ID   RNB_YERE8               Reviewed;         644 AA.
AC   A1JM34;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Exoribonuclease 2 {ECO:0000255|HAMAP-Rule:MF_01036};
DE            EC=3.1.13.1 {ECO:0000255|HAMAP-Rule:MF_01036};
DE   AltName: Full=Exoribonuclease II {ECO:0000255|HAMAP-Rule:MF_01036};
DE            Short=RNase II {ECO:0000255|HAMAP-Rule:MF_01036};
DE            Short=Ribonuclease II {ECO:0000255|HAMAP-Rule:MF_01036};
GN   Name=rnb {ECO:0000255|HAMAP-Rule:MF_01036}; OrderedLocusNames=YE1982;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Involved in mRNA degradation. Hydrolyzes single-stranded
CC       polyribonucleotides processively in the 3' to 5' direction.
CC       {ECO:0000255|HAMAP-Rule:MF_01036}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC         nucleoside 5'-phosphates.; EC=3.1.13.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01036};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01036}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase II subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01036}.
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DR   EMBL; AM286415; CAL12061.1; -; Genomic_DNA.
DR   RefSeq; WP_005169906.1; NC_008800.1.
DR   RefSeq; YP_001006235.1; NC_008800.1.
DR   AlphaFoldDB; A1JM34; -.
DR   SMR; A1JM34; -.
DR   STRING; 393305.YE1982; -.
DR   EnsemblBacteria; CAL12061; CAL12061; YE1982.
DR   KEGG; yen:YE1982; -.
DR   PATRIC; fig|393305.7.peg.2143; -.
DR   eggNOG; COG4776; Bacteria.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
DR   Proteomes; UP000000642; 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   InterPro; IPR003029; S1_domain.
DR   Pfam; PF08206; OB_RNB; 1.
DR   Pfam; PF00773; RNB; 1.
DR   Pfam; PF00575; S1; 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..644
FT                   /note="Exoribonuclease 2"
FT                   /id="PRO_1000063903"
FT   DOMAIN          561..643
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   644 AA;  72724 MW;  162E4C6A3BBDA5F4 CRC64;
     MFQDNPLLAQ LKQQLHTQTP RVEGVVKGTE KGFGFLEVDG QKSYFIPPPQ MKKVMHGDRI
     IATLHTDKDR EIAEPETLVE PFLSRFVGRV QRKDDRLSIV PDHPLLRDAI QCRPVRELTH
     DFQSGDWAVA EMRRHPLKGD RGFNADLTAF ITDGEDHFVP WWVTLARHNL EREAPVMVES
     ALHDANLQRE DLTALNFVTI DSASTEDMDD ALQVQDNGDG SLLLTIAIAD PTAYVDENSE
     LDLIARKRAF TNYLPGFNIP MLPRDLSDNL CSLRPNERRP VLVCRVTIAA DGTLGEDIHF
     SAAWVESKAK LVYDEVSDWL EGSGDWQPQN ADIAEQITLL KRVCEARSHW REQHALVFKD
     RPDYRFLLGE KGEVLDIIVE HRRIANRIVE ECMIAANVCA AIALRDNLGF GIYNVHTGFD
     PALVEQAANV LQANGVEADP QALLTLPGFC ELRRHLDALP TQFLDSRIRR FQTFAEISTV
     PGPHFGLGLE AYATWTSPIR KYGDMVNHRL LKAIITGQQA EKPQDEITVQ LAERRRLNRM
     AERDVGDWLY ARYLQPMAGT DTRFPAEIID VTRGGLRVRL LDNGAVAFIP APFIHAVRDE
     MVCSQETGTV QIKGETVYSQ SDKIEVRIAE VRMETRNVVA RPVV