RNU2_USTSP
ID RNU2_USTSP Reviewed; 114 AA.
AC P00654; Q9HGK7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 4.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Ribonuclease U2;
DE Short=RNase U2;
DE EC=4.6.1.20;
GN Name=RNU2;
OS Ustilago sphaerogena (Smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=5271;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1156364; DOI=10.1042/bj1450353;
RA Sato S., Uchida T.;
RT "The amino acid sequence of ribonuclease U2 from Ustilago sphaerogena.";
RL Biochem. J. 145:353-360(1975).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-106.
RC STRAIN=ATCC 12421 / CBS 534.71 / IMI 61828 / 50-135;
RX PubMed=10930732; DOI=10.1111/j.1574-6968.2000.tb09224.x;
RA Martinez-Ruiz A., Garcia-Ortega L., Kao R., Onaderra M., Mancheno J.M.,
RA Davies J., Martinez del Pozo A., Gavilanes J.G.;
RT "Ribonuclease U2: cloning, production in Pichia pastoris and affinity
RT chromatography purification of the active recombinant protein.";
RL FEMS Microbiol. Lett. 189:165-169(2000).
RN [3]
RP PROTEIN SEQUENCE OF 44-53, AND SEQUENCE REVISION.
RX PubMed=8576077; DOI=10.1093/oxfordjournals.jbchem.a124964;
RA Kanaya S., Uchida T.;
RT "Revised sequence of ribonuclease U2 in the substrate-binding region.";
RL J. Biochem. 118:681-682(1995).
RN [4]
RP DISULFIDE BONDS.
RX PubMed=1225902;
RA Sato S., Uchida T.;
RT "The disulfide bridges of ribonuclease U2 from Ustilago sphaerogena.";
RL J. Biochem. 77:1171-1176(1975).
RN [5]
RP ACTIVE SITE.
RA Uchida T., Sato S.;
RL (In) Zelinka J., Balan J. (eds.);
RL Ribosomes and RNA metabolism, pp.453-472, Publ. House Slovak Acad. Sci.,
RL Bratislava (1973).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND SEQUENCE REVISION.
RX PubMed=7492561; DOI=10.1021/bi00047a025;
RA Noguchi S., Satow Y., Uchida T., Sasaki C., Matsuzaki T.;
RT "Crystal structure of Ustilago sphaerogena ribonuclease U2 at 1.8-A
RT resolution.";
RL Biochemistry 34:15583-15591(1995).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (0.96 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS AND
RP ADENOSINE 3'-MONOPHOSPHATE, FORMATION OF ISOASPARTATE, AND DISULFIDE BONDS.
RX PubMed=20606265; DOI=10.1107/s0907444910019621;
RA Noguchi S.;
RT "Isomerization mechanism of aspartate to isoaspartate implied by structures
RT of Ustilago sphaerogena ribonuclease U2 complexed with adenosine 3'-
RT monophosphate.";
RL Acta Crystallogr. D 66:843-849(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS).
RX PubMed=20623666; DOI=10.1002/bip.21514;
RA Noguchi S.;
RT "Structural changes induced by the deamidation and isomerization of
RT asparagine revealed by the crystal structure of Ustilago sphaerogena
RT ribonuclease U2B.";
RL Biopolymers 93:1003-1010(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.03 ANGSTROMS) IN COMPLEX WITH CALCIUM AND
RP ADENOSINE 2'-PHOSPHATE.
RX PubMed=20858208; DOI=10.2174/0929866511009011559;
RA Noguchi S.;
RT "Conformational variation revealed by the crystal structure of RNase U2A
RT complexed with Ca ion and 2'-adenylic acid at 1.03 A resolution.";
RL Protein Pept. Lett. 17:1559-1561(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[RNA] containing adenosine + H2O = an [RNA fragment]-3'-
CC adenosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA
CC fragment].; EC=4.6.1.20;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[RNA] containing guanosine + H2O = an [RNA fragment]-3'-
CC guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA
CC fragment].; EC=4.6.1.20;
CC -!- MISCELLANEOUS: After treatment by base Asn-32 and Asp-45 partially
CC isomerise by succinimide rearrangement to form iosaspartyl peptides.
CC -!- SIMILARITY: Belongs to the ribonuclease U2 family. {ECO:0000305}.
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DR EMBL; AJ004827; CAC04098.1; -; Genomic_DNA.
DR PIR; PC4081; NRUSU2.
DR PDB; 1RTU; X-ray; 1.80 A; A=1-114.
DR PDB; 3AGN; X-ray; 0.96 A; A=1-114.
DR PDB; 3AGO; X-ray; 0.99 A; A=1-114.
DR PDB; 3AHS; X-ray; 1.32 A; A/B/C=1-114.
DR PDB; 3AHW; X-ray; 1.03 A; A=1-114.
DR PDBsum; 1RTU; -.
DR PDBsum; 3AGN; -.
DR PDBsum; 3AGO; -.
DR PDBsum; 3AHS; -.
DR PDBsum; 3AHW; -.
DR AlphaFoldDB; P00654; -.
DR SMR; P00654; -.
DR KEGG; ag:CAC04098; -.
DR BRENDA; 4.6.1.20; 6588.
DR EvolutionaryTrace; P00654; -.
DR PRO; PR:P00654; -.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033899; F:ribonuclease U2 activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR InterPro; IPR000026; Gua-sp_ribonuclease_N1/T1/U2.
DR InterPro; IPR016191; Ribonuclease/ribotoxin.
DR Pfam; PF00545; Ribonuclease; 1.
DR SUPFAM; SSF53933; SSF53933; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Endonuclease; Hydrolase; Lyase; Metal-binding; Nuclease.
FT CHAIN 1..114
FT /note="Ribonuclease U2"
FT /id="PRO_0000137379"
FT ACT_SITE 41
FT /evidence="ECO:0000269|Ref.5"
FT ACT_SITE 62
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|Ref.5"
FT ACT_SITE 101
FT /note="Proton donor"
FT /evidence="ECO:0000269|Ref.5"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20858208"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20858208"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20858208"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20858208"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20858208"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20858208"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20858208"
FT BINDING 39..49
FT /ligand="substrate"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20858208"
FT BINDING 85
FT /ligand="substrate"
FT BINDING 108..110
FT /ligand="substrate"
FT SITE 62
FT /note="Methylation inactivates enzyme"
FT /evidence="ECO:0000269|PubMed:7492561"
FT DISULFID 1..54
FT /evidence="ECO:0000269|PubMed:1225902"
FT DISULFID 9..113
FT /evidence="ECO:0000269|PubMed:1225902"
FT DISULFID 55..96
FT /evidence="ECO:0000269|PubMed:1225902"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:3AGN"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:3AGN"
FT HELIX 16..31
FT /evidence="ECO:0007829|PDB:3AGN"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:3AGN"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3AGN"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3AGN"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:3AGN"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3AHS"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:3AGN"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:3AGN"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:3AGN"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:3AHW"
SQ SEQUENCE 114 AA; 12387 MW; 96D32CB2E23AAB98 CRC64;
CDIPQSTNCG GNVYSNDDIN TAIQGALDDV ANGDRPDNYP HQYYDEASED ITLCCGSGPW
SEFPLVYNGP YYSSRDNYVS PGPDRVIYQT NTGEFCATVT HTGAASYDGF TQCS
