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RNT_SHESR
ID   RNT_SHESR               Reviewed;         222 AA.
AC   Q0HTX3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=Shewmr7_2447;
OS   Shewanella sp. (strain MR-7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-7;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA   Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL   Submitted (AUG-2006) 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: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; CP000444; ABI43432.1; -; Genomic_DNA.
DR   RefSeq; WP_011623135.1; NC_008322.1.
DR   AlphaFoldDB; Q0HTX3; -.
DR   SMR; Q0HTX3; -.
DR   EnsemblBacteria; ABI43432; ABI43432; Shewmr7_2447.
DR   KEGG; shm:Shewmr7_2447; -.
DR   HOGENOM; CLU_082724_0_0_6; -.
DR   OMA; CYMVNHL; -.
DR   OrthoDB; 1985371at2; -.
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..222
FT                   /note="Ribonuclease T"
FT                   /id="PRO_1000011419"
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   222 AA;  24377 MW;  8477A0B286C9CC31 CRC64;
     MSDISDANKL KHRFRGYFPV VIDVETAGFN SQTDALLEIA VTLLKMDDEG LLGIDKTLHF
     NIEPFEGANL EPEALAFNGI DPTNPLRGAV SEKEAFLEIF KAVKKAQKAS DCHRSIIVAH
     NAAFDHGFVS KAIERCDLKR SPFHPFATFD TATLAGLAIG HTVLAKACIM AGIPFDNKEA
     HSALYDTERT AELFCYIVNR WKHLGGWPLL AAGESEDTDG EE
 
 
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