RNB_ENT38
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 03-AUG-2022, entry version 91.
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; Proteobacteria; 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 EnsemblBacteria; ABP60855; ABP60855; Ent638_2180.
DR KEGG; ent:Ent638_2180; -.
DR eggNOG; COG4776; Bacteria.
DR HOGENOM; CLU_002333_7_3_6; -.
DR OMA; CFTNYLP; -.
DR OrthoDB; 1602988at2; -.
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; 2.40.50.140; -; 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_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