TRUB1_RAT
ID TRUB1_RAT Reviewed; 341 AA.
AC Q5M934;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Pseudouridylate synthase TRUB1 {ECO:0000305};
DE EC=5.4.99.- {ECO:0000250|UniProtKB:Q8WWH5};
DE AltName: Full=TruB pseudouridine synthase homolog 1 {ECO:0000250|UniProtKB:Q8WWH5};
DE AltName: Full=tRNA pseudouridine 55 synthase TRUB1 {ECO:0000305};
DE Short=Psi55 synthase TRUB1 {ECO:0000305};
DE EC=5.4.99.25 {ECO:0000250|UniProtKB:Q8WWH5};
GN Name=Trub1 {ECO:0000312|RGD:1308502};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Pseudouridine synthase that catalyzes pseudouridylation of
CC mRNAs and tRNAs. Mediates pseudouridylation of mRNAs with the consensus
CC sequence 5'-GUUCNANNC-3', harboring a stem-loop structure. Constitutes
CC the major pseudouridine synthase acting on mRNAs. Also catalyzes
CC pseudouridylation of some tRNAs, including synthesis of
CC pseudouridine(55) from uracil-55, in the psi GC loop of a subset of
CC tRNAs. Promotes the processing of pri-let-7 microRNAs (pri-miRNAs)
CC independently of its RNA pseudouridylate synthase activity. Acts by
CC binding to the stem-loop structure on pri-let-7, preventing LIN28-
CC binding (LIN28A and/or LIN28B), thereby enhancing the interaction
CC between pri-let-7 and the microprocessor DGCR8, which mediates miRNA
CC maturation. {ECO:0000250|UniProtKB:Q8WWH5}.
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:Q8WWH5};
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:Q8WWH5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(55) in tRNA = pseudouridine(55) in tRNA;
CC Xref=Rhea:RHEA:42532, Rhea:RHEA-COMP:10101, Rhea:RHEA-COMP:10102,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.25;
CC Evidence={ECO:0000250|UniProtKB:Q8WWH5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42533;
CC Evidence={ECO:0000250|UniProtKB:Q8WWH5};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WWH5}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8WWH5}. Note=Catalyzes
CC pseudouridylation of mRNAs in the nucleus.
CC {ECO:0000250|UniProtKB:Q8WWH5}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
CC {ECO:0000305}.
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DR EMBL; BC087683; AAH87683.1; -; mRNA.
DR RefSeq; NP_001012173.1; NM_001012173.1.
DR AlphaFoldDB; Q5M934; -.
DR SMR; Q5M934; -.
DR STRING; 10116.ENSRNOP00000023309; -.
DR PaxDb; Q5M934; -.
DR PRIDE; Q5M934; -.
DR Ensembl; ENSRNOT00000023309; ENSRNOP00000023309; ENSRNOG00000017321.
DR GeneID; 361775; -.
DR KEGG; rno:361775; -.
DR CTD; 142940; -.
DR RGD; 1308502; Trub1.
DR eggNOG; KOG2529; Eukaryota.
DR GeneTree; ENSGT00940000158962; -.
DR HOGENOM; CLU_032087_1_0_1; -.
DR InParanoid; Q5M934; -.
DR OMA; ELQFIRW; -.
DR OrthoDB; 1535798at2759; -.
DR PhylomeDB; Q5M934; -.
DR TreeFam; TF320759; -.
DR PRO; PR:Q5M934; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017321; Expressed in ovary and 19 other tissues.
DR Genevisible; Q5M934; RN.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0070883; F:pre-miRNA binding; ISS:UniProtKB.
DR GO; GO:0009982; F:pseudouridine synthase activity; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; ISS:UniProtKB.
DR GO; GO:2000633; P:positive regulation of pre-miRNA processing; ISS:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; ISS:UniProtKB.
DR HAMAP; MF_01080; TruB_bact; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR002501; PsdUridine_synth_N.
DR InterPro; IPR014780; tRNA_psdUridine_synth_TruB.
DR PANTHER; PTHR13767; PTHR13767; 1.
DR Pfam; PF01509; TruB_N; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR00431; TruB; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Isomerase; mRNA processing; Nucleus;
KW Reference proteome; tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8WWH5"
FT CHAIN 2..341
FT /note="Pseudouridylate synthase TRUB1"
FT /id="PRO_0000252089"
FT ACT_SITE 112
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8WWH5"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWH5"
SQ SEQUENCE 341 AA; 36404 MW; 1DB4BC933B8692A3 CRC64;
MAAEEAEVVS PLIVDTAPDT SGTAAASLAA AVSAAAAAAR TGSQAQVSKA ALAAKLMSLS
GVFAVHKPKG PTSAELLNRL KEKLLAEAGL PSPEWNKRQK QTLKVGHGGT LDSAAQGVLV
VGIGRGTKML TSMLSGSKRY IATGELGKAT DTLDSTGKVT EEKPYDKITQ EDIEGILQKF
TGNIMQVPPL YSALKKDGQR LSTLMKRGET VEARPARPVT VHSISLLKYQ PPFFTLDVEC
GGGFYIRSLV SDIGKELSSC ATVLELTRTK QGPFTLAQHA LPEDRWTIND IAQSLKRCTS
LLPEELTFKK SKSEPSSDQA LSCGYITLRE TKREDDTVKT L
