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RNT_PSEAB
ID   RNT_PSEAB               Reviewed;         224 AA.
AC   Q02QZ9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=PA14_18700;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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}.
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DR   EMBL; CP000438; ABJ12763.1; -; Genomic_DNA.
DR   RefSeq; WP_003092070.1; NZ_CP034244.1.
DR   AlphaFoldDB; Q02QZ9; -.
DR   SMR; Q02QZ9; -.
DR   PRIDE; Q02QZ9; -.
DR   EnsemblBacteria; ABJ12763; ABJ12763; PA14_18700.
DR   KEGG; pau:PA14_18700; -.
DR   HOGENOM; CLU_082724_0_0_6; -.
DR   OMA; CYMVNHL; -.
DR   BioCyc; PAER208963:G1G74-1541-MON; -.
DR   Proteomes; UP000000653; 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_1000011404"
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;  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
 
 
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