ID   RUSD3_BOVIN             Reviewed;         344 AA.
AC   Q2TBK7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Mitochondrial mRNA pseudouridine synthase RPUSD3;
DE            EC=5.4.99.-;
DE   AltName: Full=RNA pseudouridylate synthase domain-containing protein 3;
DE   Flags: Precursor;
GN   Name=RPUSD3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes uridine to pseudouridine isomerization
CC       (pseudouridylation) of specific mitochondrial mRNAs (mt-mRNAs), a post-
CC       transcriptional modification necessary for their translation. Acts at
CC       position 390 in COXI mt-mRNA and at position 697-699 in mitochondrial
CC       COXIII mt-mRNA. As a component of a functional protein-RNA module,
CC       consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S
CC       mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S mt-rRNA
CC       abundance and may play a role in mitochondrial ribosome biogenesis.
CC       {ECO:0000250|UniProtKB:Q6P087}.
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:Q6P087};
CC   -!- SUBUNIT: Forms a regulatory protein-RNA complex, consisting of RCC1L,
CC       NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mt-rRNA.
CC       {ECO:0000250|UniProtKB:Q6P087}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q6P087}. Note=Localizes to mitochondrial RNA
CC       granules, platforms for post-transcriptional RNA modification and
CC       ribosome assembly. {ECO:0000250|UniProtKB:Q6P087}.
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC       {ECO:0000305}.
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DR   EMBL; BC110000; AAI10001.1; -; mRNA.
DR   RefSeq; NP_001033650.1; NM_001038561.2.
DR   AlphaFoldDB; Q2TBK7; -.
DR   SMR; Q2TBK7; -.
DR   STRING; 9913.ENSBTAP00000010478; -.
DR   PaxDb; Q2TBK7; -.
DR   GeneID; 534606; -.
DR   KEGG; bta:534606; -.
DR   CTD; 285367; -.
DR   eggNOG; KOG1919; Eukaryota.
DR   InParanoid; Q2TBK7; -.
DR   OrthoDB; 1378690at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0070131; P:positive regulation of mitochondrial translation; ISS:UniProtKB.
DR   GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR   CDD; cd02869; PseudoU_synth_RluA_like; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR   Pfam; PF00849; PseudoU_synth_2; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
PE   2: Evidence at transcript level;
KW   Isomerase; Mitochondrion; mRNA processing; Phosphoprotein;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..41
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..344
FT                   /note="Mitochondrial mRNA pseudouridine synthase RPUSD3"
FT                   /id="PRO_0000300821"
FT   REGION          29..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         64
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P087"
SQ   SEQUENCE   344 AA;  37008 MW;  ACB8EDFF73CCD0B4 CRC64;
     MGGWRVLGQA SGGWRRGLGI RATSTAAGFG TKARHQLQRR GASKPSDPPG DQPFPGLLRP
     GTFSREELVD VLRAAVVDSK GPLVTLNKPQ GLPVTGKPGE LTLLSVLPEL SRSLGLGEQE
     VQVVRASGKE ASGLVLLSSC SQTASRLQKF FTHSRRARKP TATYCAVTDG IPVTSEGKIQ
     AALKLEHIDG VNLVVPVQSP SRKDIMEGVK RTLSHFRVVA TGSGCALVQL QPLTVFPSQL
     QAHMALQLCP VLGDHTYSAR VGTVLGQRFL LPVESTKPQR QVLDEALLGR LCLTASQAAR
     LPLHLHLHCL RLPGARPRDP PIELLAPLPS YFSRTLQCLG LHYQ