TRUB2_RAT
ID TRUB2_RAT Reviewed; 323 AA.
AC Q5XFW2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
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:0000312|RGD:1359394};
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=Ovary;
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: 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. As a component of a functional
CC protein-RNA module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2,
CC FASTKD2 and 16S mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S
CC mt-rRNA abundance and is required for intra-mitochondrial translation.
CC Also catalyzes pseudouridylation of some tRNAs, including synthesis of
CC pseudouridine(55) from uracil-55, in the psi GC loop of a subset of
CC tRNAs. {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 -!- SUBUNIT: Forms a regulatory protein-RNA complex, consisting of RCC1L,
CC NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mt-rRNA.
CC {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; BC084712; AAH84712.1; -; mRNA.
DR RefSeq; NP_001014279.1; NM_001014257.2.
DR AlphaFoldDB; Q5XFW2; -.
DR SMR; Q5XFW2; -.
DR STRING; 10116.ENSRNOP00000063203; -.
DR PaxDb; Q5XFW2; -.
DR PRIDE; Q5XFW2; -.
DR GeneID; 366012; -.
DR KEGG; rno:366012; -.
DR CTD; 26995; -.
DR RGD; 1359394; Trub2.
DR VEuPathDB; HostDB:ENSRNOG00000043189; -.
DR eggNOG; KOG2559; Eukaryota.
DR HOGENOM; CLU_032087_1_1_1; -.
DR InParanoid; Q5XFW2; -.
DR OMA; CIHFQPP; -.
DR OrthoDB; 1535798at2759; -.
DR PhylomeDB; Q5XFW2; -.
DR PRO; PR:Q5XFW2; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000043189; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; Q5XFW2; RN.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0035770; C:ribonucleoprotein granule; ISO:RGD.
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:1990481; P:mRNA pseudouridine synthesis; ISO:RGD.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; ISS:UniProtKB.
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 ?..323
FT /note="Pseudouridylate synthase TRUB2, mitochondrial"
FT /id="PRO_0000252092"
FT REGION 302..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 98
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9Y606"
SQ SEQUENCE 323 AA; 36109 MW; 74C46218FD68A22F CRC64;
MGSSGLARLQ GLFAVYKPPG LKWLHVRETV ELQLLKGLNA QQPSAPEQHV RFLLGPVEGS
EEKKLTLTAT SVPSLTTHRL VRGPAFRNLK IGVGHRLDVQ ASGVLVLAVG HGRSLLTDMY
DAHLTKDYTV RGLLGKATDN FCEDGQLIEK TTYDHVTRER LDRILAMIQG SHQKALVMYS
NLDLKSQEAY ERAVQGVIRP MNKSPMLIAG IRCLHFAPPE FLLEVQCMHE TQQQLRRLVH
EIGLELKTTA VCMQVRRTRD GFFGLDDALL RTQWDLHSIQ DAIQTAAPRV ARELRKNLSL
MSGHQQQLPS AGQPWASRVQ APL
