ID   RNB_HAEIN               Reviewed;         659 AA.
AC   P44440;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 131.
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=HI_1733;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC23378.1; -; Genomic_DNA.
DR   PIR; A64139; A64139.
DR   RefSeq; NP_439875.1; NC_000907.1.
DR   RefSeq; WP_005694220.1; NC_000907.1.
DR   AlphaFoldDB; P44440; -.
DR   SMR; P44440; -.
DR   STRING; 71421.HI_1733; -.
DR   EnsemblBacteria; AAC23378; AAC23378; HI_1733.
DR   KEGG; hin:HI_1733; -.
DR   PATRIC; fig|71421.8.peg.1814; -.
DR   eggNOG; COG4776; Bacteria.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
DR   PhylomeDB; P44440; -.
DR   BioCyc; HINF71421:G1GJ1-1749-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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..659
FT                   /note="Exoribonuclease 2"
FT                   /id="PRO_0000166384"
FT   DOMAIN          576..658
FT                   /note="S1 motif"
SQ   SEQUENCE   659 AA;  75782 MW;  FDADA9097A7D3B66 CRC64;
     MFQDNPLLAQ LKQQIHDSKE QVEGVVKSTD KAYGFLECDK KTYFIAPPSM KKVMHGDKIK
     ATIEKQGDKE QAEPEALIEP MLTRFIAKVR FNKDKKLQVL VDHPSINQPI GAQQAKSVKE
     ELQEGDWVVA NLKTHPLRDD RFFYATINQL ICRADDELAP WWVTLARHEQ SRYPVRGAEP
     YEMLDQKTRE NLTALHFVTI DSESTMDMDD ALYIEPIAQN STQTGWKLVV AIADPTAYIA
     LDSQIEQEAK QRCFTNYLPG FNIPMLPREL SDELCSLIAN ETRPALVCYI ETDLTGNITA
     KPHFVSAYVQ SKAKLAYNKV SDYLEQADNA WQPEMPETAQ QIHWLHQFTK ARIQWRKTHS
     LFFKEKPDYA FVLAENGKVQ EIKAEYRRIA NQIVEEAMII ANICAAQFLH EQAKTGIFNT
     HSGFDKKFLE NAHNFLMANL ANEQNQTELA ERYSVENLAT LNGYCQMRHD IEPIESDYLE
     LRLRRYLTFA EFKSELAPHF GLGLEGYATW TSPIRKYSDM VNHRLIKAVL AKQPYEKPQN
     DVLARLQEAR RQNRLVERDI ADWLYCRYLA DKVASNAEFE AEVQDVMRAG LRVQLLENGA
     SLFIPAATLH NNKEEIQLNP DELALYIKGE RTYKIGDMVK VKLTEVKEAT RSIVGEILQ