PUS1_SCHPO
ID PUS1_SCHPO Reviewed; 534 AA.
AC O94396;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=tRNA pseudouridine synthase 1;
DE EC=5.4.99.- {ECO:0000269|PubMed:11095668};
DE AltName: Full=tRNA pseudouridylate synthase 1;
DE AltName: Full=tRNA-uridine isomerase 1;
GN Name=pus1; Synonyms=lps1; ORFNames=SPCC126.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11095668; DOI=10.1093/nar/28.23.4604;
RA Hellmuth K., Grosjean H., Motorin Y., Deinert K., Hurt E., Simos G.;
RT "Cloning and characterization of the Schizosaccharomyces pombe tRNA:
RT pseudouridine synthase Pus1p.";
RL Nucleic Acids Res. 28:4604-4610(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518; SER-519 AND SER-525, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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) (PubMed:11095668). Catalyzes pseudouridylation at
CC position 44 in U2 snRNA (By similarity). Also catalyzes
CC pseudouridylation of mRNAs (By similarity).
CC {ECO:0000250|UniProtKB:Q12211, ECO:0000269|PubMed:11095668}.
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:0000269|PubMed:11095668};
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:0000269|PubMed:11095668}.
CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC {ECO:0000305}.
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DR EMBL; AJ251329; CAB61835.1; -; mRNA.
DR EMBL; CU329672; CAA22472.1; -; Genomic_DNA.
DR PIR; T40907; T40907.
DR RefSeq; NP_588446.1; NM_001023437.2.
DR AlphaFoldDB; O94396; -.
DR SMR; O94396; -.
DR BioGRID; 275654; 34.
DR STRING; 4896.SPCC126.03.1; -.
DR iPTMnet; O94396; -.
DR MaxQB; O94396; -.
DR PaxDb; O94396; -.
DR PRIDE; O94396; -.
DR EnsemblFungi; SPCC126.03.1; SPCC126.03.1:pep; SPCC126.03.
DR GeneID; 2539082; -.
DR KEGG; spo:SPCC126.03; -.
DR PomBase; SPCC126.03; pus1.
DR VEuPathDB; FungiDB:SPCC126.03; -.
DR eggNOG; KOG2553; Eukaryota.
DR HOGENOM; CLU_021971_1_0_1; -.
DR InParanoid; O94396; -.
DR OMA; YQLCDSR; -.
DR PhylomeDB; O94396; -.
DR BRENDA; 5.4.99.B22; 5613.
DR PRO; PR:O94396; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005634; C:nucleus; IGI:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009982; F:pseudouridine synthase activity; IDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0106032; F:snRNA pseudouridine synthase activity; EXP:PomBase.
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; EXP:PomBase.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IDA:PomBase.
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 1: Evidence at protein level;
KW Isomerase; Metal-binding; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..534
FT /note="tRNA pseudouridine synthase 1"
FT /id="PRO_0000057528"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..534
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 103
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P07649"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 534 AA; 60324 MW; AF76684C952C2C8D CRC64;
MGRGGKRTWY NGDRREAKRN RPNSIYNGEG RPENLVVGEK KPKRKVACLV GYCGSGYHGM
QLNPPSKTIE GDLFDAFVKA GAVSSYNADD PKKVALARAA RTDKGVHAAG NVISLKLIME
DEKLIEKVNE HLPPSIRLWD VIRTINSFNP RTYCESRIYE YMVPTYAFVP PKPSSILGNC
IMKNSPMPAE PINKENINQL SRSLFYEEGK EFWDDYDIAA KEILSLYEQD PEGFVNPYSK
RGAAALANSE NNKGSEAGVS AKTNPDMDSD SSAIVNEFLK PDSVEDESAG SKIDPSYRLE
RALKHIEVLK LKNYRISADR LSVIRETLNQ YVGVHNFHNF TVGQAFHQKN SNRVIRSFTA
SDPFMIGDTE WISCKVHGQS FMLHQIRKMI ALAILVVRTG CPVERIQDAF KKTKINIPKG
PGFGLLLESP FFKGYNEHKA PENNRDPIDF TKYEQKITAF KHAHIYDKIF LEEARKQVFH
CFLSFIDSYN EEDFSYLSDI GITEKTQEVS SKLPDVLSSD EEEDSAENKD DLEG
