PUS10_XENLA
ID PUS10_XENLA Reviewed; 515 AA.
AC Q6ING2;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=tRNA pseudouridine synthase Pus10;
DE EC=5.4.99.25 {ECO:0000250|UniProtKB:Q3MIT2};
DE AltName: Full=tRNA pseudouridine 55 synthase;
DE Short=Psi55 synthase;
DE AltName: Full=tRNA pseudouridylate synthase;
DE AltName: Full=tRNA-uridine isomerase;
GN Name=pus10 {ECO:0000250|UniProtKB:Q3MIT2};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein with different functions depending on its subcellular
CC location: involved in miRNA processing in the nucleus and acts as a
CC tRNA pseudouridylate synthase in the cytoplasm. In the cytoplasm, acts
CC as a pseudouridylate synthase by catalyzing synthesis of
CC pseudouridine(54) and pseudouridine(55) from uracil-54 and uracil-55,
CC respectively, in the psi GC loop of a subset of tRNAs. tRNA
CC pseudouridylate synthase activity is enhanced by the presence of 1-
CC methyladenosine at position 53-61 of tRNAs. Does not show tRNA
CC pseudouridylate synthase activity in the nucleus. In the nucleus,
CC promotes primary microRNAs (pri-miRNAs) processing independently of its
CC RNA pseudouridylate synthase activity. Binds pri-miRNAs.
CC {ECO:0000250|UniProtKB:Q3MIT2}.
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:Q3MIT2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42533;
CC Evidence={ECO:0000250|UniProtKB:Q3MIT2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(54) in tRNA = pseudouridine(54) in tRNA;
CC Xref=Rhea:RHEA:57876, Rhea:RHEA-COMP:10193, Rhea:RHEA-COMP:14141,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000250|UniProtKB:Q3MIT2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57877;
CC Evidence={ECO:0000250|UniProtKB:Q3MIT2};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3MIT2}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q3MIT2}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q3MIT2}. Note=Localizes mainly in the nucleus.
CC tRNA pseudouridylate synthase activity is restricted to the cytoplasm.
CC {ECO:0000250|UniProtKB:Q3MIT2}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase Pus10 family.
CC {ECO:0000305}.
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DR EMBL; BC072319; AAH72319.1; -; mRNA.
DR RefSeq; NP_001085415.1; NM_001091946.1.
DR AlphaFoldDB; Q6ING2; -.
DR SMR; Q6ING2; -.
DR DNASU; 443841; -.
DR GeneID; 443841; -.
DR KEGG; xla:443841; -.
DR CTD; 443841; -.
DR Xenbase; XB-GENE-5903783; pus10.S.
DR OrthoDB; 1067006at2759; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 443841; Expressed in oocyte and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070878; F:primary miRNA binding; ISS:UniProtKB.
DR GO; GO:0009982; F:pseudouridine synthase activity; ISS:UniProtKB.
DR GO; GO:0106029; F:tRNA pseudouridine synthase activity; ISS:UniProtKB.
DR GO; GO:0031053; P:primary miRNA processing; ISS:UniProtKB.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; ISS:UniProtKB.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR039894; Pus10-like.
DR PANTHER; PTHR21568; PTHR21568; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Isomerase; Metal-binding; Mitochondrion; Nucleus;
KW Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..515
FT /note="tRNA pseudouridine synthase Pus10"
FT /id="PRO_0000299024"
FT REGION 55..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..304
FT /note="RNA binding forefinger loop"
FT /evidence="ECO:0000255"
FT REGION 428..443
FT /note="RNA binding thumb loop"
FT /evidence="ECO:0000255"
FT COILED 42..85
FT /evidence="ECO:0000255"
FT COMPBIAS 55..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 331
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3MIT2"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3MIT2"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3MIT2"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3MIT2"
SQ SEQUENCE 515 AA; 58590 MW; 51F63C0767E0DF04 CRC64;
MLLIEEKYRS VAQVLLSSGT CSRCVLRFCC VGSPANYRLP CKEVTYELQK YLSHGDPAEE
NDTPPSKKAK IEEDTSSNEH LGNCEDVNGS QVVRICPLCL GILQQFCEPE FIEKVFVKIN
SAVYELKDFV LSISLPAQLS VREHSAWLQA KQEMGKHGHS LDKTDIVQLK EAYKWIIHPL
LSDQLGIQAD SKSLFEVAVV FTHPETDGDC HFLATVCRDC FKPTKNKQSV FTRMAVVKAL
EKIKEEDFRV QFPFPPSSPE TTCEVVDIQC NHSPVFVAGR YNKYSRNLPQ TPWIIDGERK
IESSVEELIT DHLVAAFRSS SFNFSSSGRE DVDVRTLGKG RPFAIELLNP HKVQFTGQEI
KALQQKINTS DKIKVRDLQI VSREAVAHMK EGEEEKTKCY CALIWIEKMV RNEDLQLLDG
LEELTIAQKT PLRVLHRRPL ASRSRTIHTM RTEYVDEHHF RLYLKTQAGT YIKEFVHGDF
GRTKPNVGSI METNADILEL DVESVDVDWP PSLDD
