ID   RNB_HAEDU               Reviewed;         659 AA.
AC   Q7VLX8;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Exoribonuclease 2;
DE            EC=3.1.13.1;
DE   AltName: Full=Exoribonuclease II;
DE            Short=RNase II;
DE            Short=Ribonuclease II;
GN   Name=rnb; OrderedLocusNames=HD_1264;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in mRNA degradation. Hydrolyzes single-stranded
CC       polyribonucleotides processively in the 3' to 5' direction (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC         nucleoside 5'-phosphates.; EC=3.1.13.1;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase II subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE017143; AAP96092.1; -; Genomic_DNA.
DR   RefSeq; WP_010945141.1; NC_002940.2.
DR   AlphaFoldDB; Q7VLX8; -.
DR   SMR; Q7VLX8; -.
DR   STRING; 233412.HD_1264; -.
DR   EnsemblBacteria; AAP96092; AAP96092; HD_1264.
DR   KEGG; hdu:HD_1264; -.
DR   eggNOG; COG4776; Bacteria.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
DR   Proteomes; UP000001022; 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; 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; 3.
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..659
FT                   /note="Exoribonuclease 2"
FT                   /id="PRO_0000166383"
FT   DOMAIN          576..658
FT                   /note="S1 motif"
SQ   SEQUENCE   659 AA;  75976 MW;  49CCF3752D356926 CRC64;
     MFQNNPLLAQ LKQQIEANKE YVEGKVKASD KNFGFLEADK KSYFIPPLEM KKVMHGDNVK
     AVIKREGDKE SVEIDSLIDP MLDRFIARVR FNKDGKLQLA VDHPQIRLNI PATTHKKVTE
     QLANDDWVVA QLKSHPLRDD RFFFAQVTEF ICKADDHFAP WWVTLARHQQ PRESVKTEQS
     YTLQDQSPRE DLSHLYFTTI DSPSTQDMDD ALFIEPITEN AIQQGWRLVV AIADPTAYIA
     EDSNIEHAAR QRCFTNYLPG FNIPMLPREL SDDLCSLVPN KKRPALVVYI ETDLNGNLIK
     DASFHTAWVE SKAKLAYDNV SDYLEGVEQA WQPDCAELKQ QIYWLHQFTQ ARIQWRSKNA
     LLFKEQMDYN FELNADGSVK SIQIQYHRIA NQIIEEAMII ANICCAQFLA KHAKTGIFNS
     HAGFDPKNYE AVQTFLLNTL ATDENRSELT DLFSPTQLAT LDGYCAMRRY IEDFPEKFLE
     LRLRRYLTFA EFKAEVAPHF GLGISHYATW TSPIRKYGDI VNHRLIKQVL LNQPIKHIES
     TILARLQEAR RQNRLVERDI ADWLYARYLL PIATQGVEFD CEITDISRGG IRAKVLENGA
     QIFIPCSTLH ENKDEIDFIP EEIALYTKGE KIYQIGQATR VKLTDVRLET RSVLGNIIK