ID   RNB_BAUCH               Reviewed;         645 AA.
AC   Q1LTG8;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=BCI_0297;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H.,
RA   Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial symbiosis of
RT   sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
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; CP000238; ABF14302.1; -; Genomic_DNA.
DR   RefSeq; WP_011520479.1; NC_007984.1.
DR   AlphaFoldDB; Q1LTG8; -.
DR   SMR; Q1LTG8; -.
DR   STRING; 374463.BCI_0297; -.
DR   EnsemblBacteria; ABF14302; ABF14302; BCI_0297.
DR   KEGG; bci:BCI_0297; -.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
DR   OrthoDB; 1602988at2; -.
DR   Proteomes; UP000002427; 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..645
FT                   /note="Exoribonuclease 2"
FT                   /id="PRO_0000409533"
FT   DOMAIN          563..645
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   645 AA;  74194 MW;  A0B51F53E7B2E5E8 CRC64;
     MFQDHPLLIQ LKQQLYDKEL RMVGVVKSTD KGFGFLEVNA QKSYFIPPLF MKKVMHGDKI
     SAVLRIVNNR AIAEPETLIE PFLSRFVGKV QIKNDKLALL PKHPLIKEII PASQPRSMKN
     TQLCHGDWVI AEMCHHPLDG YRYFYAKITE LITTKDDNFA HWRVTLAHYN LEREAPAMPK
     YLTIQDNGLI REDLTELNFI TIDHASTEDI DDALHVAYGT NGALVLTIAI ADPTAWIIAG
     SQLDCIARDR AFTNYLPGFN IPMLPRMLSE DLCSLRAYEK RPALVCQVTM QHDGTLNEDM
     RFFAAWIESK AKLSYDEVSD WIENIGFWQP QNNAIAEQIR MLHIVCQARS SWRKQHALVF
     KDKPDYRFIL EENGNVKNII AEPRRIAKRM IEEAMITANI CAARVLRDNL GFGLYNTHNG
     FDTTLIDQVV AILQKHNISV DATQLLTLEG FCALRRKLNT MSTSYLDSRI RRFQTLSELK
     TEPGPHFGLG LEVYATWTSP IRKYSDMMNH RLLKALIGAG KAERPKTDIT FRMSERRRQN
     RIAERDVEDW LYASFLKNQV GSHIRYSAEI IDIYRNGMRI RLLDNGAIAF IPALLIHNIR
     DELICNQDIG IVQIQGKERY RQGDTIEVYI KEVHIDNRSI IAKIV