PUS1_CANGA
ID PUS1_CANGA Reviewed; 549 AA.
AC Q6FV05;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=CAGL0E05764g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380951; CAG58858.1; -; Genomic_DNA.
DR RefSeq; XP_445939.1; XM_445939.1.
DR AlphaFoldDB; Q6FV05; -.
DR SMR; Q6FV05; -.
DR STRING; 5478.XP_445939.1; -.
DR EnsemblFungi; CAG58858; CAG58858; CAGL0E05764g.
DR GeneID; 2887466; -.
DR KEGG; cgr:CAGL0E05764g; -.
DR CGD; CAL0128858; CAGL0E05764g.
DR VEuPathDB; FungiDB:CAGL0E05764g; -.
DR eggNOG; KOG2553; Eukaryota.
DR HOGENOM; CLU_021971_0_1_1; -.
DR InParanoid; Q6FV05; -.
DR OMA; AVMIGYC; -.
DR Proteomes; UP000002428; Chromosome E.
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:EnsemblFungi.
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; IEA:EnsemblFungi.
DR GO; GO:0031120; P:snRNA pseudouridine synthesis; IEA:EnsemblFungi.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:EnsemblFungi.
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..549
FT /note="tRNA pseudouridine synthase 1"
FT /id="PRO_0000057526"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 146
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P07649"
SQ SEQUENCE 549 AA; 62100 MW; 49E402EDE0996CB7 CRC64;
MEEVAPEQVQ EVQGNTEAHI DSTTASTAPT EALPSDKQSR KANEIDSMAD GAPAEKKQKT
DQRQIIREPK LDDNGNPIPR EPRLPKRKVA VMIGYCGTGY HGMQYNPPNP TIEAALFKAF
VDAGAISKAN SNDLKKNNFM RAARTDKGVH AGGNLISLKM IIEDPEIMDK INANLPEGIR
IWDIERVNKA FDCRKMCSSR WYEYLLPTYS LIGPKPGTIL NNDIESSKTE LPGVLDEDLE
SKEFWENFEA AAKKEFTPEE IAAIKDYSPP PREEFDDQEE LYQKVKQWKL LENTHRRQYR
ISEMKLNKFR AAMNQYLGAH NFHNFTLGKE FKDPSAIRFM KEIKVSDPFV IGDAKAEWVS
IKIHGQSFML HQIRKMISMA TLIARCGTPV ERISQAFGPQ KINIPKAPAL GLLLEAPVFE
SYNKRLEKFG YKPIDFSKYQ EKVDAFKMKH IYDKIYAEEV SDNVFNAFFS YIDSFNKVTG
AQTEESAESN KPATKSIFEF LSAHGIPGID YGKNEKEDSN KESSNDQVNK ESAPATSKPA
EAVEQTEKN
