AC   MF_00157;
DC   Protein; auto
TR   HAMAP; MF_00157; -; 1; level=0
XX
Names: RNase_T
XX
ID   RNT
DE   RecName: Full=Ribonuclease T;
DE            EC=3.1.13.-;
DE   AltName: Full=Exoribonuclease T;
DE            Short=RNase T;
GN   Name=rnt;
XX
CC   -!- FUNCTION: Trims short 3' overhangs of a variety of RNA species, leaving
CC       a one or two nucleotide 3' overhang. Responsible for the end-turnover
CC       of tRNA: specifically removes the terminal AMP residue from uncharged
CC       tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis.
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds two Mg(2+) per subunit. The active form of the enzyme binds
CC       two Mg(2+) ions in its active site. The first Mg(2+) forms only one
CC       salt bridge with the protein.;
end case
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the RNase T family.
XX
DR   Pfam; PF00929; RNase_T; 1; trigger=yes
DR   NCBIfam; TIGR01298; RNaseT; 1; trigger=no
XX
KW   Exonuclease
KW   Hydrolase
KW   Nuclease
KW   tRNA processing
case <FTGroup:1>
KW   Magnesium
KW   Metal-binding
end case
XX
GO   GO:0016896; F:RNA exonuclease activity, producing 5'-phosphomonoesters
case <FTGroup:1>
GO   GO:0000287; F:magnesium ion binding
end case
GO   GO:0006396; P:RNA processing
XX
FT   From: RNT_ECOLI (P30014)
FT   ACT_SITE        181
FT                   /note="Proton donor/acceptor"
FT   Condition: H
FT   BINDING         23
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: D
FT   BINDING         23
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: D
FT   BINDING         25
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: E
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: H
FT   BINDING         186
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: D
FT   SITE            29
FT                   /note="Important for substrate binding and specificity"
FT   Optional; Condition: F
FT   SITE            77
FT                   /note="Important for substrate binding and specificity"
FT   Optional; Condition: F
FT   SITE            124
FT                   /note="Important for substrate binding and specificity"
FT   Optional; Condition: F
FT   SITE            146
FT                   /note="Important for substrate binding and specificity"
FT   Optional; Condition: F
XX
Size: 190-275;
Related: None;
Template: P30014;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.25 2023/06/01
//