ID   RNB_VIBPA               Reviewed;         668 AA.
AC   Q87IJ9;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=VPA0607;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(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}.
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DR   EMBL; BA000032; BAC61950.1; -; Genomic_DNA.
DR   RefSeq; NP_800117.1; NC_004605.1.
DR   RefSeq; WP_005489296.1; NC_004605.1.
DR   AlphaFoldDB; Q87IJ9; -.
DR   SMR; Q87IJ9; -.
DR   STRING; 223926.28808842; -.
DR   EnsemblBacteria; BAC61950; BAC61950; BAC61950.
DR   GeneID; 1191296; -.
DR   KEGG; vpa:VPA0607; -.
DR   PATRIC; fig|223926.6.peg.3547; -.
DR   eggNOG; COG4776; Bacteria.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
DR   Proteomes; UP000002493; Chromosome 2.
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.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..668
FT                   /note="Exoribonuclease 2"
FT                   /id="PRO_0000166391"
FT   DOMAIN          568..650
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   668 AA;  75438 MW;  F1A1C2D6E2D25648 CRC64;
     MFQDNPLLAQ LKQQIQENLP KKEGSIKATD KGFGFLEVDS KTSFFIPPAY MKKCIHGDKV
     VAIIRTENER EVAEPQELIE QSLTRFIGRV KMFKGKLNVV PDHPQLKKLS LKAKLKKGLK
     PDNFAEGDWV VAHLVRHPLK GDNTFFVEIS EKITDADDKI APWWVTLAQN DLPNSEPAGI
     ENWELKDDAD LERIEMTHVP FVTIDGESTK DMDDALYAKK TESGDFELTI AIADPTAYIT
     PEDEMDKVAR ERGYTIYLPG RNIPMLPRDL ADNLCSLIEG EIRPAICCTV TVSKDGVIGD
     DIKFFAANIK SHARLAYDHV SDWLENGNSD AWQPSEEIAT IVRDLYEFSL ARAEWREKNA
     VVFPDRPDYR FELSEDNDVI AIHADMRRSA NRLVEESMIT ANICAGRTLR EKFETGVFNT
     HAGLKPEKIE EVVQLVNPEG TLEFTAESIA TLEGFAALRR WLAVQETSYL DNRIRKFQAY
     SEVGNQPLPH YAMGLDIYAT WTSPIRKYGD MINHRMLKAV ILDKEPVQKP DDQVGEELAL
     HRKHHKIAER NVSDWLYART LADEPSKQTC FTGEIFDINR AGARVRLLEN GAAAFIPGAL
     ILDNKERIEC NGDNGTISID KEVVYKLGDT LEIVLADVNQ ENRSLVAKPT QVFADQPAPQ
     TEQTVSEE