RNT_BUCAI
ID RNT_BUCAI Reviewed; 221 AA.
AC P57285;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=BU188;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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; BA000003; BAB12905.1; -; Genomic_DNA.
DR RefSeq; NP_240019.1; NC_002528.1.
DR RefSeq; WP_009874145.1; NC_002528.1.
DR AlphaFoldDB; P57285; -.
DR SMR; P57285; -.
DR STRING; 107806.10038870; -.
DR EnsemblBacteria; BAB12905; BAB12905; BAB12905.
DR KEGG; buc:BU188; -.
DR PATRIC; fig|107806.10.peg.199; -.
DR eggNOG; COG0847; Bacteria.
DR HOGENOM; CLU_082724_0_0_6; -.
DR OMA; CYMVNHL; -.
DR Proteomes; UP000001806; 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 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..221
FT /note="Ribonuclease T"
FT /id="PRO_0000208956"
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 221 AA; 24699 MW; EFB66808C8CCBDEF CRC64;
MSTNQEFNLL SNRFRTFYPV VIDIETAGFN ANTDAVLEIA IITLKMDELG WLHKEDTLHF
HIEPFKGSII NSDAIAFNKI DPFNPLRGAI SEKIAIQSIL KKVRNGIKIQ GCSRGIVVAH
NANFDHNFLM AAIQRVKIKN NPFHPFATFD TAALSGLVVG QTVLSKACKA IGLSFDNHQA
HSALYDTLQT ANLFCELVNR WKRLGGWPVD IKKNNSTSNK Y
