ID A0A3D8VJM7_9GAMM Unreviewed; 214 AA.
AC A0A3D8VJM7;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Ribonuclease T {ECO:0000256|HAMAP-Rule:MF_00157};
DE EC=3.1.13.- {ECO:0000256|HAMAP-Rule:MF_00157};
DE AltName: Full=Exoribonuclease T {ECO:0000256|HAMAP-Rule:MF_00157};
DE Short=RNase T {ECO:0000256|HAMAP-Rule:MF_00157};
GN Name=rnt {ECO:0000256|HAMAP-Rule:MF_00157,
GN ECO:0000313|EMBL:RDY69590.1};
GN ORFNames=DX912_02250 {ECO:0000313|EMBL:RDY69590.1}, GOY17_06310
GN {ECO:0000313|EMBL:QGW64566.1};
OS Lysobacter soli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=453783 {ECO:0000313|EMBL:RDY69590.1, ECO:0000313|Proteomes:UP000256829};
RN [1] {ECO:0000313|EMBL:RDY69590.1, ECO:0000313|Proteomes:UP000256829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 22011 {ECO:0000313|EMBL:RDY69590.1,
RC ECO:0000313|Proteomes:UP000256829};
RA Zhang X., Feng G., Zhu H.;
RT "Lysobacter soli KCTC 22011, whole genome shotgun sequence.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QGW64566.1, ECO:0000313|Proteomes:UP000424027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XL170 {ECO:0000313|EMBL:QGW64566.1,
RC ECO:0000313|Proteomes:UP000424027};
RA Sun X.;
RT "Microbial interaction.";
RL Submitted (DEC-2019) 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:0000256|HAMAP-Rule:MF_00157}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00157};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00157}.
CC -!- SIMILARITY: Belongs to the RNase T family. {ECO:0000256|HAMAP-
CC Rule:MF_00157}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00157}.
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DR EMBL; CP046603; QGW64566.1; -; Genomic_DNA.
DR EMBL; QTJR01000001; RDY69590.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8VJM7; -.
DR KEGG; lsol:GOY17_06310; -.
DR OrthoDB; 9778264at2; -.
DR Proteomes; UP000256829; Unassembled WGS sequence.
DR Proteomes; UP000424027; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0016896; F:RNA exonuclease activity, producing 5'-phosphomonoesters; IEA:UniProtKB-UniRule.
DR GO; GO:0006259; P:DNA metabolic process; IEA:UniProt.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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 NCBIfam; TIGR01298; RNaseT; 1.
DR PANTHER; PTHR30231; DNA POLYMERASE III SUBUNIT EPSILON; 1.
DR PANTHER; PTHR30231:SF2; RIBONUCLEASE T; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_00157}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00157};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00157};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00157};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00157};
KW Reference proteome {ECO:0000313|Proteomes:UP000256829};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00157}.
FT DOMAIN 21..206
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT ACT_SITE 184
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT BINDING 26
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT BINDING 26
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT BINDING 28
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT SITE 32
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT SITE 127
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT SITE 149
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
SQ SEQUENCE 214 AA; 23136 MW; 811C45D3C5BAEBDA CRC64;
MQNADAPAPP ARLCTRFRGF LPVVVDVETG GFDWNRHALL EIAVAPIDLD ENGLLVVGEI
TSSHVVPAPG LDIDPKSLEV TGIDIDHPFR DAKTERVALE TVFAPVRAAL KKHGCQRAIL
VGHNAHFDLN FLNAAVARSG HKRNPFHPFS VFDTVSLAGV AYGQTVLARA VQAAGLSWNS
EEQHSAVYDT ERTAQLFCRI VNAWPSPVPP VVAP
//
