PUS1_YARLI
ID PUS1_YARLI Reviewed; 528 AA.
AC Q6CC39;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=tRNA pseudouridine synthase 1;
DE EC=5.4.99.- {ECO:0000250|UniProtKB:Q12211};
DE AltName: Full=tRNA pseudouridylate synthase 1;
DE AltName: Full=tRNA-uridine isomerase 1;
GN Name=PUS1; OrderedLocusNames=YALI0C12749g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Formation of pseudouridine at positions 27 and 28 in the
CC anticodon stem and loop of transfer RNAs; at positions 34 and 36 of
CC intron-containing precursor tRNA(Ile) and at position 35 in the intron-
CC containing tRNA(Tyr). Catalyzes pseudouridylation at position 44 in U2
CC snRNA. Also catalyzes pseudouridylation of mRNAs.
CC {ECO:0000250|UniProtKB:Q12211}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in tRNA = a pseudouridine in tRNA;
CC Xref=Rhea:RHEA:54572, Rhea:RHEA-COMP:13339, Rhea:RHEA-COMP:13934,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000250|UniProtKB:Q12211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine in snRNA = pseudouridine in snRNA;
CC Xref=Rhea:RHEA:51124, Rhea:RHEA-COMP:12891, Rhea:RHEA-COMP:12892,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000250|UniProtKB:Q12211};
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:0000250|UniProtKB:Q12211};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q12211};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q12211};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q12211}.
CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC {ECO:0000305}.
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DR EMBL; CR382129; CAG82083.1; -; Genomic_DNA.
DR RefSeq; XP_501773.1; XM_501773.1.
DR AlphaFoldDB; Q6CC39; -.
DR SMR; Q6CC39; -.
DR STRING; 4952.CAG82083; -.
DR EnsemblFungi; CAG82083; CAG82083; YALI0_C12749g.
DR GeneID; 2909512; -.
DR KEGG; yli:YALI0C12749g; -.
DR VEuPathDB; FungiDB:YALI0_C12749g; -.
DR HOGENOM; CLU_021971_1_0_1; -.
DR InParanoid; Q6CC39; -.
DR OMA; AVMIGYC; -.
DR Proteomes; UP000001300; Chromosome C.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IBA:GO_Central.
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 3: Inferred from homology;
KW Isomerase; Metal-binding; mRNA processing; Nucleus; Reference proteome;
KW tRNA processing; Zinc.
FT CHAIN 1..528
FT /note="tRNA pseudouridine synthase 1"
FT /id="PRO_0000057529"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P07649"
SQ SEQUENCE 528 AA; 60051 MW; 63792327581C3FAA CRC64;
MSEPTTTPVV GNSASGDSAE QHDLGQKRGK GGNWNRPRGD HQAKKQKMDR RGDRQREQEK
QGEGRDTRRK TDGPLVADEV RQPKRKVACM IGYCGTGYHG MQLNPPQKTI EGDIFQAFVK
AGAISQNNAD DPKKSAFMRA ARTDKGVHAA GNVISLKMII EDENIVEKIN SHLPEQLRVW
GVSRTNKAFE CRKLCSSRVY EYLMPTYSFL NPRPGTVMSE KLLKDGTSPD EEGKKYWESV
AADLESQGVS YDEWMKRACI DEIKGEETKE VAESEVKTDS KTDAATLEKI KAVERRHREE
FRISGERLAK IREILKIYEG THNFHNFTLG KAFKDPSAMR TMKSLTCSDP FLIDGTEWVS
IKIHGQSFML HQIRKMISMV ALSVRCNADP QKLIPQTFEK ARINIPKAPA LGLLLERPVY
DSYNKKLQGE FGREGVHFDN WNDQIEAFKH KFIYDKIYAE EKGQHVFHAF FSFVDVFTGD
ASFDFLLKQG ITKECTTDYM NKKAKEEGKE IKKLEEDDDE VANEQNEG
