ID   RNB_PECCP               Reviewed;         644 AA.
AC   C6DK05;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=PC1_2357;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) 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; CP001657; ACT13388.1; -; Genomic_DNA.
DR   RefSeq; WP_015840571.1; NC_012917.1.
DR   AlphaFoldDB; C6DK05; -.
DR   SMR; C6DK05; -.
DR   STRING; 561230.PC1_2357; -.
DR   EnsemblBacteria; ACT13388; ACT13388; PC1_2357.
DR   KEGG; pct:PC1_2357; -.
DR   eggNOG; COG4776; Bacteria.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
DR   OrthoDB; 1602988at2; -.
DR   Proteomes; UP000002736; 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; IPR040476; CSD2.
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; PF17876; CSD2; 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; 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; RNA-binding.
FT   CHAIN           1..644
FT                   /note="Exoribonuclease 2"
FT                   /id="PRO_1000213379"
FT   DOMAIN          561..643
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   644 AA;  72321 MW;  9151D1621FFEB8B5 CRC64;
     MFQDNPLLAQ LKQQLHSQTP RVEGVVKGTD KGFGFLEADG QKSYFIPPPH MKKVMHGDRI
     TATLHTEKDR EIVEPETLIE PFLTRFVGRI HKKDDRLSIT PDHPLLKDAI PCRAARDVTH
     TFQEGDWAVA EMRRHPLKGD RGFHAELTQY ITTGDDPLVP WWVTLSRHNL ERAAPDVEAT
     ERHDGELVRE DLTALSFVTI DSASTEDMDD ALYVQDNGDG SLQLTIAIAD PTAYVDAGSE
     LDKIARQRAF TNYLPGFNIP MLPRSLSDDI CSLRPDERRP VLACRVTIAA DGALGDDIHF
     FAAWIESKAK LAYDNVSDWL EEQGEWQPQN DAIAEQIRLL HRVCLARSEW RTTHALVFKD
     RPDYRFLLGE KGDVLDIVVE HRRIANRIVE EAMIAANVCA AIVLRDKLGF GIYNVHNGFD
     PVSIDQAVTV LDTHGVQADA QTLLTLEGFC KLRRELDAQP TQFLDSRIRR FQSFAEVSIT
     PGPHFGLGLE AYATWTSPIR KYGDMVNHRL LKAVITGQAA EKPQDDVTVQ LAERRRLNRM
     AERDVGDWLY ARYLSDKAGT DVRFNAEIID VTRGGLRVRL LDNGAVAFIP SSFIHAVRDE
     LVCSQEMGTL AVKGDVVYRQ GDTLDVVIAE VRLETRSVVA KPAA