ID   RNB_YERPB               Reviewed;         644 AA.
AC   B2K4J2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=YPTS_2227;
OS   Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB1/+;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT   "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001048; ACC89188.1; -; Genomic_DNA.
DR   RefSeq; WP_011192452.1; NZ_CP009780.1.
DR   AlphaFoldDB; B2K4J2; -.
DR   SMR; B2K4J2; -.
DR   GeneID; 66841410; -.
DR   KEGG; ypb:YPTS_2227; -.
DR   PATRIC; fig|502801.10.peg.1619; -.
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; 2.40.50.640; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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   NCBIfam; TIGR00358; 3_prime_RNase; 1.
DR   NCBIfam; TIGR02062; RNase_B; 1.
DR   PANTHER; PTHR23355:SF37; EXORIBONUCLEASE 2; 1.
DR   PANTHER; PTHR23355; RIBONUCLEASE; 1.
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; Nucleic acid-binding proteins; 4.
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_1000135882"
FT   DOMAIN          561..643
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   644 AA;  72961 MW;  C0962ED45682D052 CRC64;
     MFQDNPLLAQ LKQQLHTQTP RVEGVVKGTE KGFGFLEVDG QKSYFIPPPQ MKKVMHGDRI
     IATLHTDKDR EIAEPETLVE PFLSRFVGRV QRKDDRLSIV PDHPLLRDAI QCRPVRELTH
     SFQNGDWVVA 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 LKANGVDADP QALLTLPGFC ELRRHLDALP TQFLDSRIRR FQTFAEISTV
     PGPHFGLGLE AYATWTSPIR KYGDMVNHRL LKAMITGQQA EKPQEEITVQ LAERRRLNRM
     AERDVGDWLY ARYLQPQAGT DTRFTAEIID ITRGGLRVRL LDNGAVAFIP APFIHAVRDE
     VVCSQETGTV QIKGETVYSQ SDKIEVRIAE VRMETRNVIA RPVA
//