ID   RNB_MANSM               Reviewed;         659 AA.
AC   Q65SI5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=MS1468;
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E;
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(2004).
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; AE016827; AAU38075.1; -; Genomic_DNA.
DR   RefSeq; WP_011200641.1; NC_006300.1.
DR   AlphaFoldDB; Q65SI5; -.
DR   SMR; Q65SI5; -.
DR   STRING; 221988.MS1468; -.
DR   PRIDE; Q65SI5; -.
DR   EnsemblBacteria; AAU38075; AAU38075; MS1468.
DR   KEGG; msu:MS1468; -.
DR   eggNOG; COG4776; Bacteria.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
DR   OrthoDB; 1602988at2; -.
DR   Proteomes; UP000000607; 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_1000063894"
FT   DOMAIN          577..659
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   659 AA;  75769 MW;  7D2FA765ED465023 CRC64;
     MFQNNPLLSQ LKQQLHDSKP HVEGVVKGTD KAYGFLETEK ETFFIAPPAM KKVMHGDKIK
     AAIETIGDKK QAEPEELIEP MLTRFIAKVR FNKDKKLQVL VDHPNINQPI GAAQAKTVKQ
     ELKEGDWVVA TLKTHPLRDD RFFYAQIAEF ICSAEDEFAP WWVTLARHEQ SRYPVQGQEV
     YSMLDTETRR DLTALHFVTI DSENTQDMDD ALYIEPVTAP NDEQTGWKLA VAIADPTAYI
     ALDSQIEKDA RKRCFTNYLP GFNIPMLPRE LSDELCSLME NETRAALVCR LETDMQGEIV
     GEPEFILAQV QSKAKLAYNN VSDYLEQVEN AWQPENESTQ QQINWLHQFA LVRINWRKKH
     GLLFKEKPDY SFVLADNGHV REIKAEYRRI ANQIVEESMI IANICCAHYL AKNAQTGIFN
     THVGFDKKFL PNAHNFLMAN LSNEENQQEL AERYSVENLA TLAGYCRMRH DIEPIEGDYL
     EFRLRRFLTF AEFKSELAPH FGLGLTGYAT WTSPIRKYSD MVNHRLIKAC LANRECVKPS
     DETLARLQEA RKQNRMVERD IADWLYCRYL ADKVESNPEF RAEVQDCMRG GLRVQLLENG
     ASVFVPASSI HPNKDEIQVN TDELALYING ERRYKIGDIV NIRLTEVKEE TRSLIGNLV