PUS4_SCHPO
ID PUS4_SCHPO Reviewed; 407 AA.
AC O59721;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=tRNA pseudouridine synthase 4;
DE EC=5.4.99.25 {ECO:0000250|UniProtKB:P48567};
DE AltName: Full=tRNA pseudouridine(55) synthase;
DE Short=Psi55 synthase;
DE AltName: Full=tRNA pseudouridylate synthase 4;
DE AltName: Full=tRNA-uridine isomerase 4;
GN ORFNames=SPBC11C11.10, SPBC3B8.13c;
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).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291; THR-293; SER-296 AND
RP THR-406, AND 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: Responsible for synthesis of pseudouridine from uracil-55 in
CC the psi GC loop of transfer RNAs. Also catalyzes pseudouridylation of
CC mRNAs with the consensus sequence 5'-GGUUCRA-3'.
CC {ECO:0000250|UniProtKB:P48567}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(55) in tRNA = pseudouridine(55) in tRNA;
CC Xref=Rhea:RHEA:42532, Rhea:RHEA-COMP:10101, Rhea:RHEA-COMP:10102,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.25;
CC Evidence={ECO:0000250|UniProtKB:P48567};
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:P48567};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P48567}.
CC Mitochondrion {ECO:0000250|UniProtKB:P48567}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA20692.1; -; Genomic_DNA.
DR PIR; T39326; T39326.
DR RefSeq; NP_596400.1; NM_001022320.2.
DR AlphaFoldDB; O59721; -.
DR SMR; O59721; -.
DR BioGRID; 276567; 28.
DR STRING; 4896.SPBC11C11.10.1; -.
DR iPTMnet; O59721; -.
DR MaxQB; O59721; -.
DR PaxDb; O59721; -.
DR PRIDE; O59721; -.
DR EnsemblFungi; SPBC11C11.10.1; SPBC11C11.10.1:pep; SPBC11C11.10.
DR GeneID; 2540023; -.
DR KEGG; spo:SPBC11C11.10; -.
DR PomBase; SPBC11C11.10; -.
DR VEuPathDB; FungiDB:SPBC11C11.10; -.
DR eggNOG; KOG2529; Eukaryota.
DR HOGENOM; CLU_032087_4_2_1; -.
DR InParanoid; O59721; -.
DR OMA; QVKIGHG; -.
DR PhylomeDB; O59721; -.
DR PRO; PR:O59721; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005739; C:mitochondrion; ISS:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IC:PomBase.
DR HAMAP; MF_01080; TruB_bact; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR002501; PsdUridine_synth_N.
DR InterPro; IPR014780; tRNA_psdUridine_synth_TruB.
DR PANTHER; PTHR13767; PTHR13767; 1.
DR Pfam; PF01509; TruB_N; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
PE 1: Evidence at protein level;
KW Isomerase; Mitochondrion; Nucleus; Phosphoprotein; Reference proteome;
KW tRNA processing.
FT CHAIN 1..407
FT /note="tRNA pseudouridine synthase 4"
FT /id="PRO_0000121975"
FT REGION 83..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 115
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P60340"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 293
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 406
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 407 AA; 45166 MW; D0CB88C503C774DB CRC64;
MTVTNTYNPT LFFTRVVFQR ITKFTAKANE ENEILFYALF VADLCLDMKG GLIAINKPSG
RTSAQCLNEL KKIISNSELA QYFRPAPPHP NDRNRRRRKS NRLPDIKIGH GGTLDPLASG
VLVVGLGTGT KQLSSLLSCM KTYRATALFG CSTDTYDSAG KIIKIAVHIP TKEEILSGLD
AFRGDISQLP PLYSALHIQG KRLYEYAREG IPLPESIKAR SMHCEELILK DFIPKEEHTY
TDPDEFASKE AIESEELLRP IEGGAERHDL LAKTEQDINP QDGDEKINAK SPTTNSVTDV
AKDQTVTNPK KRKFEVTDLA RGSRPAIGPI AVLDMTVSSG FYVRSLIHDL GRQVNSEAHM
VDLVRLKQGS FALDDENCFD FSEFSAPGWE EKLAAAFKID LKGDETS
