ID   RNB_ACTP7               Reviewed;         658 AA.
AC   B3GXJ4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=APP7_0801;
OS   Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=537457;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP76;
RA   Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA   Tegetmeyer H., Singh M., Gerlach G.F.;
RT   "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001091; ACE61453.1; -; Genomic_DNA.
DR   RefSeq; WP_005617246.1; NC_010939.1.
DR   AlphaFoldDB; B3GXJ4; -.
DR   SMR; B3GXJ4; -.
DR   EnsemblBacteria; ACE61453; ACE61453; APP7_0801.
DR   KEGG; apa:APP7_0801; -.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
DR   BioCyc; APLE537457:APP7_RS04060-MON; -.
DR   Proteomes; UP000001226; 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; 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; 2.
DR   SUPFAM; SSF50249; SSF50249; 4.
DR   TIGRFAMs; TIGR00358; 3_prime_RNase; 1.
DR   TIGRFAMs; TIGR02062; RNase_B; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Nuclease; RNA-binding.
FT   CHAIN           1..658
FT                   /note="Exoribonuclease 2"
FT                   /id="PRO_1000135859"
FT   DOMAIN          576..658
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   658 AA;  75731 MW;  E23025C3A4969167 CRC64;
     MFQNNPLLAQ LKQQIEANKE YVEGTVKASD KAFGFLECDK KSYFIPPMEM KKVMHGDKVK
     AVVKREDDKE QVEIDSLLEP MLDRFIAQVR FNKDNKLQLI VDHPSIKNII PANTHKKVTE
     TLESGDWVVA QLKTHPLRDD RFLFAQVTQF ICKADDNFAP WWVTLARHEQ PREPVANEKS
     YELHDELDRE DLTSLYFTTI DSPSTQDMDD ALYIEPIKQG EVQTGWRLVV AIADPTAYIP
     ENSNLEKAAR QRCFTNYLPG FNIPMLPREL SDDLCSLVPN EKRPALVGYI ETDLAGNITG
     DTRFVSAWVE SKAKLAYDNV SDYLEQVENA WQPESAETKQ QIDWLHQFTL ARIEWRRNNA
     LLFKESGDYS FELNEDGSVR DIHVEYRRIA NQMIEESMII ANICCAKFLA DNAKTGVFNT
     HAGFDPKNLE LAQKFLLDTL ANDENRDALT ALYAPEKLAT LEGYCEMRRS IDEFPEKFLE
     LRLRRYLTFA EFKSEVAPHL GLGISHYATW TSPIRKYGDM VNHRLIKQVL LGKQAKTVEE
     GILVRLQEAR RQNRLVERDI ADWLYARYLF PMVEQAVEFD CEIADVSRGG VRAKVIANGA
     QIFVPFSTLH DKKEEMEFRP EEIALYIKGE KAYQIGQAVK VKLTEVRLET RSIVGNII