ENDUA_XENLA
ID ENDUA_XENLA Reviewed; 292 AA.
AC Q8JFY9;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Poly(U)-specific endoribonuclease-A;
DE EC=4.6.1.- {ECO:0000269|PubMed:12571235, ECO:0000269|PubMed:15755742};
DE AltName: Full=Protein endoU-A;
DE AltName: Full=Uridylate-specific endoribonuclease-A;
DE AltName: Full=XendoU-A;
GN Name=endou-a;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, SUBUNIT, COFACTOR, AND PROTEIN SEQUENCE OF 117-123; 137-142 AND
RP 276-284.
RC TISSUE=Oocyte;
RX PubMed=12571235; DOI=10.1074/jbc.m211937200;
RA Laneve P., Altieri F., Fiori M.E., Scaloni A., Bozzoni I., Caffarelli E.;
RT "Purification, cloning, and characterization of XendoU, a novel
RT endoribonuclease involved in processing of intron-encoded small nucleolar
RT RNAs in Xenopus laevis.";
RL J. Biol. Chem. 278:13026-13032(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP MUTAGENESIS OF GLU-92; SER-157; GLU-161; HIS-162; GLU-167; HIS-178;
RP LYS-224; GLY-232; SER-234; PRO-235 AND GLU-236, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=15755742; DOI=10.1074/jbc.m501160200;
RA Gioia U., Laneve P., Dlakic M., Arceci M., Bozzoni I., Caffarelli E.;
RT "Functional characterization of XendoU, the endoribonuclease involved in
RT small nucleolar RNA biosynthesis.";
RL J. Biol. Chem. 280:18996-19002(2005).
RN [3]
RP FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=7513048; DOI=10.1128/mcb.14.5.2966-2974.1994;
RA Caffarelli E., Arese M., Santoro B., Fragapane P., Bozzoni I.;
RT "In vitro study of processing of the intron-encoded U16 small nucleolar RNA
RT in Xenopus laevis.";
RL Mol. Cell. Biol. 14:2966-2974(1994).
RN [4]
RP FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=9144568; DOI=10.1006/bbrc.1997.6487;
RA Caffarelli E., Maggi L., Fatica A., Jiricny J., Bozzoni I.;
RT "A novel Mn++-dependent ribonuclease that functions in U16 SnoRNA
RT processing in X. laevis.";
RL Biochem. Biophys. Res. Commun. 233:514-517(1997).
RN [5]
RP PURIFICATION, AND CRYSTALLIZATION.
RX PubMed=16511328; DOI=10.1107/s1744309106006373;
RA Renzi F., Panetta G., Vallone B., Brunori M., Arceci M., Bozzoni I.,
RA Laneve P., Caffarelli E.;
RT "Large-scale purification and crystallization of the endoribonuclease
RT XendoU: troubleshooting with His-tagged proteins.";
RL Acta Crystallogr. F 62:298-301(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND SUBUNIT.
RX PubMed=16895992; DOI=10.1073/pnas.0602426103;
RA Renzi F., Caffarelli E., Laneve P., Bozzoni I., Brunori M., Vallone B.;
RT "The structure of the endoribonuclease XendoU: from small nucleolar RNA
RT processing to severe acute respiratory syndrome coronavirus replication.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:12365-12370(2006).
CC -!- FUNCTION: Poly(U)-specific endoribonuclease involved in the processing
CC of intron-encoded box C/D snoRNAs, such as U16 and U86. Releases
CC products that have 2',3'-cyclic phosphate termini at the 3'-end.
CC {ECO:0000269|PubMed:12571235, ECO:0000269|PubMed:15755742,
CC ECO:0000269|PubMed:7513048, ECO:0000269|PubMed:9144568}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-
CC 2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-
CC RNA; Xref=Rhea:RHEA:67732, Rhea:RHEA-COMP:13936, Rhea:RHEA-
CC COMP:17334, Rhea:RHEA-COMP:17335, ChEBI:CHEBI:138284,
CC ChEBI:CHEBI:173079, ChEBI:CHEBI:173080;
CC Evidence={ECO:0000269|PubMed:12571235, ECO:0000269|PubMed:15755742};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67733;
CC Evidence={ECO:0000305|PubMed:12571235, ECO:0000305|PubMed:15755742};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12571235, ECO:0000269|PubMed:15755742,
CC ECO:0000269|PubMed:7513048, ECO:0000269|PubMed:9144568};
CC Note=In vitro, optimal manganese concentration is in the range of 5-10
CC mM. {ECO:0000269|PubMed:12571235, ECO:0000269|PubMed:15755742,
CC ECO:0000269|PubMed:7513048, ECO:0000269|PubMed:9144568};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:15755742};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12571235,
CC ECO:0000269|PubMed:16895992}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12571235,
CC ECO:0000269|PubMed:7513048, ECO:0000269|PubMed:9144568}.
CC -!- SIMILARITY: Belongs to the ENDOU family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ507315; CAD45344.1; -; mRNA.
DR RefSeq; NP_001081040.1; NM_001087571.1.
DR PDB; 2C1W; X-ray; 2.20 A; A/B/C=1-292.
DR PDBsum; 2C1W; -.
DR AlphaFoldDB; Q8JFY9; -.
DR SMR; Q8JFY9; -.
DR MaxQB; Q8JFY9; -.
DR GeneID; 394346; -.
DR CTD; 394346; -.
DR Xenbase; XB-GENE-5883648; endoul.L.
DR EvolutionaryTrace; Q8JFY9; -.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 394346; Expressed in oocyte and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; TAS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0043144; P:sno(s)RNA processing; TAS:UniProtKB.
DR CDD; cd21159; XendoU; 1.
DR InterPro; IPR039787; ENDOU.
DR InterPro; IPR037227; EndoU-like.
DR InterPro; IPR018998; EndoU_C.
DR PANTHER; PTHR12439; PTHR12439; 1.
DR Pfam; PF09412; XendoU; 1.
DR SUPFAM; SSF142877; SSF142877; 1.
DR PROSITE; PS51959; ENDOU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Endonuclease; Hydrolase; Lyase;
KW Manganese; Metal-binding; Nuclease; Nucleus; Reference proteome;
KW RNA-binding.
FT CHAIN 1..292
FT /note="Poly(U)-specific endoribonuclease-A"
FT /id="PRO_0000350627"
FT DOMAIN 8..285
FT /note="EndoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT MUTAGEN 92
FT /note="E->Q: No change in affinity for RNA substrate."
FT /evidence="ECO:0000269|PubMed:15755742"
FT MUTAGEN 157
FT /note="S->A: No change in affinity for RNA substrate."
FT /evidence="ECO:0000269|PubMed:15755742"
FT MUTAGEN 161
FT /note="E->Q: No effect. Loss of activity and affinity for
FT RNA substrate; when associated with Q-167."
FT /evidence="ECO:0000269|PubMed:15755742"
FT MUTAGEN 162
FT /note="H->A: Loss of catalytic activity and affinity for
FT RNA substrate."
FT /evidence="ECO:0000269|PubMed:15755742"
FT MUTAGEN 167
FT /note="E->Q: No effect. Loss of activity and affinity for
FT RNA substrate; when associated with Q-161."
FT /evidence="ECO:0000269|PubMed:15755742"
FT MUTAGEN 178
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15755742"
FT MUTAGEN 224
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15755742"
FT MUTAGEN 232
FT /note="G->A: No change in affinity for RNA substrate."
FT /evidence="ECO:0000269|PubMed:15755742"
FT MUTAGEN 234
FT /note="S->A: No change in affinity for RNA substrate."
FT /evidence="ECO:0000269|PubMed:15755742"
FT MUTAGEN 235
FT /note="P->A: No change in affinity for RNA substrate."
FT /evidence="ECO:0000269|PubMed:15755742"
FT MUTAGEN 236
FT /note="E->Q: Shows higher affinity for RNA substrate."
FT /evidence="ECO:0000269|PubMed:15755742"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:2C1W"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:2C1W"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:2C1W"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:2C1W"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:2C1W"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:2C1W"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:2C1W"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:2C1W"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:2C1W"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:2C1W"
FT HELIX 132..144
FT /evidence="ECO:0007829|PDB:2C1W"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:2C1W"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:2C1W"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:2C1W"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:2C1W"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:2C1W"
FT STRAND 211..219
FT /evidence="ECO:0007829|PDB:2C1W"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:2C1W"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:2C1W"
FT STRAND 250..260
FT /evidence="ECO:0007829|PDB:2C1W"
FT STRAND 263..272
FT /evidence="ECO:0007829|PDB:2C1W"
FT STRAND 275..287
FT /evidence="ECO:0007829|PDB:2C1W"
SQ SEQUENCE 292 AA; 33863 MW; 910ED803409E25A5 CRC64;
MASNRGQLNH ELSKLFNELW DADQNRMKSG KDYRISLQGK AGYVPAGSNQ ARDSASFPLF
QFVDEEKLKS RKTFATFISL LDNYEMDTGV AEVVTPEEIA ENNNFLDAIL ETKVMKMAHD
YLVRKNQAKP TRNDFKVQLY NIWFQLYSRA PGSRPDSCGF EHVFVGESKR GQEMMGLHNW
VQFYLQEKRK NIDYKGYVAR QNKSRPDEDD QVLNLQFNWK EMVKPVGSSF IGVSPEFEFA
LYTIVFLASQ EKMSREVVRL EEYELQIVVN RHGRYIGTAY PVLLSTNNPD LY
