RNT_PSEA7
ID RNT_PSEA7 Reviewed; 224 AA.
AC A6V1R8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Ribonuclease T {ECO:0000255|HAMAP-Rule:MF_00157};
DE EC=3.1.13.- {ECO:0000255|HAMAP-Rule:MF_00157};
DE AltName: Full=Exoribonuclease T {ECO:0000255|HAMAP-Rule:MF_00157};
DE Short=RNase T {ECO:0000255|HAMAP-Rule:MF_00157};
GN Name=rnt {ECO:0000255|HAMAP-Rule:MF_00157}; OrderedLocusNames=PSPA7_1619;
OS Pseudomonas aeruginosa (strain PA7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=381754;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7;
RA Dodson R.J., Harkins D., Paulsen I.T.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000255|HAMAP-Rule:MF_00157}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00157};
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. {ECO:0000255|HAMAP-Rule:MF_00157};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00157}.
CC -!- SIMILARITY: Belongs to the RNase T family. {ECO:0000255|HAMAP-
CC Rule:MF_00157}.
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; CP000744; ABR85976.1; -; Genomic_DNA.
DR RefSeq; WP_003155625.1; NC_009656.1.
DR AlphaFoldDB; A6V1R8; -.
DR SMR; A6V1R8; -.
DR EnsemblBacteria; ABR85976; ABR85976; PSPA7_1619.
DR KEGG; pap:PSPA7_1619; -.
DR HOGENOM; CLU_082724_0_0_6; -.
DR OMA; CYMVNHL; -.
DR OrthoDB; 1985371at2; -.
DR Proteomes; UP000001582; Chromosome.
DR GO; GO:0016896; F:exoribonuclease activity, producing 5'-phosphomonoesters; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd06134; RNaseT; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_00157; RNase_T; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR005987; RNase_T.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR30231:SF2; PTHR30231:SF2; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR TIGRFAMs; TIGR01298; RNaseT; 1.
PE 3: Inferred from homology;
KW Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW tRNA processing.
FT CHAIN 1..224
FT /note="Ribonuclease T"
FT /id="PRO_1000011403"
FT DOMAIN 32..206
FT /note="Exonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT ACT_SITE 193
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT BINDING 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT BINDING 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT BINDING 37
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT SITE 41
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT SITE 89
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT SITE 136
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT SITE 158
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
SQ SEQUENCE 224 AA; 24808 MW; 74E2DBBA1F5574C6 CRC64;
MSEDNFDEEF DGTLPSGPRH PMARRFRGYL PVVVDVETGG FNSATDALLE IAATTVGMDE
KGFLFPEHTY FFRIEPFEGA NIEPAALEFT GIKLDHPLRM AVQEEQALTE IFRGIRKALK
ANGCKRAILV GHNSSFDLGF LNAAVARTGI KRNPFHPFSS FDTATLAGLA YGQTVLAKAC
QAAGMEFDNR EAHSARYDTE KTAELFCGIV NRWKEMGGWM DDDD
