ID   RUSD4_XENTR             Reviewed;         324 AA.
AC   Q28C59;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Pseudouridylate synthase RPUSD4, mitochondrial {ECO:0000305};
DE            EC=5.4.99.- {ECO:0000250|UniProtKB:Q96CM3};
DE   AltName: Full=RNA pseudouridylate synthase domain-containing protein 4 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=rpusd4 {ECO:0000250|UniProtKB:Q96CM3};
GN   ORFNames=TEgg022l16.1 {ECO:0000303|Ref.1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes uridine to pseudouridine isomerization
CC       (pseudouridylation) of different mitochondrial RNA substrates. Acts on
CC       position 1397 in 16S mitochondrial ribosomal RNA (16S mt-rRNA). This
CC       modification is required for the assembly of 16S mt-rRNA into a
CC       functional mitochondrial ribosome. Acts on position 39 in mitochondrial
CC       tRNA(Phe). Also catalyzes pseudouridylation of mRNAs in nucleus: acts
CC       as a regulator of pre-mRNA splicing by mediating pseudouridylation of
CC       pre-mRNAs at locations associated with alternatively spliced regions.
CC       Pseudouridylation of pre-mRNAs near splice sites directly regulates
CC       mRNA splicing and mRNA 3'-end processing.
CC       {ECO:0000250|UniProtKB:Q96CM3}.
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:Q96CM3};
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:Q96CM3};
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:Q96CM3};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q96CM3}. Nucleus {ECO:0000250|UniProtKB:Q96CM3}.
CC       Cytoplasm {ECO:0000250|UniProtKB:Q96CM3}. Note=Mainly localizes to
CC       mitochondrion. Localizes to mitochondrial RNA granules, platforms for
CC       post-transcriptional RNA modification and ribosome assembly. Also found
CC       in nucleus and cytoplasm. {ECO:0000250|UniProtKB:Q96CM3}.
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC       {ECO:0000305}.
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DR   EMBL; CR942440; CAJ83700.1; -; mRNA.
DR   RefSeq; NP_001039205.1; NM_001045740.1.
DR   AlphaFoldDB; Q28C59; -.
DR   SMR; Q28C59; -.
DR   GeneID; 734064; -.
DR   KEGG; xtr:734064; -.
DR   CTD; 84881; -.
DR   Xenbase; XB-GENE-6455737; rpusd4.
DR   InParanoid; Q28C59; -.
DR   OrthoDB; 1378690at2759; -.
DR   Proteomes; UP000008143; Chromosome 9.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IBA:GO_Central.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd02869; PseudoU_synth_RluA_like; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR006224; PsdUridine_synth_RluC/D_CS.
DR   InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR   Pfam; PF00849; PseudoU_synth_2; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
DR   PROSITE; PS01129; PSI_RLU; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Isomerase; Mitochondrion; mRNA processing; mRNA splicing;
KW   Nucleus; Reference proteome; rRNA processing; Transit peptide;
KW   tRNA processing.
FT   TRANSIT         1..11
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           12..324
FT                   /note="Pseudouridylate synthase RPUSD4, mitochondrial"
FT                   /id="PRO_0000300829"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000250|UniProtKB:P0AA39"
SQ   SEQUENCE   324 AA;  35724 MW;  3904E4B14E5F76D2 CRC64;
     MAAAGGGATR GARMLAERIR AERKVLEGAA RETSRKNAPT IVYLRELKSQ VVREDPELVL
     VNKPHGLPVH GGPTVERSVA SLLPALAKHH FGWKAEPLKL CHRLDRDTTG ALILARTTEA
     AERVQQALRE REVHRVYWAL CLGTPSPREG ILDIPIMEKE TSGPQKHYKM ALSPRFRVSE
     EGAVERVRVP RSAHEAVTRY RTLGAASGAS LVELHPITGV KHQLRVHLAL GLNCPILGDH
     KYSHWGRLAP QKPPDSVLRA LGLTVPQART LSLHLHAVQL TLPSSDGSTP IVLQCPLPYT
     FRKTLRKLRI PPPDLESLQP PPTD