ID   RNB_VIBVY               Reviewed;         664 AA.
AC   Q7MEL4;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 2.
DT   03-AUG-2022, entry version 113.
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=VVA0656;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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=BAC96682.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000038; BAC96682.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_015727827.1; NC_005140.1.
DR   AlphaFoldDB; Q7MEL4; -.
DR   SMR; Q7MEL4; -.
DR   STRING; 672.VV93_v1c36570; -.
DR   EnsemblBacteria; BAC96682; BAC96682; BAC96682.
DR   KEGG; vvy:VVA0656; -.
DR   PATRIC; fig|196600.6.peg.3850; -.
DR   eggNOG; COG4776; Bacteria.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
DR   OrthoDB; 1602988at2; -.
DR   Proteomes; UP000002675; 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; IPR022967; S1_dom.
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   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.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..664
FT                   /note="Exoribonuclease 2"
FT                   /id="PRO_0000166393"
FT   DOMAIN          568..650
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   664 AA;  75069 MW;  8EFD0B9610CF6E02 CRC64;
     MFQDNPLLAQ LKQQIQENLP KKEGTIKATE KGFGFLEVDS KTSFFIPPAY MKKCMHGDKV
     IAIIRTENER EVAEPQELVE QMLNRFIGRV KMFKGKLNVV PDHPQLKKMS LKAKTKKGLN
     PQEFAEGDWV VGHLIRHPLK DDNGFFVEIS EKITDADDKI APWWVTLAEN DLPNSEPAGI
     DDWQIKDDAD LERIDMTHIP FVTIDGESTK DMDDALYAKK NDAGDFELTI AIADPTAYIT
     PDDEMDKVAR ERGFTIYLPG RNIPMLPRDL ADELCSLIEG EIRPALCCTV TVSKDGVIGD
     DIQFFAANIK SHARLAYDNV SDWLETGSCE KWQPSEEIAA IVRDLYEFSQ ARAEWREKNA
     VVFPDRPDYR FELSEDNDVV AIHADMRRSA NRLVEESMIT ANICAGKTLQ AHFGTGVFNC
     HAGFKPEKIA DVVELVNPEG TLEFTAESIA TREGFAALRR WLSKQETTYL DNRIRKFQTY
     SEVSNQPLPH YAMGLDIYAT WTSPIRKYGD MINHRMLKAL ILNKEPVQKP DDSVGEELAL
     HRKHHKIAER NVADWLYART LADAPENQTL FTGEIFDINR AGMRIRLLEN GAAAFIPGSL
     IIDNKERIEC NGDLGTVSID KEVVYKLGDV LEVVLADVNQ ENRSLVAKPT QVFAELPVVE
     ETQN