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RNT_ECO57
ID   RNT_ECO57               Reviewed;         215 AA.
AC   P66682; Q8X627;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
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};
GN   OrderedLocusNames=Z2671, ECs2361;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG56641.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35784.1; -; Genomic_DNA.
DR   PIR; A90924; A90924.
DR   PIR; E85772; E85772.
DR   RefSeq; NP_310388.1; NC_002695.1.
DR   RefSeq; WP_001282281.1; NZ_SWKA01000004.1.
DR   AlphaFoldDB; P66682; -.
DR   SMR; P66682; -.
DR   STRING; 155864.EDL933_2609; -.
DR   EnsemblBacteria; AAG56641; AAG56641; Z2671.
DR   EnsemblBacteria; BAB35784; BAB35784; ECs_2361.
DR   GeneID; 67415644; -.
DR   GeneID; 914111; -.
DR   KEGG; ece:Z2671; -.
DR   KEGG; ecs:ECs_2361; -.
DR   PATRIC; fig|386585.9.peg.2470; -.
DR   eggNOG; COG0847; Bacteria.
DR   HOGENOM; CLU_082724_0_0_6; -.
DR   OMA; CYMVNHL; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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   Reference proteome; tRNA processing.
FT   CHAIN           1..215
FT                   /note="Ribonuclease T"
FT                   /id="PRO_0000208962"
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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