ID   RNB_PASMU               Reviewed;         658 AA.
AC   Q9CP74;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=PM0181;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK02265.1; -; Genomic_DNA.
DR   RefSeq; WP_005723421.1; NC_002663.1.
DR   AlphaFoldDB; Q9CP74; -.
DR   SMR; Q9CP74; -.
DR   STRING; 747.DR93_1885; -.
DR   EnsemblBacteria; AAK02265; AAK02265; PM0181.
DR   KEGG; pmu:PM0181; -.
DR   PATRIC; fig|272843.6.peg.186; -.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
DR   Proteomes; UP000000809; 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; 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   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; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..658
FT                   /note="Exoribonuclease 2"
FT                   /id="PRO_0000166385"
FT   DOMAIN          576..658
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   658 AA;  75588 MW;  F9E57D32EAD26EDF CRC64;
     MFQNNPLLSQ LKQQIRDSKQ QVEGIVKGSD KAFGFLECDK KSYFIPPAAM KKVMHGDKIK
     ALIEVVGEKE QAEPDALIEP MLTRFIARVR FNKDKKLQVL VDHPQINQAI GAAQDKSITE
     TLQEGDWVVA TLKTHPLRDD RFFFAQIQQF ICRAEDELAP WWVTLARHGQ SRYPVQGCAD
     YPMIDQHTRE DLTALHFITI DAETTLDMDD ALYLEPIHQA EEQIGWRLVV AVADPTAYIP
     LDSQIEQEAR QRCFTNYLPG FNIPMLPPEL SDERCSLMQD EIRPALVCYI ETDLTGNITE
     KPRFVSAYVQ SKAKLAYDHV SDYLENCLDA WQPENPQIAQ QIQWLHQFTQ ARIEWRKQHA
     LLFKEKPDYS FILAENGSVQ AIQAQYRRIA NQMVEECMIL ANICAAHYLD EHAKCGIFNT
     HSGFDKKYLE SAHQFLLNQL SDETNQAVLA TRYSVANLTT LAGYCQMRHD IELLNSDYLE
     LRLRRFLTFA EFKSEIAPHF GLGLSGYATW TSPIRKYSDM VNHRLIKAVL TQQTCEKPQD
     DLFVRLQEAR RQNRLVERDI ADWLYCRYLA TQVEQKPTFQ AEIQDVMRGG LRVQLLANGA
     PMFIPASLIH DNKEAIQVNT DTLTLSIQGE VKYKLGDIIQ VQLLDVKEET RSIVGTLC