ID   RNB_ACTSZ               Reviewed;         659 AA.
AC   A6VN85;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=Asuc_1066;
OS   Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS   130Z).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=339671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z;
RX   PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA   McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA   Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA   Burkhart K.B., Harkins V., Vieille C.;
RT   "A genomic perspective on the potential of Actinobacillus succinogenes for
RT   industrial succinate production.";
RL   BMC Genomics 11:680-680(2010).
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; CP000746; ABR74432.1; -; Genomic_DNA.
DR   RefSeq; WP_012072809.1; NC_009655.1.
DR   AlphaFoldDB; A6VN85; -.
DR   SMR; A6VN85; -.
DR   STRING; 339671.Asuc_1066; -.
DR   PRIDE; A6VN85; -.
DR   EnsemblBacteria; ABR74432; ABR74432; Asuc_1066.
DR   KEGG; asu:Asuc_1066; -.
DR   eggNOG; COG4776; Bacteria.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
DR   OrthoDB; 1602988at2; -.
DR   Proteomes; UP000001114; 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.
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_1000072974"
FT   DOMAIN          576..658
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   659 AA;  75788 MW;  EF55B18529FD57D5 CRC64;
     MFQNNPLLSQ LKQQLHDSKP HVEGVVKGTD KAYGFLETDK ETFFIAPPAM KKVMHGDKIK
     ATIETIGDKK QADPEELIEP MLTRFIAKVR FNKDKKLQVL ADHPNINQPI GAAQTKAVKE
     ELHEGDWVVA TLKTHPLRDD RFFYAQIVEF ICRAEDEFAP WWVTLARHQQ SRYPVQGQDS
     YKMLDPQTRK DLTALHFVTI DSESTQDMDD ALYIEPLEQN GEQTGWKLTV AIADPTAYIA
     ADSQIEKDAR QRCFTNYLPG FNIPMLPREL SDELCSLMEN ETRAALVCRL QTDLQGELQG
     KPEFLLADVQ SKAKLAYNRV SDYLEQAEGA WQPENETTKQ QIHWLHRFAL TRINWRKTHG
     LLFKEKPDYS FVLADNGHVQ EIKAEYRRIA NQIVEESMIV ANICCAHYLA DNAKTGIFNT
     HAGFDKKFLP NAHHFLMTNL SNAQNQDELT VRYSVENLAT LEGYCRMRHD IEPIDGDYLE
     FRLRRFLTFA EFKSELAPHF GLGLTGYATW TSPIRKYSDM VNHRLIKACI AEQACLKPSD
     DILTRLQEAR KQNRMVERDI ADWLYCRYLA DKVENKPEFQ AEVQDCMRGG LRVQLLENGA
     SVFVPASTIH PNKEEIQVNS DELAFYINGE RRYKIGDIVN IQLTEVKEET RSLIGNLVL