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Protein

tRNA pseudouridine(27/28) synthase

Gene

PUS2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Mitochondrial-specific pseudouridine synthase catalyzing the formation of pseudouridine at positions 27 and 28 in the anticodon stem and loop of mitochondrial transfer RNAs.1 Publication

Catalytic activityi

Mitochondrial tRNA uridine(27/28) = mitochondrial tRNA pseudouridine(27/28).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei56 – 561Nucleophile
Binding sitei111 – 1111SubstrateBy similarity

GO - Molecular functioni

  • pseudouridine synthase activity Source: SGD
  • RNA binding Source: InterPro

GO - Biological processi

  • mRNA pseudouridine synthesis Source: SGD
  • tRNA pseudouridine synthesis Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

tRNA processing

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16706.
YEAST:YGL063W-MONOMER.
BRENDAi5.4.99.44. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA pseudouridine(27/28) synthase (EC:5.4.99.44)
Alternative name(s):
tRNA pseudouridine synthase 2
tRNA pseudouridylate synthase 2
tRNA-uridine isomerase 2
Gene namesi
Name:PUS2
Ordered Locus Names:YGL063W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGL063w.
EuPathDBiFungiDB:YGL063W.
SGDiS000003031. PUS2.

Subcellular locationi

  • Mitochondrion 1 Publication

GO - Cellular componenti

  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 561D → A: Abolishes catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 370370tRNA pseudouridine(27/28) synthasePRO_0000057532Add
BLAST

Proteomic databases

MaxQBiP53167.
PaxDbiP53167.

Interactioni

Protein-protein interaction databases

BioGridi33184. 31 interactions.
DIPiDIP-5022N.
MINTiMINT-499274.

Structurei

3D structure databases

ProteinModelPortaliP53167.
SMRiP53167. Positions 1-352.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0101.
GeneTreeiENSGT00510000047706.
HOGENOMiHOG000213984.
InParanoidiP53167.
KOiK15452.
OMAiCFISSES.
OrthoDBiEOG7DVDMQ.

Family and domain databases

Gene3Di3.30.70.580. 1 hit.
3.30.70.660. 1 hit.
InterProiIPR020103. PsdUridine_synth_cat_dom.
IPR001406. PsdUridine_synth_TruA.
IPR020097. PsdUridine_synth_TruA_a/b_dom.
IPR020095. PsdUridine_synth_TruA_C.
IPR020094. PsdUridine_synth_TruA_N.
[Graphical view]
PANTHERiPTHR11142. PTHR11142. 1 hit.
PfamiPF01416. PseudoU_synth_1. 2 hits.
[Graphical view]
SUPFAMiSSF55120. SSF55120. 2 hits.
TIGRFAMsiTIGR00071. hisT_truA. 1 hit.

Sequencei

Sequence statusi: Complete.

P53167-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLGYCGSGY YGMQYNPPHK TIEGEILTKL FDVGAISEEN SLAPKKNSFM
60 70 80 90 100
AAARTDKGVH AMLNLLSLKI TLREDTVAKL NAALPPEIRV WGIQPVNKKF
110 120 130 140 150
NARSACDSRW YQYLIPEFIL IGPPRSSLLH RNVGGCYRED GSQEVWDTFL
160 170 180 190 200
EQTRGRFSGD ELCRLQDTAQ KLSESDPLVQ DYVGLLSGTL SGYCLSPSKL
210 220 230 240 250
DAFEAAMQEY VGTHNFHNFT TGKLWGDPSA QRHIKKVVVS QASPGWICVR
260 270 280 290 300
IHGQSFMLHQ IRRMVALAVL AARCQLPPNI VRNYFNAGPR KYIPRAPAQG
310 320 330 340 350
LLLEGPVFDG YNTKLRNLLY CEIRPDDITL ERMCRFRERQ ICTAIAHEET
360 370
QRHVFCHFVR QMNRLATPLI
Length:370
Mass (Da):41,891
Last modified:September 21, 2011 - v4
Checksum:i776D3A5D8C83EBC3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1361C → S (PubMed:9234674).Curated
Sequence conflicti136 – 1361C → S in CAA96766 (PubMed:9169869).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80674 Genomic DNA. Translation: CAA56699.1.
Z72585 Genomic DNA. Translation: CAA96766.1.
BK006941 Genomic DNA. Translation: DAA08039.2.
PIRiS64067.
RefSeqiNP_011452.4. NM_001180928.4.

Genome annotation databases

EnsemblFungiiYGL063W; YGL063W; YGL063W.
GeneIDi852817.
KEGGisce:YGL063W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80674 Genomic DNA. Translation: CAA56699.1.
Z72585 Genomic DNA. Translation: CAA96766.1.
BK006941 Genomic DNA. Translation: DAA08039.2.
PIRiS64067.
RefSeqiNP_011452.4. NM_001180928.4.

3D structure databases

ProteinModelPortaliP53167.
SMRiP53167. Positions 1-352.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33184. 31 interactions.
DIPiDIP-5022N.
MINTiMINT-499274.

Proteomic databases

MaxQBiP53167.
PaxDbiP53167.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL063W; YGL063W; YGL063W.
GeneIDi852817.
KEGGisce:YGL063W.

Organism-specific databases

CYGDiYGL063w.
EuPathDBiFungiDB:YGL063W.
SGDiS000003031. PUS2.

Phylogenomic databases

eggNOGiCOG0101.
GeneTreeiENSGT00510000047706.
HOGENOMiHOG000213984.
InParanoidiP53167.
KOiK15452.
OMAiCFISSES.
OrthoDBiEOG7DVDMQ.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16706.
YEAST:YGL063W-MONOMER.
BRENDAi5.4.99.44. 984.

Miscellaneous databases

NextBioi972357.
PROiP53167.

Family and domain databases

Gene3Di3.30.70.580. 1 hit.
3.30.70.660. 1 hit.
InterProiIPR020103. PsdUridine_synth_cat_dom.
IPR001406. PsdUridine_synth_TruA.
IPR020097. PsdUridine_synth_TruA_a/b_dom.
IPR020095. PsdUridine_synth_TruA_C.
IPR020094. PsdUridine_synth_TruA_N.
[Graphical view]
PANTHERiPTHR11142. PTHR11142. 1 hit.
PfamiPF01416. PseudoU_synth_1. 2 hits.
[Graphical view]
SUPFAMiSSF55120. SSF55120. 2 hits.
TIGRFAMsiTIGR00071. hisT_truA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nuclear pore proteins are involved in the biogenesis of functional tRNA."
    Simos G., Tekotte H., Grosjean H., Segref A., Sharma K., Tollervey D., Hurt E.C.
    EMBO J. 15:2270-2284(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes."
    Feuermann M., de Montigny J., Potier S., Souciet J.-L.
    Yeast 13:861-869(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 136.
    Strain: ATCC 204508 / S288c.
  5. "The Saccharomyces cerevisiae Pus2 protein encoded by YGL063w ORF is a mitochondrial tRNA:Psi27/28-synthase."
    Behm-Ansmant I., Branlant C., Motorin Y.
    RNA 13:1641-1647(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-56.

Entry informationi

Entry nameiPUS2_YEAST
AccessioniPrimary (citable) accession number: P53167
Secondary accession number(s): D6VU78, Q06713
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 21, 2011
Last modified: July 22, 2015
This is version 116 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.