RNT_VIBCH
ID RNT_VIBCH Reviewed; 224 AA.
AC Q9KT97;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 102.
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=VC_1006;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF94167.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF94167.1; ALT_INIT; Genomic_DNA.
DR PIR; H82253; H82253.
DR RefSeq; NP_230652.1; NC_002505.1.
DR RefSeq; WP_000130223.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KT97; -.
DR SMR; Q9KT97; -.
DR STRING; 243277.VC_1006; -.
DR DNASU; 2614259; -.
DR EnsemblBacteria; AAF94167; AAF94167; VC_1006.
DR GeneID; 57739691; -.
DR GeneID; 66939771; -.
DR KEGG; vch:VC_1006; -.
DR PATRIC; fig|243277.26.peg.960; -.
DR eggNOG; COG0847; Bacteria.
DR HOGENOM; CLU_082724_0_0_6; -.
DR OMA; CYMVNHL; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IBA:GO_Central.
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:0045004; P:DNA replication proofreading; IBA:GO_Central.
DR GO; GO:0042780; P:tRNA 3'-end processing; IBA:GO_Central.
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..224
FT /note="Ribonuclease T"
FT /id="PRO_0000208976"
FT DOMAIN 20..195
FT /note="Exonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT ACT_SITE 182
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 182
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 187
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 125
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT SITE 147
FT /note="Important for substrate binding and specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
SQ SEQUENCE 224 AA; 24812 MW; 232E06F3AEE2D6DC CRC64;
MTDKNDALTL KKRFRGYFPV VIDVETAGFN AQTDALLEIC AVTLSMDENG DLHPASTIHF
HVEPFEGANL EKAALEFTGI YDPFSPLRGA VSEDHALKEI YKLVRKEQKA ADCSRAIIVA
HNAHFDHSFV MAASERCKLK RVPFHPFATF DTATLSGLAF GQTVLAKACK TAGMEFDNRE
AHSALYDTQK TAELFCTIVN QWKALGGWPL VNDDEDNNND ADLD
