ID   ORN_SALPA               Reviewed;         181 AA.
AC   Q5PLG7;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 84.
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=SPA4167;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000026; AAV79907.1; -; Genomic_DNA.
DR   RefSeq; WP_001271546.1; NC_006511.1.
DR   AlphaFoldDB; Q5PLG7; -.
DR   SMR; Q5PLG7; -.
DR   PRIDE; Q5PLG7; -.
DR   EnsemblBacteria; AAV79907; AAV79907; SPA4167.
DR   KEGG; spt:SPA4167; -.
DR   HOGENOM; CLU_064761_2_0_6; -.
DR   OMA; AFFHYRN; -.
DR   Proteomes; UP000008185; 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.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..181
FT                   /note="Oligoribonuclease"
FT                   /id="PRO_0000111067"
FT   DOMAIN          8..171
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00045"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00045"
SQ   SEQUENCE   181 AA;  20632 MW;  70ACBE7616D6D824 CRC64;
     MSADENNLIW IDLEMTGLDP ERDRIIEIAT LVTDASLNIL AEGPTIAVHQ SDAQLALMDD
     WNVRTHTGSG LVDRVKASTM GERDAELATI EFLKTWVPAG KSPICGNSIG QDRRFLFKYM
     PELEAYFHYR YLDVSTLKEL ARRWKPEILA GFTKQGTHQA MDDIRESVAE LAYYREHFIK
     L