ID   RNB_SALAR               Reviewed;         644 AA.
AC   A9MQ20;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 82.
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=SARI_01262;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) 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; CP000880; ABX21164.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9MQ20; -.
DR   SMR; A9MQ20; -.
DR   STRING; 41514.SARI_01262; -.
DR   KEGG; ses:SARI_01262; -.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   Proteomes; UP000002084; 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; 2.40.50.640; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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   NCBIfam; TIGR00358; 3_prime_RNase; 1.
DR   NCBIfam; TIGR02062; RNase_B; 1.
DR   PANTHER; PTHR23355:SF37; EXORIBONUCLEASE 2; 1.
DR   PANTHER; PTHR23355; RIBONUCLEASE; 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   SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
DR   PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..644
FT                   /note="Exoribonuclease 2"
FT                   /id="PRO_1000084280"
FT   DOMAIN          561..643
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   644 AA;  72393 MW;  2AC5AA112A1301EA CRC64;
     MFQDNPLLAQ LKQQLHSQTP RAEGVVKATE KGFGFLEVDA QKSYFIPPPQ MKKVMHGDRI
     VAVIHTEKER ESAEPEALIE PFLTRFVGKI QGKNDRLTIV PDHPMLKDAI PCRAARGVQH
     EFKEGDWAVA EMRRHPLKGD RSFYADLTQY ITFADDHFAP WWVTLARHNL EKEAPNGVAT
     EMLDEGLERQ DLTALNFVTI DSASTEDMDD ALYAEELADG RLQLTVAIAD PTAWIAEGSK
     LDNAAKIRAF TNYLPGFNIP MLPRELSDDL CSLRANEVRP TLTCRMIIAA DGSIDDDIAF
     FAATIESKAK LAYDNVSDWL ENSGTWQPDN EGIAQQIRLL HRICLSRGEW RHHHALVFKD
     RPDYRFVLGE KGEVLDIVAE PRRIANRIVE ESMIAANLCA ARVLRDKLGF GIYNVHTGFD
     PANADALAAL LKTHGLHVDA EEVLTLEGFC KLRRELDAQP SGFLDSRIRR FQSFAEISTE
     PGPHFGLGLE AYATWTSPIR KYGDMINHRL LKAVIKGETI ARPREDITQQ MAERRRLNRM
     AERDVGDWLY ARFLNDKAGT DTRFAAEIID VSRGGMRVRL VDNGAVAFIP ASFLHAVRDE
     LVCSQENGTI QIKGETVYKV TDVIDVTIAE VRMDTRSIIA RPAA
//