ID   RNB_ERWT9               Reviewed;         647 AA.
AC   B2VKS8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=ETA_16280;
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
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; CU468135; CAO96674.1; -; Genomic_DNA.
DR   RefSeq; WP_012441367.1; NC_010694.1.
DR   AlphaFoldDB; B2VKS8; -.
DR   SMR; B2VKS8; -.
DR   STRING; 465817.ETA_16280; -.
DR   EnsemblBacteria; CAO96674; CAO96674; ETA_16280.
DR   KEGG; eta:ETA_16280; -.
DR   eggNOG; COG4776; Bacteria.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
DR   OrthoDB; 1602988at2; -.
DR   Proteomes; UP000001726; 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; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..647
FT                   /note="Exoribonuclease 2"
FT                   /id="PRO_1000135869"
FT   DOMAIN          564..646
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   647 AA;  72686 MW;  12AEC82F2DA7C665 CRC64;
     MFQDNPLLAQ LKEKLHSQTP RVEGVVKGTE KGFGFLEVDA QKSYFIPPPF MKKVMHGDRV
     SAVIQSDKDR EVADPETLIE PFLTRFVGRV QKKDDRLSII PDHPLLKDAI QCRPERSVKH
     DFQAGDWAVA EMRRHPLKGD RTFYAELTEF ITTAEDHLAP WWVTLSRHNL EREAPDVTTP
     QSMLDEQLER EDLTSLPFVT IDSASTEDMD DALYVEDAGN GALKLIVAIA DPTAYVPVGS
     KLDAVAAERA FTNYLPGFNI PMLPRQLSDD ICSLRPHERR PVLACRITLA ADGTPADDVQ
     FFAAWIESHA KLAYNDVSDW LETGGSSAWQ PENEAIANQI RLLNRLCLAR SEWRQAHALV
     FKDRPDFRFL LGEKGEVLDI IAEHRRIANR IVEESMILAN ICAATVLRDR LGFGIYNVHL
     GFDEANAEQA AAVLANHGVT ADPLAIATLE GFRNLRRELD ALPTQFLDSR IRRFQSFAEV
     STTPGPHFGL GLEAYATWTS PIRKYGDMVN HRLLKAIIKG EQSARPADEL SLKMAERRRQ
     NRMAERDVGD WLYSRFLQKA AGSEQRFSAE VIDVSRGGMR VRLQENGAVA FIPAPFIHAV
     RDEMVCSNEN GSVQIKGEVA YRVTDLIEVT IAEVRMETRS IVARPVA