PUS6_YEAST
ID PUS6_YEAST Reviewed; 404 AA.
AC P53294; D6VUV2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=tRNA pseudouridine(31) synthase;
DE EC=5.4.99.42;
DE AltName: Full=Pseudouridine synthase 6;
DE AltName: Full=Pseudouridylate synthase 6;
DE AltName: Full=Uracil hydrolyase;
DE AltName: Full=tRNA pseudouridine 31 synthase;
DE Short=PSI31 synthase;
GN Name=PUS6; OrderedLocusNames=YGR169C;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [2]
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 [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ASP-168.
RX PubMed=11406626; DOI=10.1074/jbc.m103131200;
RA Ansmant I., Motorin Y., Massenet S., Grosjean H., Branlant C.;
RT "Identification and characterization of the tRNA:Psi 31-synthase (Pus6p) of
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 276:34934-34940(2001).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Catalyzes the formation of pseudouridine at position 31 in
CC the psi GC loop of tRNAS. {ECO:0000269|PubMed:11406626}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(31) in tRNA = pseudouridine(31) in tRNA;
CC Xref=Rhea:RHEA:42552, Rhea:RHEA-COMP:10111, Rhea:RHEA-COMP:10112,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.42;
CC Evidence={ECO:0000269|PubMed:11406626};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11406626}.
CC Mitochondrion {ECO:0000269|PubMed:11406626}.
CC -!- MISCELLANEOUS: Present with 377 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC {ECO:0000305}.
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DR EMBL; Z72954; CAA97195.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08263.1; -; Genomic_DNA.
DR PIR; S64480; S64480.
DR RefSeq; NP_011685.3; NM_001181298.3.
DR AlphaFoldDB; P53294; -.
DR BioGRID; 33421; 38.
DR DIP; DIP-5429N; -.
DR STRING; 4932.YGR169C; -.
DR iPTMnet; P53294; -.
DR MaxQB; P53294; -.
DR PaxDb; P53294; -.
DR PRIDE; P53294; -.
DR EnsemblFungi; YGR169C_mRNA; YGR169C; YGR169C.
DR GeneID; 853079; -.
DR KEGG; sce:YGR169C; -.
DR SGD; S000003401; PUS6.
DR VEuPathDB; FungiDB:YGR169C; -.
DR eggNOG; KOG1919; Eukaryota.
DR HOGENOM; CLU_016902_12_1_1; -.
DR InParanoid; P53294; -.
DR OMA; CYRLDKI; -.
DR BioCyc; MetaCyc:YGR169C-MON; -.
DR BioCyc; YEAST:YGR169C-MON; -.
DR BRENDA; 5.4.99.42; 984.
DR BRENDA; 5.4.99.B22; 984.
DR PRO; PR:P53294; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53294; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0009982; F:pseudouridine synthase activity; IDA: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:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IDA:SGD.
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 Cytoplasm; Isomerase; Mitochondrion; Reference proteome; tRNA processing.
FT CHAIN 1..404
FT /note="tRNA pseudouridine(31) synthase"
FT /id="PRO_0000162757"
FT ACT_SITE 168
FT MUTAGEN 168
FT /note="D->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:11406626"
SQ SEQUENCE 404 AA; 46816 MW; A654F170BA4E33A4 CRC64;
MSTIKVIEVY TQNGLRKVRP YYNRRSAFVK GRWLGKLLID VLVSEFKLRP RAYYLDQIRK
GTYRLIRDGV PLVPDHLMTT IIKNHDVLET TTHKHEPPVK QWCSQEVEAE DLPGRIAGFN
IVFEDESILV IDKPSGIPVH PTGQFYQNTI TELLKLHGVD ALPCYRLDKI TSGLLILAKN
SQSAGEIQKS IRSRDMIKIY LARVKGRFPH SELILDNENA AETTFEDTSK VTVEMTPIYS
IDPKRQFPVG LSTSKDAITK FYPIRYFSHA DETVVACKPI TGRTHQIRIH LARLGHPIVN
DSVYCSHITK YPERLKFITQ FPRWENQQDL DAEELKVRFQ KFVDETKNNC RTMETFCPEC
HTVDLKDPVL SDLELWLHAW KYEEINGKFK FKTDLPKWAQ LDNS
