ID I3DHH1_9PAST Unreviewed; 227 AA.
AC I3DHH1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
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:EIJ71164.1};
GN ORFNames=HMPREF1052_1925 {ECO:0000313|EMBL:EIJ71164.1};
OS Pasteurella bettyae CCUG 2042.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=1095749 {ECO:0000313|EMBL:EIJ71164.1, ECO:0000313|Proteomes:UP000006457};
RN [1] {ECO:0000313|EMBL:EIJ71164.1, ECO:0000313|Proteomes:UP000006457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 2042 {ECO:0000313|EMBL:EIJ71164.1,
RC ECO:0000313|Proteomes:UP000006457};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (MAR-2012) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIJ71164.1}.
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DR EMBL; AJSX01000008; EIJ71164.1; -; Genomic_DNA.
DR RefSeq; WP_005759312.1; NZ_AJSX01000008.1.
DR AlphaFoldDB; I3DHH1; -.
DR PATRIC; fig|1095749.3.peg.520; -.
DR eggNOG; COG0847; Bacteria.
DR OrthoDB; 9778264at2; -.
DR Proteomes; UP000006457; Unassembled WGS sequence.
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 CDD; cd06134; RNaseT; 1.
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};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00157, ECO:0000313|EMBL:EIJ71164.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, 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:UP000006457};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00157}.
FT DOMAIN 27..212
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT ACT_SITE 190
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT BINDING 32
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 32
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 34
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 190
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 195
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 38
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT SITE 86
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT SITE 133
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
FT SITE 155
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00157"
SQ SEQUENCE 227 AA; 25326 MW; 9D7AA459E7E98108 CRC64;
MTELHTETTE NETTNYNLLK NRFRGYYPVI IDVETAGFNA KQDALLELAA ITVKMDENGW
LVPDQKYHAH IEPFEGANIN PDSLKFNGID IHNPLRGAIS ETDAITGLFQ MVRRGQKDNG
CQRSIIVAHN ATFDQSFVMA AAERCGVKRN PFHPFGMFDT ATLSGFMLGQ TVLVKACKVA
KITFDGKQAH SALYDTERTA ELFCYMVNHL KHLGGFPHIV QSDDSAN
//
