ID   PUS7_SCHPO              Reviewed;         680 AA.
AC   O74343;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Multisubstrate pseudouridine synthase 7;
DE            EC=5.4.99.- {ECO:0000250|UniProtKB:Q08647};
DE            EC=5.4.99.27 {ECO:0000250|UniProtKB:Q08647};
DE   AltName: Full=RNA pseudouridylate synthase 7;
DE   AltName: Full=RNA-uridine isomerase 7;
GN   Name=pus7; ORFNames=SPBC1A4.09;
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: Catalyzes pseudouridylation at position 35 in U2 snRNA stem-
CC       loop II region which induces particular conformation of the mRNA-U2
CC       snRNA duplex and places the nucleophile in an accessible position for
CC       the first step of splicing. Also catalyzes pseudouridylation at
CC       position 56 in U2 snRNA. Catalyzes also pseudouridylation at position
CC       50 in 5S rRNA, position 13 in cytoplasmic tRNAs, and position 35 in
CC       pre-tRNA(Tyr). Pseudouridine residues in tRNAs may stabilize the local
CC       RNA conformation, favor interactions with protein partners and play an
CC       important role in the stabilization of the codon-anticodon interaction
CC       with mRNA. Also catalyzes pseudouridylation of mRNAs in response to
CC       heat shock: mediates pseudouridylation of mRNAs with the consensus
CC       sequence 5'-UGUAR-3'. {ECO:0000250|UniProtKB:Q08647}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine in 5S rRNA = pseudouridine in 5S rRNA;
CC         Xref=Rhea:RHEA:47036, Rhea:RHEA-COMP:11730, Rhea:RHEA-COMP:11731,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC         Evidence={ECO:0000250|UniProtKB:Q08647};
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:Q08647};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine(13) in tRNA = pseudouridine(13) in tRNA;
CC         Xref=Rhea:RHEA:42540, Rhea:RHEA-COMP:10105, Rhea:RHEA-COMP:10106,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.27;
CC         Evidence={ECO:0000250|UniProtKB:Q08647};
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:Q08647};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q08647}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q08647}.
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase TruD family.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAA20114.1; -; Genomic_DNA.
DR   PIR; T39858; T39858.
DR   RefSeq; NP_595812.1; NM_001021715.2.
DR   AlphaFoldDB; O74343; -.
DR   SMR; O74343; -.
DR   STRING; 4896.SPBC1A4.09.1; -.
DR   iPTMnet; O74343; -.
DR   MaxQB; O74343; -.
DR   PaxDb; O74343; -.
DR   PRIDE; O74343; -.
DR   EnsemblFungi; SPBC1A4.09.1; SPBC1A4.09.1:pep; SPBC1A4.09.
DR   GeneID; 2540668; -.
DR   KEGG; spo:SPBC1A4.09; -.
DR   PomBase; SPBC1A4.09; pus7.
DR   VEuPathDB; FungiDB:SPBC1A4.09; -.
DR   eggNOG; KOG2339; Eukaryota.
DR   HOGENOM; CLU_005281_0_2_1; -.
DR   InParanoid; O74343; -.
DR   OMA; CCETLPE; -.
DR   PhylomeDB; O74343; -.
DR   PRO; PR:O74343; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0000455; P:enzyme-directed rRNA pseudouridine synthesis; ISO:PomBase.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0001522; P:pseudouridine synthesis; IBA:GO_Central.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   GO; GO:0031120; P:snRNA pseudouridine synthesis; ISO:PomBase.
DR   GO; GO:0031119; P:tRNA pseudouridine synthesis; ISO:PomBase.
DR   Gene3D; 3.30.2350.20; -; 2.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR001656; PsdUridine_synth_TruD.
DR   InterPro; IPR020119; PsdUridine_synth_TruD_CS.
DR   InterPro; IPR011760; PsdUridine_synth_TruD_insert.
DR   InterPro; IPR042214; TruD_catalytic.
DR   PANTHER; PTHR13326; PTHR13326; 1.
DR   Pfam; PF01142; TruD; 1.
DR   PIRSF; PIRSF037016; Pseudouridin_synth_euk_prd; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
DR   TIGRFAMs; TIGR00094; tRNA_TruD_broad; 1.
DR   PROSITE; PS50984; TRUD; 1.
DR   PROSITE; PS01268; UPF0024; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; Ribosome biogenesis; rRNA processing; tRNA processing.
FT   CHAIN           1..680
FT                   /note="Multisubstrate pseudouridine synthase 7"
FT                   /id="PRO_0000152560"
FT   DOMAIN          358..596
FT                   /note="TRUD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00342"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          206..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        277
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q57261"
SQ   SEQUENCE   680 AA;  76438 MW;  B4A52DAECEA1B9A6 CRC64;
     MSQENHVDVP RKRIRIDQSE SSRNLERNGL EDEANAPSDL SGQKFYMTES DVGIDAFLNP
     NLPSIDGIIK ARFTDFAVFE VDTDGNIVHL TDMEAHDPIL SKATGDKETE DAKDSSNQDI
     SNDQKAPSFK EQEPATLPIL PNDLQSIIPK GIGNEFIQSL HKLSVGEITD PISLILPENT
     PPMDKGQRTI LHQFIRNNFS GLESSTKGNG TFTVSKTTRK NQPRSRRDPR LSWKALGGEY
     CHFHLYKENR DSMDCLGKIA RLLKVPTRTL SIAGTKDRRG VTCQRVAIHH VRASRLAQLN
     SGSLKNSTYG FLLGNYSYKN SNLRLGDLKG NEFHIVVRNV ITPKEKVVEA LNSLKEHGFI
     NYFGLQRFGT SSVGTHTIGV RLLQSDWKGA VDLILSPRPE HTGSVKEAID LWHSTHDAEA
     SLRILPRRMI AESSILETWS RSGNQTDYLG AFQRIPRHLR SIYPHAYQSY VWNRVASWRI
     KNLGDRPVVG DLVYSTESNG LSQKSPIVDP EAPDLLEDLP VSSKLSARPI EEDEVNNFSI
     YDIVLPLPGR NVIYPKNETF DIYKSVMNEA SLDPLNMSRK DRELSLPGDY RKLLVRPENM
     EFNFIKYDNM EQQLILTDKD RLENRSISVS SEVGKHTAVT LKFVLPSSAY ATMALREALR
     TATASGDQRM LMPAVLKDSI