RNT_PSEAE
ID RNT_PSEAE Reviewed; 224 AA.
AC Q9HY82;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=PA3528;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, COFACTOR,
RP AND SUBUNIT.
RX PubMed=17437714; DOI=10.1016/j.str.2007.02.004;
RA Zuo Y., Zheng H., Wang Y., Chruszcz M., Cymborowski M., Skarina T.,
RA Savchenko A., Malhotra A., Minor W.;
RT "Crystal structure of RNase T, an exoribonuclease involved in tRNA
RT maturation and end turnover.";
RL Structure 15:417-428(2007).
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 ECO:0000269|PubMed:17437714}.
CC -!- MISCELLANEOUS: Member of the DEDD group of RNAses that are
CC characterized by the presence of four acidic residues in the active
CC site. These residues are conserved even when the proteins have highly
CC divergent sequences.
CC -!- SIMILARITY: Belongs to the RNase T family. {ECO:0000255|HAMAP-
CC Rule:MF_00157}.
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DR EMBL; AE004091; AAG06916.1; -; Genomic_DNA.
DR PIR; F83204; F83204.
DR RefSeq; NP_252218.1; NC_002516.2.
DR RefSeq; WP_003092070.1; NZ_QZGE01000001.1.
DR PDB; 2F96; X-ray; 2.09 A; A/B=1-224.
DR PDBsum; 2F96; -.
DR AlphaFoldDB; Q9HY82; -.
DR SMR; Q9HY82; -.
DR DIP; DIP-29430N; -.
DR STRING; 287.DR97_4414; -.
DR PaxDb; Q9HY82; -.
DR PRIDE; Q9HY82; -.
DR EnsemblBacteria; AAG06916; AAG06916; PA3528.
DR GeneID; 879810; -.
DR KEGG; pae:PA3528; -.
DR PATRIC; fig|208964.12.peg.3692; -.
DR PseudoCAP; PA3528; -.
DR HOGENOM; CLU_082724_0_0_6; -.
DR InParanoid; Q9HY82; -.
DR OMA; CYMVNHL; -.
DR PhylomeDB; Q9HY82; -.
DR BioCyc; PAER208964:G1FZ6-3596-MON; -.
DR BRENDA; 3.1.13.3; 5087.
DR EvolutionaryTrace; Q9HY82; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IBA:GO_Central.
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:0045004; P:DNA replication proofreading; IBA:GO_Central.
DR GO; GO:0042780; P:tRNA 3'-end processing; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome; tRNA processing.
FT CHAIN 1..224
FT /note="Ribonuclease T"
FT /id="PRO_0000208969"
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 ECO:0000269|PubMed:17437714"
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"
FT HELIX 21..25
FT /evidence="ECO:0007829|PDB:2F96"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:2F96"
FT STRAND 29..41
FT /evidence="ECO:0007829|PDB:2F96"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:2F96"
FT STRAND 48..58
FT /evidence="ECO:0007829|PDB:2F96"
FT STRAND 64..74
FT /evidence="ECO:0007829|PDB:2F96"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:2F96"
FT HELIX 104..121
FT /evidence="ECO:0007829|PDB:2F96"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:2F96"
FT HELIX 134..148
FT /evidence="ECO:0007829|PDB:2F96"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:2F96"
FT HELIX 163..171
FT /evidence="ECO:0007829|PDB:2F96"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:2F96"
FT HELIX 195..215
FT /evidence="ECO:0007829|PDB:2F96"
SQ SEQUENCE 224 AA; 24723 MW; CC1010D3AD60F442 CRC64;
MSEDNFDDEF DGSLPSGPRH PMARRFRGYL PVVVDVETGG FNSATDALLE IAATTVGMDE
KGFLFPEHTY FFRIEPFEGA NIEPAALEFT GIKLDHPLRM AVQEEAALTE IFRGIRKALK
ANGCKRAILV GHNSSFDLGF LNAAVARTGI KRNPFHPFSS FDTATLAGLA YGQTVLAKAC
QAAGMEFDNR EAHSARYDTE KTAELFCGIV NRWKEMGGWM DDDD
