PUS4_YEAST
ID PUS4_YEAST Reviewed; 403 AA.
AC P48567; D6W0Q1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=tRNA pseudouridine synthase 4;
DE EC=5.4.99.25 {ECO:0000269|PubMed:9358157};
DE AltName: Full=tRNA pseudouridine(55) synthase;
DE Short=Psi55 synthase;
DE AltName: Full=tRNA pseudouridylate synthase 4;
DE AltName: Full=tRNA-uridine isomerase 4;
GN Name=PUS4; OrderedLocusNames=YNL292W; ORFNames=N0480;
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 96604 / S288c / FY1679;
RX PubMed=8553702; DOI=10.1002/yea.320111311;
RA Maurer K.C.T., Urbanus J.H.M., Planta R.J.;
RT "Sequence analysis of a 30 kb DNA segment from yeast chromosome XIV
RT carrying a ribosomal protein gene cluster, the genes encoding a plasma
RT membrane protein and a subunit of replication factor C, and a novel
RT putative serine/threonine protein kinase gene.";
RL Yeast 11:1303-1310(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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, AND SUBSTRATE SPECIFICITY.
RX PubMed=9358157; DOI=10.1093/nar/25.22.4493;
RA Becker H.F., Motorin Y., Planta R.J., Grosjean H.;
RT "The yeast gene YNL292w encodes a pseudouridine synthase (Pus4) catalyzing
RT the formation of psi55 in both mitochondrial and cytoplasmic tRNAs.";
RL Nucleic Acids Res. 25:4493-4499(1997).
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).
RN [6]
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: Responsible for synthesis of pseudouridine from uracil-55 in
CC the psi GC loop of transfer RNAs (PubMed:9358157). Also catalyzes
CC pseudouridylation of mRNAs with the consensus sequence 5'-GGUUCRA-3'
CC (PubMed:25219674). {ECO:0000269|PubMed:25219674,
CC ECO:0000269|PubMed:9358157}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(55) in tRNA = pseudouridine(55) in tRNA;
CC Xref=Rhea:RHEA:42532, Rhea:RHEA-COMP:10101, Rhea:RHEA-COMP:10102,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.25;
CC Evidence={ECO:0000269|PubMed:9358157};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in mRNA = a pseudouridine in mRNA;
CC Xref=Rhea:RHEA:56644, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:14659,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000269|PubMed:25219674};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9358157}.
CC Mitochondrion {ECO:0000269|PubMed:9358157}.
CC -!- MISCELLANEOUS: Present with 3990 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
CC {ECO:0000305}.
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DR EMBL; U23084; AAC49108.1; -; Genomic_DNA.
DR EMBL; Z71568; CAA96210.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10267.1; -; Genomic_DNA.
DR PIR; S60410; S60410.
DR RefSeq; NP_014107.1; NM_001183130.1.
DR AlphaFoldDB; P48567; -.
DR SMR; P48567; -.
DR BioGRID; 35545; 43.
DR DIP; DIP-4256N; -.
DR IntAct; P48567; 1.
DR MINT; P48567; -.
DR STRING; 4932.YNL292W; -.
DR iPTMnet; P48567; -.
DR MaxQB; P48567; -.
DR PaxDb; P48567; -.
DR PRIDE; P48567; -.
DR EnsemblFungi; YNL292W_mRNA; YNL292W; YNL292W.
DR GeneID; 855424; -.
DR KEGG; sce:YNL292W; -.
DR SGD; S000005236; PUS4.
DR VEuPathDB; FungiDB:YNL292W; -.
DR eggNOG; KOG2529; Eukaryota.
DR GeneTree; ENSGT00940000158962; -.
DR HOGENOM; CLU_032087_4_2_1; -.
DR InParanoid; P48567; -.
DR OMA; QVKIGHG; -.
DR BioCyc; MetaCyc:YNL292W-MON; -.
DR BioCyc; YEAST:YNL292W-MON; -.
DR BRENDA; 5.4.99.25; 984.
DR BRENDA; 5.4.99.B22; 984.
DR PRO; PR:P48567; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P48567; protein.
DR GO; GO:0005739; C:mitochondrion; IMP:SGD.
DR GO; GO:0005634; C:nucleus; IMP: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:1990481; P:mRNA pseudouridine synthesis; IMP:SGD.
DR GO; GO:0006400; P:tRNA modification; IDA:SGD.
DR HAMAP; MF_01080; TruB_bact; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR002501; PsdUridine_synth_N.
DR InterPro; IPR014780; tRNA_psdUridine_synth_TruB.
DR PANTHER; PTHR13767; PTHR13767; 1.
DR Pfam; PF01509; TruB_N; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
PE 1: Evidence at protein level;
KW Isomerase; Mitochondrion; Nucleus; Reference proteome; tRNA processing.
FT CHAIN 1..403
FT /note="tRNA pseudouridine synthase 4"
FT /id="PRO_0000121976"
FT ACT_SITE 75
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P60340"
SQ SEQUENCE 403 AA; 45273 MW; 5E9D652F07362A27 CRC64;
MNGIFAIEKP SGITSNQFML KLQHALTKSQ VFSKEIQRAT AERKQQYEKQ TGKKASKRKL
RKVSKVKMGH GGTLDPLASG VLVIGIGAGT KKLANYLSGT VKVYESEALF GVSTTSGDVE
GEILSQNSVK HLNFDDLKTV EEKFVGQLKQ TPPIYAALKM DGKPLHEYAR EGKPLPRAIE
PRQVTIYDLK VFSDSLKRDH DYPLLRPTTE EAVDTVKNLN ANMLNDVLYF SKEYTEKHGL
DSEVAKVEEP FPLSEQEEQE IQKEGDSYRA PKLHFKANVS SGTYIRSLVS DIGKSMRSSC
YMVKLIRLQQ QDWSLEKNNV FQLTDFTERD EKVWSKVLEK VLDEGATVDV IEELKKAEKE
IPADVKECIV SSDQPGDEAT AETIETANAE EHSNTLKRKI EQV
