PUS2_SCHPO
ID PUS2_SCHPO Reviewed; 451 AA.
AC O94295;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=tRNA pseudouridine synthase 2;
DE EC=5.4.99.-;
DE AltName: Full=tRNA pseudouridylate synthase 2;
DE AltName: Full=tRNA-uridine isomerase 2;
GN Name=pus2; ORFNames=SPBC887.11;
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 [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).
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). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA21896.1; -; Genomic_DNA.
DR PIR; T40736; T40736.
DR RefSeq; NP_596485.1; NM_001022405.2.
DR AlphaFoldDB; O94295; -.
DR SMR; O94295; -.
DR BioGRID; 277750; 13.
DR STRING; 4896.SPBC887.11.1; -.
DR MaxQB; O94295; -.
DR PaxDb; O94295; -.
DR EnsemblFungi; SPBC887.11.1; SPBC887.11.1:pep; SPBC887.11.
DR GeneID; 2541236; -.
DR KEGG; spo:SPBC887.11; -.
DR PomBase; SPBC887.11; pus2.
DR VEuPathDB; FungiDB:SPBC887.11; -.
DR eggNOG; KOG2553; Eukaryota.
DR HOGENOM; CLU_021971_0_0_1; -.
DR InParanoid; O94295; -.
DR OMA; WEWIPVT; -.
DR PhylomeDB; O94295; -.
DR PRO; PR:O94295; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009982; F:pseudouridine synthase activity; ISO:PomBase.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; ISO: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 3: Inferred from homology;
KW Isomerase; Metal-binding; Nucleus; Reference proteome; tRNA processing;
KW Zinc.
FT CHAIN 1..451
FT /note="tRNA pseudouridine synthase 2"
FT /id="PRO_0000057531"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 97
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 451 AA; 52272 MW; CAA6F1939CE5480F CRC64;
MTSISKRKNQ QEHIPAEDLE TPKLPKREKI EGTKESNKVR IIILLGYSGY GYHGIQINNP
LKTIEGDVVA VLKKLGYLKT NNIDAEHLCI ARAARTDKGV HTLRNLISLN LFVDKPLDIS
LLKTELNEAL CSQIRVWSVF PAPKYFNPRI SCESRTYEYL IPSFALLPPK PSCPLFKKMQ
KNLSRKLDNE LERNLVYSMN DLISFWNTVK LKQKEIQEMF DTNKDAFTNP FKGMFYEKPI
PAGIVIPPQA KLKKALKQAE YYCYMNYRIK EDRLKVLQQL LKKYEGRHNF HNFTVTDDST
SPSNYRFIES VTCGTPFVYE NWEWIPVTIK GNSFMLNQIR KMMAHVLMII RSCAPTGLID
KAFDPNITMN ISKSPGHVLL LKDIKFSSYN DSVTDGLEKI QFDCFEEDIL SLKIKTIYPD
IIKLEQKEKL FFSFLSYIDQ HTGHQFDYLF G
