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Database: UniProt
Entry: B1ITG7
LinkDB: B1ITG7
Original site: B1ITG7 
ID   RNB_ECOLC               Reviewed;         644 AA.
AC   B1ITG7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   16-APR-2014, entry version 40.
DE   RecName: Full=Exoribonuclease 2;
DE            EC=3.1.13.1;
DE   AltName: Full=Exoribonuclease II;
DE            Short=RNase II;
DE            Short=Ribonuclease II;
GN   Name=rnb; OrderedLocusNames=EcolC_2339;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-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 (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'-
CC       direction to yield nucleoside 5'-phosphates.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase II
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 S1 motif domain.
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DR   EMBL; CP000946; ACA77974.1; -; Genomic_DNA.
DR   RefSeq; YP_001725301.1; NC_010468.1.
DR   ProteinModelPortal; B1ITG7; -.
DR   SMR; B1ITG7; 5-644.
DR   STRING; 481805.EcolC_2339; -.
DR   EnsemblBacteria; ACA77974; ACA77974; EcolC_2339.
DR   GeneID; 6065623; -.
DR   KEGG; ecl:EcolC_2339; -.
DR   PATRIC; 18227550; VBIEscCol82905_2498.
DR   eggNOG; COG4776; -.
DR   HOGENOM; HOG000271427; -.
DR   KO; K01147; -.
DR   OMA; PWWVTLS; -.
DR   OrthoDB; EOG6Q5NRD; -.
DR   ProtClustDB; PRK05054; -.
DR   BioCyc; ECOL481805:GI3G-2385-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01036; RNase_II; 1.
DR   InterPro; IPR011129; Cold_shock_prot.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR003029; Rbsml_prot_S1_RNA-bd_dom.
DR   InterPro; IPR022967; RNA-binding_domain_S1.
DR   InterPro; IPR013223; RNase_B_OB_dom.
DR   InterPro; IPR011804; RNase_II.
DR   InterPro; IPR022966; RNase_II/R_CS.
DR   InterPro; IPR004476; RNase_II/RNase_R.
DR   Pfam; PF08206; OB_RNB; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00357; CSP; 1.
DR   SMART; SM00316; S1; 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   Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Nuclease;
KW   RNA-binding.
FT   CHAIN         1    644       Exoribonuclease 2.
FT                                /FTId=PRO_1000084279.
FT   DOMAIN      561    643       S1 motif.
SQ   SEQUENCE   644 AA;  72509 MW;  3387266195A9B066 CRC64;
     MFQDNPLLAQ LKQQLHSQTP RAEGVVKATE KGFGFLEVDA QKSYFIPPPQ MKKVMHGDRI
     IAVIHSEKER ESAEPEELVE PFLTRFVGKV QGKNDRLAIV PDHPLLKDAI PCRAARGLNH
     EFKEGDWAVA EMRRHPLKGD RSFYAELTQY ITFGDDHFVP WWVTLARHNL EKEAPDGVAT
     EMLDEGLVRE DLTALDFVTI DSASTEDMDD ALFAKALPDD KLQLIVAIAD PTAWIAEGSK
     LDKAAKIRAF TNYLPGFNIP MLPRELSDDL CSLRANEVRP VLACRMTLSA DGTIEDNIEF
     FAATIESKAK LVYDQVSDWL ENTGDWKPES EAIAEQVRLL AQICQRRGEW RHNHALVFKD
     RPDYRFILGE KGEVLDIVAE PRRIANRIVE EAMIAANICA ARVLRDKLGF GIYNVHMGFD
     PANADALAAL LKTHGLHVDA EEVLTLDGFC KLRRELDAQP TGFLDSRIRR FQSFAEISTE
     PGPHFGLGLE AYATWTSPIR KYGDMINHRL LKAVIKGETA TRPQDEITVQ MAERRRLNRM
     AERDVGDWLY ARFLKDKAGT DTRFAAEIVD ISRGGMRVRL VDNGAIAFIP APFLHAVRDE
     MVCSQENGTV QIKGETVYKV TDVIDVTIAE VRMETRSIIA RPVA
//
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