PUS7_BOVIN
ID PUS7_BOVIN Reviewed; 659 AA.
AC Q08DI8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Pseudouridylate synthase 7 homolog {ECO:0000305};
DE EC=5.4.99.- {ECO:0000250|UniProtKB:Q96PZ0};
GN Name=PUS7 {ECO:0000250|UniProtKB:Q96PZ0};
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=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pseudouridylate synthase that catalyzes pseudouridylation of
CC RNAs. Acts as a regulator of protein synthesis in embryonic stem cells
CC by mediating pseudouridylation of RNA fragments derived from tRNAs
CC (tRFs): pseudouridylated tRFs inhibit translation by targeting the
CC translation initiation complex. Also catalyzes pseudouridylation of
CC mRNAs: mediates pseudouridylation of mRNAs with the consensus sequence
CC 5'-UGUAG-3'. Acts as a regulator of pre-mRNA splicing by mediating
CC pseudouridylation of pre-mRNAs at locations associated with
CC alternatively spliced regions. Pseudouridylation of pre-mRNAs near
CC splice sites directly regulates mRNA splicing and mRNA 3'-end
CC processing. In addition to mRNAs and tRNAs, binds other types of RNAs,
CC such as snRNAs, Y RNAs and vault RNAs, suggesting that it can catalyze
CC pseudouridylation of many RNA types. {ECO:0000250|UniProtKB:Q96PZ0}.
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:Q96PZ0};
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;
CC Evidence={ECO:0000250|UniProtKB:Q96PZ0};
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:Q96PZ0};
CC -!- SUBUNIT: Interacts with SIRT1. {ECO:0000250|UniProtKB:Q96PZ0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96PZ0}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruD family.
CC {ECO:0000305}.
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DR EMBL; BC123723; AAI23724.1; -; mRNA.
DR RefSeq; NP_001070407.1; NM_001076939.1.
DR AlphaFoldDB; Q08DI8; -.
DR SMR; Q08DI8; -.
DR STRING; 9913.ENSBTAP00000055411; -.
DR PaxDb; Q08DI8; -.
DR PRIDE; Q08DI8; -.
DR GeneID; 615644; -.
DR KEGG; bta:615644; -.
DR CTD; 54517; -.
DR eggNOG; KOG2339; Eukaryota.
DR InParanoid; Q08DI8; -.
DR OrthoDB; 955294at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; 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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; ISS:UniProtKB.
DR GO; GO:2000380; P:regulation of mesoderm development; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; Isomerase; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; tRNA processing.
FT CHAIN 1..659
FT /note="Pseudouridylate synthase 7 homolog"
FT /id="PRO_0000316784"
FT DOMAIN 368..578
FT /note="TRUD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00342"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..97
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 292
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q57261"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96PZ0"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PZ0"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PZ0"
SQ SEQUENCE 659 AA; 74594 MW; 40DD960E3C83CACF CRC64;
MEMTEMTSVS LKRGSVAIED NDSVAPAEEA KRQKVSGCCP TTGQDGIENS SLPSSEKVPG
PPETAEQGEK NSEVPSEEEE EEDGLSEEEE EEEEEAESFA DMMKHGLTEL DVGITKFVSS
HQGFSGILKE RYSDFVVHEI GRDGRISHLS DLSVPVDEED PSEDVFTVLT AEEKQRLEEL
QLFKNKETSV AIEVIEDTKE KRTIIHQAIK SLFPGLETKT EDREGKKYIV AYHAAGKKAL
ANPRKHSWPK SRGSYCHFVL YKENKDTMDA INLLSKYLRV KPNIFSYMGT KDKRAITVQE
IAVLKITAQR LAHLNKCLMN FKLGNFSYQK NPLKLGELQG NHFTVVLRNI TGTDNQVEQA
MNSLKEIGFI NYYGMQRFGT TAVPTYQVGR AILQNSWAEV MDLILKPRSG AEKGYLVKCR
EEWAKSKDPA AALRKLPVKR CVEGQLLRGL SKYGMKNIVS AFGIIPRNNR LMYIHSYQSY
VWNNMVSKRI DEYGLKPVPG DLVLKGATAT FIEEDDVNNY SIHDVVMPLP GFDVIYPKHK
ISEAYREMLT ADNLDIDNMR HKIRDYSLSG AYRKIIIRPQ NVSWEVVAYD DPKIPLFNTD
VDNLEGRPPP VFASEGKYRA LKMDFSLPPS TYATMAIREV LKMDTSIKNQ TQLNTTWLR
