TRUB2_XENTR
ID TRUB2_XENTR Reviewed; 325 AA.
AC Q5XGG2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Pseudouridylate synthase TRUB2, mitochondrial {ECO:0000305};
DE EC=5.4.99.- {ECO:0000250|UniProtKB:O95900};
DE AltName: Full=TruB pseudouridine synthase homolog 2 {ECO:0000250|UniProtKB:O95900};
DE AltName: Full=tRNA pseudouridine 55 synthase TRUB2 {ECO:0000305};
DE Short=Psi55 synthase TRUB2 {ECO:0000305};
DE EC=5.4.99.25 {ECO:0000250|UniProtKB:O95900};
DE Flags: Precursor;
GN Name=Trub2 {ECO:0000250|UniProtKB:O95900};
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=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Minor enzyme contributing to the isomerization of uridine to
CC pseudouridine (pseudouridylation) of specific mitochondrial mRNAs (mt-
CC mRNAs) such as COXI and COXIII mt-mRNAs, modulating the efficiency of
CC mitochondrial protein synthesis without changes in transcript abundance
CC or stability (By similarity). Also catalyzes pseudouridylation of some
CC tRNAs, including synthesis of pseudouridine(55) from uracil-55, in the
CC psi GC loop of a subset of tRNAs (By similarity).
CC {ECO:0000250|UniProtKB:O95900}.
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:O95900};
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:O95900};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42533;
CC Evidence={ECO:0000250|UniProtKB:O95900};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:O95900}. Note=Localizes to mitochondrial RNA
CC granules, platforms for post-transcriptional RNA modification and
CC ribosome assembly. {ECO:0000250|UniProtKB:O95900}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
CC {ECO:0000305}.
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DR EMBL; BC084478; AAH84478.1; -; mRNA.
DR RefSeq; NP_001011086.1; NM_001011086.1.
DR AlphaFoldDB; Q5XGG2; -.
DR SMR; Q5XGG2; -.
DR STRING; 8364.ENSXETP00000008598; -.
DR PaxDb; Q5XGG2; -.
DR DNASU; 496499; -.
DR GeneID; 496499; -.
DR KEGG; xtr:496499; -.
DR CTD; 26995; -.
DR Xenbase; XB-GENE-996199; trub2.
DR eggNOG; KOG2559; Eukaryota.
DR InParanoid; Q5XGG2; -.
DR OrthoDB; 1535798at2759; -.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0009982; F:pseudouridine synthase activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR002501; PsdUridine_synth_N.
DR InterPro; IPR039048; Trub2.
DR PANTHER; PTHR13195; PTHR13195; 1.
DR Pfam; PF01509; TruB_N; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
PE 2: Evidence at transcript level;
KW Isomerase; Mitochondrion; mRNA processing; Reference proteome;
KW Transit peptide; tRNA processing.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..325
FT /note="Pseudouridylate synthase TRUB2, mitochondrial"
FT /id="PRO_0000252093"
FT REGION 292..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9Y606"
SQ SEQUENCE 325 AA; 36099 MW; 6C2A2CDE81AEC293 CRC64;
MAQFAPGVFR TLHGLFAVYK PPGVHWKSVR DTVETNLLKE LNALKQRPPR QQIRFLPAGT
EGSNGLEVTR VPSAVPVLAD HVLVKGPAFT HIRVGTGHRL DIQSSGVFVL GIGHGNKLLK
DMYNSHFTRD YTVRGMLGKA TEDFTELGKT IEKTTYDHIT REKLERILAV IQGTNQKALI
THSHLDLQSQ EAYDLAVQGK LRPMVKSPPI ILGIRCLEFS PPEFTLEIQC MHETQQYLRK
MIHEIGLELR SSAVCTQVRR SRDGPFTVDC SLLRTQWDLG SIQGAIRECR AQTEGVSRGN
PDREAAEGPI PGPSRGAEGE GELRA