ID   RNB_ENT38               Reviewed;         644 AA.
AC   A4WAX5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 99.
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=Ent638_2180;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(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; CP000653; ABP60855.1; -; Genomic_DNA.
DR   RefSeq; WP_012017570.1; NC_009436.1.
DR   AlphaFoldDB; A4WAX5; -.
DR   SMR; A4WAX5; -.
DR   STRING; 399742.Ent638_2180; -.
DR   KEGG; ent:Ent638_2180; -.
DR   eggNOG; COG4776; Bacteria.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OrthoDB; 9764149at2; -.
DR   Proteomes; UP000000230; 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; 2.40.50.640; -; 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; 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; 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_1000063888"
FT   DOMAIN          561..643
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   644 AA;  72518 MW;  0E95B2C3F175D95B CRC64;
     MLQDNPLLAQ LKQQLHSQTP RAEGVVKATE KGFGFLEVDA QKSYFIPPPQ MKKVMHGDRV
     TAVIHTQKDR ETAEPEELIE PFLTRFVGKV HKKDDRLSIV PDHPLLKDAI PCRADRNCEH
     DFKEGDWAVA QMRRHPLKGD RGFYADLTHF ITYSDDHFVP WWVTLARHNL EKEAPNGVAT
     EMLDEGLERR DLTALNFVTI DSASTQDMDD ALYVEEGADG KLHLTVAIAD PTAWIAEGSK
     LDDSAKVRAF TNYLPGFNIP MLPRELSDDL CSLRPNQIRP VLACRMTIAA DGTIEDDIEF
     FAATIESKAK LAYDDVSNWL EGAGNWKPES EAIAQQITLL QRVCLSRGEW RKTHALVFKD
     RPDYRFVLGE KGEVLDIVAE PRRIANRIVE ESMIAANICA ARVLRDKLGF GIYNVHTGFD
     PANTEALAAL LKTHDVHVDP QEVLTLEGFC KLRRELDAQP SGFLDSRIRR FQSYAEISTE
     PGPHFGLGLE AYATWTSPIR KYGDMVNHRL LKAIVKGETI ARPQDEATVQ MAERRRLNRM
     AERDVGDWLY ARFLSDKAGT DTRFAAEIID ISRGGMRVRL VENGAVAFIP APFLHAVRDE
     LVCSQENGSV QIKGETVYKV TDVIDVNIAE VRMETRSIIA RPVV
//