ID   RNB_GLAP5               Reviewed;         659 AA.
AC   B8F4C5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=HAPS_0516;
OS   Glaesserella parasuis serovar 5 (strain SH0165) (Haemophilus parasuis).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Glaesserella.
OX   NCBI_TaxID=557723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH0165;
RX   PubMed=19074396; DOI=10.1128/jb.01682-08;
RA   Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R.,
RA   Jin M., Jin Q., Chen H.;
RT   "Complete genome sequence of Haemophilus parasuis SH0165.";
RL   J. Bacteriol. 191:1359-1360(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; CP001321; ACL32177.1; -; Genomic_DNA.
DR   RefSeq; WP_012621771.1; NC_011852.1.
DR   AlphaFoldDB; B8F4C5; -.
DR   SMR; B8F4C5; -.
DR   STRING; 557723.HAPS_0516; -.
DR   EnsemblBacteria; ACL32177; ACL32177; HAPS_0516.
DR   KEGG; hap:HAPS_0516; -.
DR   PATRIC; fig|557723.8.peg.522; -.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
DR   Proteomes; UP000006743; 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; IPR004476; RNase_II/RNase_R.
DR   InterPro; IPR022967; S1_dom.
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   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; SSF50249; 3.
DR   TIGRFAMs; TIGR00358; 3_prime_RNase; 1.
DR   TIGRFAMs; TIGR02062; RNase_B; 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_1000149458"
FT   DOMAIN          576..658
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   659 AA;  75735 MW;  273AABA3EE8A0C25 CRC64;
     MFQNNPLLAQ LKQQIEASKE YVEGVVKTSD KSYGFLECEK NSYFIPPAEM KKVMHGDKVK
     AVVKRDGDKE QVEIDSLLEP MLERFIAQVR FNKDGKLQLA VDHPSINNFI PANTQKKVTE
     PLENGDWVVA QLKTHPLRDD RFFFAQVTQF ICKADDNFAP WWVTLARHEQ PREPVANEKS
     YELQDQVERE DLTHLYFTTI DSASTKDMDD ALYVEPISEN GTQTGWRLVV AIADPTAYIP
     EQSAIEKAAR QRCFTNYLPG FNIPMLPREL SDDLCSLVPN EKRPALVGYI ETDLSGNVVG
     EARFVSAWVQ SKARLVYDEV SDYLEKVENH WTPDCAETAQ QIDWLHQFTL ARIDWRSKNA
     LLFKEQGDYS FELAEDGAVK AIHIDYRRIA NQMIEEAMII ANICAAQFLD KYAHTGVFNT
     HSGFDSKNLE PARKFLLDTL ANDENRESLS ERYSPERLST LEGYCEMRRD IEQFPENFLE
     MRLRRYLTFA EFKATSAPHL GLGISHYATW TSPIRKYGDM VNHRLIKQVL SNQTAKPVEE
     TVLARLQEAR KQNRMVERDI ADWLYARYLE PMVEQNVEFD GEIQDVSRGG LRVKVIENGA
     SVFVPFSTLH NNKEEMLFSP EEIALYIKGE KAYQIGQAVK VKLKEVRVET RSVVGDVLI