ID   RNB_BUCAT               Reviewed;         649 AA.
AC   B8D7G3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=BUAPTUC7_263;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=561501;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuc7;
RX   PubMed=19150844; DOI=10.1126/science.1167140;
RA   Moran N.A., McLaughlin H.J., Sorek R.;
RT   "The dynamics and time scale of ongoing genomic erosion in symbiotic
RT   bacteria.";
RL   Science 323:379-382(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}.
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DR   EMBL; CP001158; ACL30078.1; -; Genomic_DNA.
DR   RefSeq; WP_009874220.1; NC_011834.1.
DR   AlphaFoldDB; B8D7G3; -.
DR   SMR; B8D7G3; -.
DR   KEGG; bau:BUAPTUC7_263; -.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
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   Pfam; PF08206; OB_RNB; 1.
DR   Pfam; PF00773; RNB; 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..649
FT                   /note="Exoribonuclease 2"
FT                   /id="PRO_1000149455"
FT   DOMAIN          562..644
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   649 AA;  75132 MW;  B1F28EC2ECCF97DF CRC64;
     MFQNNPLLTQ LKKNLHAKSP RVEGIVKSTE RGFGFLEVDP QKSYFIPPKN MKNVMHGDKI
     IALLTTEKDR EIVEPEKLIE PFLNRFVGKI EKKDNRLFIV PDYPFLKDLI TCQPNKNCIN
     IFQNGDWAVA QLKKHKLKGD HLFYAELTEK ITQEDDPLIP WWVTLARHDL DRKEPLAEED
     DLILKESDNR KDLTDLDFIT IDNTNTKDID DALFVSEKNN GDISLIVAIA DPTAYIKHGS
     KLDVIASKRI FTNYLPGFNI PMLPRNLSED ICSLNPNKRR PVLACHITVL KNGNISNKIE
     FFLAWIKSKS KLSYDHVSDW IEKIGSWIPP TKSIANQILI LHRLCLLRIK WRKKNAVLFK
     DSIEYRFHVS EHGKIIDVLI EKRRIAHKII EESMIVANIS AANFLSKNIG FGIYNVHSGF
     DLVNAENAVS FLRSYNLNFT VKEITTLKGF CNLRRVLNII SNNYIDSRIR RFQSFGDFST
     IPGPHFALGF SEYATWTSPI RKYSDMINHR LLKSIIKKEK SIKPGEDIKI KISEQRRRNR
     MAERDVSDWL YTIFLQKKKY QNQKFNAEIT DISRSGIRAR LIENGANVFI PGTLIHPIRE
     ELNFNQESGK VFINGIMHYK ISDLIQVTLS DIRLKTRSII AKPVFEKFK