ID   ORN_RHOJR               Reviewed;         199 AA.
AC   Q0SGU7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Oligoribonuclease {ECO:0000255|HAMAP-Rule:MF_00045};
DE            EC=3.1.15.- {ECO:0000255|HAMAP-Rule:MF_00045};
GN   Name=orn {ECO:0000255|HAMAP-Rule:MF_00045}; OrderedLocusNames=RHA1_ro01418;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- FUNCTION: 3'-to-5' exoribonuclease specific for small
CC       oligoribonucleotides. {ECO:0000255|HAMAP-Rule:MF_00045}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00045}.
CC   -!- SIMILARITY: Belongs to the oligoribonuclease family.
CC       {ECO:0000255|HAMAP-Rule:MF_00045}.
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DR   EMBL; CP000431; ABG93239.1; -; Genomic_DNA.
DR   RefSeq; WP_011594440.1; NC_008268.1.
DR   AlphaFoldDB; Q0SGU7; -.
DR   SMR; Q0SGU7; -.
DR   STRING; 101510.RHA1_ro01418; -.
DR   EnsemblBacteria; ABG93239; ABG93239; RHA1_ro01418.
DR   KEGG; rha:RHA1_ro01418; -.
DR   PATRIC; fig|101510.16.peg.1443; -.
DR   eggNOG; COG1949; Bacteria.
DR   HOGENOM; CLU_064761_3_0_11; -.
DR   OMA; AFFHYRN; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd06135; Orn; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   HAMAP; MF_00045; Oligoribonuclease; 1.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR022894; Oligoribonuclease.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR11046; PTHR11046; 1.
DR   Pfam; PF00929; RNase_T; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome.
FT   CHAIN           1..199
FT                   /note="Oligoribonuclease"
FT                   /id="PRO_1000004280"
FT   DOMAIN          5..170
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00045"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00045"
SQ   SEQUENCE   199 AA;  22036 MW;  D17879FC54840D3B CRC64;
     MQDKLVWIDC EMTGLRLGTD KLIEIAALVT DSELNVLGEG VDIVIHADDD ALAAMPDVVT
     KMHENSGLTD EVRKSTVTLA EAEQQVLAYI REHVPVAGTA PLAGNSIATD RGFIARDMPD
     LDTYLHYRMI DVSSIKELSR RWYPRIYFGQ PEKGLAHRAL ADIRESIREL KYYRKTAFVP
     EPGPSTSDIA AVVEELGPA