ID   RNB_EDWTE               Reviewed;         647 AA.
AC   D0Z8E6;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 2.
DT   24-JAN-2024, entry version 73.
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=ETAE_1878;
OS   Edwardsiella tarda (strain EIB202).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=498217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EIB202;
RX   PubMed=19865481; DOI=10.1371/journal.pone.0007646;
RA   Wang Q., Yang M., Xiao J., Wu H., Wang X., Lv Y., Xu L., Zheng H., Wang S.,
RA   Zhao G., Liu Q., Zhang Y.;
RT   "Genome sequence of the versatile fish pathogen Edwardsiella tarda provides
RT   insights into its adaptation to broad host ranges and intracellular
RT   niches.";
RL   PLoS ONE 4:E7646-E7646(2009).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACY84715.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001135; ACY84715.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; D0Z8E6; -.
DR   SMR; D0Z8E6; -.
DR   KEGG; etr:ETAE_1878; -.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OrthoDB; 9764149at2; -.
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..647
FT                   /note="Exoribonuclease 2"
FT                   /id="PRO_0000409535"
FT   DOMAIN          563..645
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   647 AA;  72754 MW;  5CAB459060AFDFA7 CRC64;
     MFQDNPLLAQ LKQQLHSQTP RVEGVVKGTD KGFGFLEVDA QKSYFIPPPQ MKKVMHGDRV
     RAAVQVDKER EIAEPEELLE PFLTRFVGRI QKKENDERLS IIPDHSLLKD AIGCRPARGL
     DRAFRQGDWV LAEMRRHPLK GDRSFFAEIT AFITDGSDHF APWWVTLTRH DLARSAPQWQ
     AGTLLEEGLA REDLCALPFV TIDSASTEDM DDALHVRENA DGSLCLTIAI ADPTAYVSAD
     SPLDAEARHR AFTTYLPGFN IPMLPRDLSD DLCSLREGQR RPVLACEVTL DADGSLRDDI
     RFFSGWIESK AKLVYDRVSD WLEGRGDWQP PSDDIAAQIR LLHRVANART QWRQQHALVF
     RDRPDYRFVL DDHGDVTDIV AEPRRVANRI VEECMITANV CAALVLRERL GFGIYNVHTG
     FDPALVEQAV SLLNANDVAA NAEALLTLDG FCTLRRHLDS LPSTFLDSRI RRFQTFAEIS
     TEPGPHFGLG LEAYATWTSP IRKYGDMVNH RLLKALIAGA PATRPDPAMT LQLAERRRQN
     RMAERDVGDW LYARFLKDKV NAPTPFNAEI IDISRGGMRV RLLENGAVAF IPASFIHAVR
     DEMVCSQENG TLQVKGSVVY RQGDTVPVTL SEVRLDTRSL IARPFSA
//