ID   RNB_YERPG               Reviewed;         644 AA.
AC   A9R8T9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
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};
GN   OrderedLocusNames=YpAngola_A2244;
OS   Yersinia pestis bv. Antiqua (strain Angola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Angola;
RX   PubMed=20061468; DOI=10.1128/jb.01518-09;
RA   Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA   Achtman M., Lindler L.E., Ravel J.;
RT   "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT   new insights into the evolution and pangenome of the plague bacterium.";
RL   J. Bacteriol. 192:1685-1699(2010).
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; CP000901; ABX88295.1; -; Genomic_DNA.
DR   RefSeq; WP_002210605.1; NZ_CP009935.1.
DR   AlphaFoldDB; A9R8T9; -.
DR   SMR; A9R8T9; -.
DR   GeneID; 57976433; -.
DR   KEGG; ypg:YpAngola_A2244; -.
DR   PATRIC; fig|349746.12.peg.3248; -.
DR   OMA; CFTNYLP; -.
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; IPR040476; CSD2.
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; PF17876; CSD2; 1.
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_1000135883"
FT   DOMAIN          561..643
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   644 AA;  72875 MW;  EC59E0463F46CB2E CRC64;
     MFQDNPLLAQ LKQQLHTQTP RVEGVVKGTE KGFGFLEVDG QKSYFIPPPQ MKKVMHGDRI
     IATLHTDKDR EIAEPETLVE PFLSRFVGRV QRKDDRLSIV PDHPLLRDAI QCRPVRELTH
     SFQNGDWAVA EMCRHPLKGD RAFQADLTAF ITNGEDHFVP WWVTLARHNL EREAPAMVES
     ALNDAELERE DLTALNFVTI DSASTEDMDD ALFVQDNGDG SWLLTIAIAD PTAYVVENSE
     LDLTARKRAF TNYLPGFNIP MLPRDLSDNL CSLRPNERRP VLVCRVTITE EGTLSNDIRF
     SAAWVESKAK LVYDDVSDWL EGNNRWQPQD TAIAEQITLL KRICDARSNW RQQHALVFKD
     RPDYRFLLGE KGEVLDIIVE HRRIANRIVE ECMIAANVCA ALALREHLGF GIYNVHTGFD
     PALVEQAASV LKANGVGADP QALLTLPGFC ELRRHLDALP TQFLDSRIRR FQTFAEISTV
     PGPHFGLGLE AYATWTSPIR KYGDMVNHRL LKAMITGQQA EKPQEEITVQ LAERRRLNRM
     AERDVGDWLY ARYLQPQAGT DTRFTAEIID ITRGGLRVRL LDNGAVAFIP APFIHAVRDE
     VVCSQETGTV QIKGETVYSQ SDKIEVRIAE VRMETRNVIA RPVA