ID   RNB_BUCAP               Reviewed;         646 AA.
AC   Q8K9Q5;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Exoribonuclease 2;
DE            EC=3.1.13.1;
DE   AltName: Full=Exoribonuclease II;
DE            Short=RNase II;
DE            Short=Ribonuclease II;
GN   Name=rnb; OrderedLocusNames=BUsg_256;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- FUNCTION: Involved in mRNA degradation. Hydrolyzes single-stranded
CC       polyribonucleotides processively in the 3' to 5' direction (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC         nucleoside 5'-phosphates.; EC=3.1.13.1;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase II subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE013218; AAM67814.1; -; Genomic_DNA.
DR   RefSeq; WP_011053781.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9Q5; -.
DR   SMR; Q8K9Q5; -.
DR   STRING; 198804.BUsg_256; -.
DR   PRIDE; Q8K9Q5; -.
DR   EnsemblBacteria; AAM67814; AAM67814; BUsg_256.
DR   KEGG; bas:BUsg_256; -.
DR   eggNOG; COG4776; Bacteria.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
DR   OrthoDB; 1602988at2; -.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
DR   GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.50.140; -; 2.
DR   HAMAP; MF_01036; RNase_II; 1.
DR   InterPro; IPR011129; CSD.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR013223; RNase_B_OB_dom.
DR   InterPro; IPR011804; RNase_II.
DR   InterPro; IPR001900; RNase_II/R.
DR   InterPro; IPR022966; RNase_II/R_CS.
DR   InterPro; IPR004476; RNase_II/RNase_R.
DR   Pfam; PF08206; OB_RNB; 1.
DR   Pfam; PF00773; RNB; 1.
DR   SMART; SM00357; CSP; 1.
DR   SMART; SM00955; RNB; 1.
DR   SUPFAM; SSF50249; SSF50249; 4.
DR   TIGRFAMs; TIGR00358; 3_prime_RNase; 1.
DR   TIGRFAMs; TIGR02062; RNase_B; 1.
DR   PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Nuclease; RNA-binding.
FT   CHAIN           1..646
FT                   /note="Exoribonuclease 2"
FT                   /id="PRO_0000166378"
FT   DOMAIN          563..645
FT                   /note="S1 motif"
SQ   SEQUENCE   646 AA;  74775 MW;  87FA3049920CAC9A CRC64;
     MFQNNPLLAQ LKKNLHAKTP RVEGIVKSTE RGFGFLEVDA QKSYFIPPKN MKNVMHGDKI
     SAVLKIEKDR EIAEPEKLIE PFLNRFVGKI EKKDNKLFIF PDYPFLKDFI ACRPKKSCVH
     VFQTGDWAVA KLIQHKLNGN HIFYAELIEE IVKANNPLIP WWVTLSRHNL ERKEPKIEKD
     DLILKNNSHR EDLTHLNFIT IDNFNTKDID DALFIEEIHN GNLRLIVAIA DPTSYIKSGS
     KLDITAAKRG FTNYLPGFNV PMLPRSLSED ICSLNPHERR PVLACCITIL KDGNICSKIN
     FFLAWIKSKS KLSYDNVSDW IEKKSSWKPE TKSIENQILL LHRLCLLRIK WRTSNAVLFQ
     DSLEYRFQFS ETGIVEDVVI EKRRIAHKII EESMIIANIS AANFLSKNLG FGIYNTHAGF
     DPINAENVVS FLNNYNLKFT VKEITTLKGF CNLRRVLNIL SDNYINSRIR RYQSFGDFSI
     TPSPHFALGL VEYATWTSPI RKYSDMINHR LLKSIINQDT NITKPSEDIK LKISEQKRRN
     RIAERDISDW LYTLLLQKKE FKNKKFNAEI IDVSRSGIRA KLLENGANVF IPALFLHPIR
     EELVFNQETG KVFIKGVLYY KISDLITVVL SEIRLQTRSI IARIDH