ID   RNT_AZOVI               Reviewed;         116 AA.
AC   Q9Z5X0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 62.
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};
DE   Flags: Fragment;
GN   Name=rnt {ECO:0000255|HAMAP-Rule:MF_00157};
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Garg R.P., Kurtz D.M. Jr.;
RT   "Azotobacter vinelandii bfd (bacterioferritin-associated ferredoxin).";
RL   Submitted (JAN-1999) 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   -!- 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; AF121138; AAD19703.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Z5X0; -.
DR   SMR; Q9Z5X0; -.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004540; F:ribonuclease activity; 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   SUPFAM; SSF53098; SSF53098; 1.
PE   3: Inferred from homology;
KW   Exonuclease; Hydrolase; Nuclease; tRNA processing.
FT   CHAIN           <1..116
FT                   /note="Ribonuclease T"
FT                   /id="PRO_0000208955"
FT   DOMAIN          18..99
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT   ACT_SITE        86
FT                   /note="Proton donor/acceptor"
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            51
FT                   /note="Important for substrate binding and specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00157"
FT   NON_TER         1
SQ   SEQUENCE   116 AA;  12769 MW;  55A83D7454433B7F CRC64;
     LQEIFRGVRK AVKSHGCKRA ILVGHNSSFD LAFLNAAVAR CDIKRNPFHP FSSFDTATLA
     GLAYGQTVLA KACQSAGIEF DGREAHSARY DTEKTAELFC GIVNRWKEMG GWVDFA