ID   RNB_VIBCM               Reviewed;         678 AA.
AC   C3LW69;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=VCM66_A0764;
OS   Vibrio cholerae serotype O1 (strain M66-2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=579112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M66-2;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(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; CP001234; ACP07724.1; -; Genomic_DNA.
DR   RefSeq; WP_000484954.1; NC_012580.1.
DR   AlphaFoldDB; C3LW69; -.
DR   SMR; C3LW69; -.
DR   EnsemblBacteria; ACP07724; ACP07724; VCM66_A0764.
DR   GeneID; 57742185; -.
DR   KEGG; vcm:VCM66_A0764; -.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
DR   Proteomes; UP000001217; Chromosome II.
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; 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; 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..678
FT                   /note="Exoribonuclease 2"
FT                   /id="PRO_1000149460"
FT   DOMAIN          568..650
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
FT   REGION          659..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   678 AA;  76149 MW;  F1F3E282087CA5EB CRC64;
     MFQDNPLLAQ LKQKIQETLP KKEGTIKASD KGFGFLEVDS KTSYFVPPPY MKKCMHGDKV
     VAFIRTENER EVAEPSELIE QSLTRFIGRV KLFKGKLNVA PDHPQLKKLS LKAKTKKGLN
     EADFQEGDWV VAHLVRHPLK GDDGFFVQIS HKITDANDKI APWWVTLAEN DLPNSEPAGI
     DDWQLKDDAD LVREDLTALP FVTIDGESTK DMDDALYAQQ LPNGDFALTI AIADPTAYIT
     PEDEMDKVAR ERGFTIYLPG RNIPMLPRDL ADELCSLMEN QVRPALCCSV TIRKDGVIGD
     DIRFFAANIK SHARLVYDHV SDWLETGSSE QWQPSEEIAQ VVRDLYAFSQ ARANWRETHA
     VVFPDRPDYR FELSADNDVV AIHADMRRTA NRLVEESMIT ANICAGKTLQ TTFGFGVFNT
     HAGFKAEKMA DVVELMAVNG APNADAETLA TVEGFAALRR WLATQETSYL DNRIRKYQSY
     SEIGNQPLPH FAMGLDVYAT WTSPIRKYGD MINHRLLKAH ILGKAPVQTP DETVGEELAL
     HRKHHKIAER NVADWLYART LADEPAKETR FQAEIFDINR PGMRVRLLEN GAMAFIPGAL
     ILDNKERIEC NGEDGTVLID KEVVYKLGDV LEIVLTEVNQ ENRSLVGKPT QVFADLVSET
     QTSAEQPAEG AENNEPQV