ID PUS1_CANAL Reviewed; 612 AA.
AC Q59S63; A0A1D8PPW4;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 27-MAR-2024, entry version 105.
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=CAALFM_C602350CA;
GN ORFNames=CaO19.10981, CaO19.3477;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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; CP017628; AOW30170.1; -; Genomic_DNA.
DR RefSeq; XP_019331009.1; XM_019475464.1.
DR AlphaFoldDB; Q59S63; -.
DR SMR; Q59S63; -.
DR BioGRID; 1228947; 1.
DR STRING; 237561.Q59S63; -.
DR EnsemblFungi; C6_02350C_A-T; C6_02350C_A-T-p1; C6_02350C_A.
DR GeneID; 3645881; -.
DR KEGG; cal:CAALFM_C602350CA; -.
DR CGD; CAL0000183350; orf19.10981.
DR VEuPathDB; FungiDB:C6_02350C_A; -.
DR eggNOG; KOG2553; Eukaryota.
DR HOGENOM; CLU_021971_0_0_1; -.
DR InParanoid; Q59S63; -.
DR OMA; NKAFDCR; -.
DR OrthoDB; 12038at2759; -.
DR Proteomes; UP000000559; Chromosome 6.
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; 3.30.70.660; 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..612
FT /note="tRNA pseudouridine synthase 1"
FT /id="PRO_0000057525"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 210
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P07649"
SQ SEQUENCE 612 AA; 70099 MW; E78819E09010846B CRC64;
MGDKFSVPTN QSKERQPIVK KKKKKKRTNI YSYILIISFP VIDQFQMSES LNIQELTDNS
SIIPIPTEST DVQDVTSVSN KDTTTTTTTT TTTTESTTRV RKSSPSPSAN ENDKKRLKKE
FQPRQKIEYT PLVDENGQPI PKAPRKPKRK VAVMLGYCGT GYNGMQVQND PNVKTIEKDI
YDAMATAGAI SAENAVDLKK SGFQRAARTD KGVHAAGNVI SLKMIIEDPE IINKINDLLP
KQIRIWGIQR TTKGFDCRKC CSSRIYEYLL PTFSLLPPKP KSVLSELVKE KKLENPDLFE
DDQEGIDWWE NVKSKILASG ITQEQIDSIT SSYDEQQQQQ QQQQQQQADE EERDISELSF
TKLIKQIKTI ENQSRRSYRI SSSRLQHFRE VMKQYEGTHN FHNFTVGKPF KDTSANRFMI
KTIVSDPFVI EGTEWISIKI HGQSFMLHQI RKMIAMAALV VRLSLPCGII NNFFQSTKIN
IPKAPALGLL LENPVFDGYN IKLTKSDYEP IDFTKFDKEM NEFKMKYIYD KIYAEESKEN
IFYGFFGYID AYRGNKNEDG EPIQNGASIF DFLFNYTERV ENTKNKDAKN TSKTEESKPE
ESKPEESKSE QS
//
