ID   RNB_HAEIG               Reviewed;         659 AA.
AC   A5UFG3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
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};
GN   OrderedLocusNames=CGSHiGG_02405;
OS   Haemophilus influenzae (strain PittGG).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittGG;
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
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; CP000672; ABQ99518.1; -; Genomic_DNA.
DR   RefSeq; WP_012054750.1; NC_009567.1.
DR   AlphaFoldDB; A5UFG3; -.
DR   SMR; A5UFG3; -.
DR   EnsemblBacteria; ABQ99518; ABQ99518; CGSHiGG_02405.
DR   KEGG; hiq:CGSHiGG_02405; -.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
DR   Proteomes; UP000001990; 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; 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; RNA-binding.
FT   CHAIN           1..659
FT                   /note="Exoribonuclease 2"
FT                   /id="PRO_1000063892"
FT   DOMAIN          576..658
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   659 AA;  75830 MW;  E867EF45CB8D4D43 CRC64;
     MFQDNPLLAQ LKQQIHDSKE QVEGVVKSTD KAYGFLECDK KTYFIAPPSM KKVMHGDKIK
     ATIEKQGDKE QAEPESLIEP MLTRFIAKVR FNKDKKLQVL VDHPNINQPI GAQQAKSVKE
     ELQEGDWVVA NLKTHPLRDD RFFYATINQF ICRAEDELAP WWVTLARHEQ SRYPVRGAEP
     YEMLDQKTRE NLTALHFVTI DSESTMDMDD ALYIEPIAQN STQTGWKLVV AIADPTAYIA
     LDSQIEQEAK QRCFTNYLPG FNIPMLPREL SDELCSLIAN ETRPALVCYI ETDLAGNITA
     KPNFVSAYVQ SKAKLAYNKV SDYLEQADNA WQPEMPEIAQ QIHWLHQFTK ARIQWRKTHS
     LFFKEKPDYT 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 DELALYIKGD RTYKIGDIVK VKLTEVKEAT RSIVGEILQ