ID   PUS3_BOVIN              Reviewed;         481 AA.
AC   Q3SX07;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=tRNA pseudouridine(38/39) synthase;
DE            EC=5.4.99.45 {ECO:0000250|UniProtKB:Q9BZE2};
DE   AltName: Full=tRNA pseudouridine synthase 3;
DE   AltName: Full=tRNA pseudouridylate synthase 3;
DE   AltName: Full=tRNA-uridine isomerase 3;
GN   Name=PUS3;
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=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Formation of pseudouridine at position 39 in the anticodon
CC       stem and loop of transfer RNAs. {ECO:0000250|UniProtKB:Q9BZE2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine(38/39) in tRNA = pseudouridine(38/39) in tRNA;
CC         Xref=Rhea:RHEA:42564, Rhea:RHEA-COMP:10117, Rhea:RHEA-COMP:10118,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.45;
CC         Evidence={ECO:0000250|UniProtKB:Q9BZE2};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BZE2}.
CC   -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC       {ECO:0000305}.
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DR   EMBL; BC104569; AAI04570.1; -; mRNA.
DR   RefSeq; NP_001029684.1; NM_001034512.1.
DR   AlphaFoldDB; Q3SX07; -.
DR   SMR; Q3SX07; -.
DR   STRING; 9913.ENSBTAP00000019065; -.
DR   PaxDb; Q3SX07; -.
DR   PRIDE; Q3SX07; -.
DR   GeneID; 515824; -.
DR   KEGG; bta:515824; -.
DR   CTD; 83480; -.
DR   eggNOG; KOG2554; Eukaryota.
DR   InParanoid; Q3SX07; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0009982; F:pseudouridine synthase activity; ISS:UniProtKB.
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:0031119; P:tRNA pseudouridine synthesis; ISS:UniProtKB.
DR   CDD; cd02569; PseudoU_synth_ScPus3; 1.
DR   Gene3D; 3.30.70.580; -; 1.
DR   Gene3D; 3.30.70.660; -; 1.
DR   HAMAP; MF_00171; TruA; 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; IPR041707; Pus3-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   2: Evidence at transcript level;
KW   Acetylation; Isomerase; Nucleus; Phosphoprotein; Reference proteome;
KW   tRNA processing.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZE2"
FT   CHAIN           2..481
FT                   /note="tRNA pseudouridine(38/39) synthase"
FT                   /id="PRO_0000265107"
FT   REGION          29..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        118
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZE2"
FT   MOD_RES         456
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZE2"
SQ   SEQUENCE   481 AA;  55665 MW;  D2956FB95D93F178 CRC64;
     MAENDVDRIQ TEKLLKRVQE LEQEVKRLKK EQANNKDSNI RENSSGAGGK PKRAFDFSAH
     GQRHVALKIA YLGWGYQGFA SQENTSNTIE EKLFEALTKT RLVENRQTSN YHRCGRTDKG
     VSAFGQVISL DLRSHIPKGR DSEHFNLKNE VNDVATEIRY THILNRVLPP DIRVLAWAPV
     ETSFSARFSC LERTYRYFFP RANLDIVTMN YAAQKYVGTH DFRNLCKMDV ANGVINFQRT
     ILSAQVQRVG QNLGEEGWQE PFQLCQFEVT GQAFLYHQVR CMMAVLFLIG QGMEKPEVID
     ELLNIEKNPQ KPQYSMAVEF PLVLYDCKFE NIKWIYDREV QEFNVTHLQQ LWANHAVKTQ
     MLYSMLQGLD SVALPCGTGP KMDGMIEWRN VKPSVTKQTS AFVEGVKMRT YKPLMDRPKC
     QGLESRIQHF VRRGRIEHPH LFHEEETKAK RDCSDTLEEE NTVFEKPMKR ICVDTELKSI
     I