ID   PUS1_KLULA              Reviewed;         553 AA.
AC   Q6CWQ8;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 113.
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=KLLA0B02244g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC   WM37;
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; CR382122; CAH02024.1; -; Genomic_DNA.
DR   RefSeq; XP_451631.1; XM_451631.1.
DR   AlphaFoldDB; Q6CWQ8; -.
DR   SMR; Q6CWQ8; -.
DR   STRING; 284590.Q6CWQ8; -.
DR   PaxDb; 284590-Q6CWQ8; -.
DR   GeneID; 2897526; -.
DR   KEGG; kla:KLLA0_B02244g; -.
DR   eggNOG; KOG2553; Eukaryota.
DR   HOGENOM; CLU_021971_0_1_1; -.
DR   InParanoid; Q6CWQ8; -.
DR   OMA; NKAFDCR; -.
DR   Proteomes; UP000000598; Chromosome B.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:InterPro.
DR   CDD; cd02568; PseudoU_synth_PUS1_PUS2; 1.
DR   Gene3D; 3.30.70.660; Pseudouridine synthase I, catalytic domain, C-terminal subdomain; 1.
DR   Gene3D; 3.30.70.580; Pseudouridine synthase I, catalytic domain, N-terminal subdomain; 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   NCBIfam; TIGR00071; hisT_truA; 1.
DR   PANTHER; PTHR11142; PSEUDOURIDYLATE SYNTHASE; 1.
DR   PANTHER; PTHR11142:SF4; PSEUDOURIDYLATE SYNTHASE 1 HOMOLOG; 1.
DR   Pfam; PF01416; PseudoU_synth_1; 1.
DR   SUPFAM; SSF55120; Pseudouridine synthase; 1.
PE   3: Inferred from homology;
KW   Isomerase; Metal-binding; mRNA processing; Nucleus; Reference proteome;
KW   tRNA processing; Zinc.
FT   CHAIN           1..553
FT                   /note="tRNA pseudouridine synthase 1"
FT                   /id="PRO_0000057527"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..538
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        158
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P07649"
SQ   SEQUENCE   553 AA;  63660 MW;  569D70FDB3B1200C CRC64;
     MSEEQNLRPV YDDDQPGEDT YKRGAIYKQT RSRKADYEDG ENSEKRQKPN DTDNGPTAVV
     TDLSNEKKET RSKDKDESVA LAVDADGNPI PQEVRLPKRK VAVMIGYCGT GYHGMQYNPP
     NDTIEKELFE AFVRAGAISK ANSTDLKKNG FQRAARTDKG VHAGGNVISL KLIIEDPEVK
     EKINNELPDQ IRVWDISRVN KAFDCRKMCS SRWYEYLLPT YSLIGPKPST YLYNEIEASK
     KEIPNVIQDD VESAQFWEAF STEAESKFTK EELEEIAAFV MPKDSFDENN ETYQKSKAFK
     KLEAEHKRAY RISKERLDRF RSALKQYEGT FNFHNFTLGK DFNDPSAKRF MKQITVSEPF
     VIGEAKTEWV SIKIHGQSFM LHQIRKMISM ATLITRCFSP LERIRQAYGQ EKINIPKAPA
     LGLLLEAPVY DGYNTRLQEF GYDPIDFSKY QSEMDTFKMK HIYDKIYLEE VNENVFNAFF
     SYIDTFNPSY NISQEQQQLK GQELQQPSQA VELVTEDLEQ KAPSDPTPSD EKGKKPQRPI
     FDFLTARGIQ LQD
//