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RNT_ECOHS
ID   RNT_ECOHS               Reviewed;         215 AA.
AC   A8A0J6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=EcHS_A1729;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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; CP000802; ABV06050.1; -; Genomic_DNA.
DR   RefSeq; WP_001282281.1; NC_009800.1.
DR   AlphaFoldDB; A8A0J6; -.
DR   SMR; A8A0J6; -.
DR   GeneID; 67415644; -.
DR   KEGG; ecx:EcHS_A1729; -.
DR   HOGENOM; CLU_082724_0_0_6; -.
DR   OMA; CYMVNHL; -.
DR   Proteomes; UP000001123; 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..215
FT                   /note="Ribonuclease T"
FT                   /id="PRO_1000058189"
FT   DOMAIN          20..194
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT   ACT_SITE        181
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT   BINDING         23
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         23
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         25
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         181
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         186
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            29
FT                   /note="Important for substrate binding and specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT   SITE            77
FT                   /note="Important for substrate binding and specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT   SITE            124
FT                   /note="Important for substrate binding and specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT   SITE            146
FT                   /note="Important for substrate binding and specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
SQ   SEQUENCE   215 AA;  23533 MW;  502C1CCEFABD9B05 CRC64;
     MSDNAQLTGL CDRFRGFYPV VIDVETAGFN AKTDALLEIA AITLKMDEQG WLMPDTTLHF
     HVEPFVGANL QPEALAFNGI DPNDPDRGAV SEYEALHEIF KVVRKGIKAS GCNRAIMVAH
     NANFDHSFMM AAAERASLKR NPFHPFATFD TAALAGLALG QTVLSKACQT AGMDFDSTQA
     HSALYDTERT AVLFCEIVNR WKRLGGWPLP AAEEV
 
 
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