PUS1_ASHGO
ID PUS1_ASHGO Reviewed; 528 AA.
AC Q755C8;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 111.
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=AFL105C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 327.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53269.2; -; Genomic_DNA.
DR RefSeq; NP_985445.2; NM_210799.2.
DR AlphaFoldDB; Q755C8; -.
DR SMR; Q755C8; -.
DR STRING; 33169.AAS53269; -.
DR PRIDE; Q755C8; -.
DR EnsemblFungi; AAS53269; AAS53269; AGOS_AFL105C.
DR GeneID; 4621672; -.
DR KEGG; ago:AGOS_AFL105C; -.
DR eggNOG; KOG2553; Eukaryota.
DR HOGENOM; CLU_021971_0_1_1; -.
DR InParanoid; Q755C8; -.
DR OMA; AVMIGYC; -.
DR Proteomes; UP000000591; Chromosome VI.
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:0031120; P:snRNA pseudouridine synthesis; IEA:EnsemblFungi.
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_0000057524"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 126
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P07649"
SQ SEQUENCE 528 AA; 59697 MW; CCEF5C6C1A82775E CRC64;
MPSDASTGYV DDQPGDEAYK RGALYKQTKA RRADYDSDKE AKRPCTEDSD VALAGTSEEK
EARLPKRKVA VMVGYCGTGY HGMQYNPPNR TIEAELFEAF VKAGAISRAN STDLKKNGFM
RAARTDKGVH AGGNVISLKL IIEDPAIKDK INEHLPPGIR VWGISRVNKA FDCRKLCGSR
WYEYLLPTYS FIGPKPNTYL ARTIEQCGEA ASEKPDRDQE SLDFWEAFRK AVDEKFTQEE
QDAIVNYVAP SKEDFDENSG LYQKVKQYKQ MENAHRRSYR VSSAKLARFR EAMKQYLGPH
NFHNYTLGKD FKDPSTVRFM KDITVSDPFV IGEMKTEWVS IKIHGQSFML HQIRKMISMA
TLVARCNCSP ERIAQSYGPQ KINIPKAPAL GLLLESPVYE GYNKRLLEFG YEPIDFRNYQ
KEMDTFKMVH IYDKIYKEEV DENVFNAFFN YIDAFNQVTG AQGEPTKSHD PAKIQLSIID
FLLPCSSSPQ ENASPEAQKA PETPAGDNTI SAEQPKTATE VPTTQSDA
