRAPAQG
LLLEGPVFDG YNTKLRNLLY CEIRPDDITL ERMCRFRERQ ICTAIAHEET QRHVFCHFVR
QMNRLATPLI
