ID RNB_SHIB3 Reviewed; 644 AA.
AC B2U0I4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
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};
GN OrderedLocusNames=SbBS512_E1520;
OS Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=344609;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 3083-94 / BS512;
RA Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA Jiang L., Ravel J., Sebastian Y.;
RT "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL Submitted (MAY-2008) 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; CP001063; ACD09829.1; -; Genomic_DNA.
DR RefSeq; WP_000484972.1; NC_010658.1.
DR AlphaFoldDB; B2U0I4; -.
DR SMR; B2U0I4; -.
DR STRING; 344609.SbBS512_E1520; -.
DR KEGG; sbc:SbBS512_E1520; -.
DR HOGENOM; CLU_002333_7_3_6; -.
DR Proteomes; UP000001030; 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_1000135881"
FT DOMAIN 561..643
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ SEQUENCE 644 AA; 72493 MW; 47677A651A2D2FE6 CRC64;
MFQDNPLLAQ LKQQLHSQTP RAEGVVKATE KGFGFLEVDA QKSYFIPPPQ MKKVMHGDRI
IAVIHSEKER ESAEPEELVE PFLTRFVGKV QGKNDRLAIV PDHPLLKDAI PCRAARGLNH
EFKEGDWAVA EMRRHPLKGD RSFYAELTQY ITFGDDHFVP WWVTLARHNL EKEAPDGVAT
EMLDEGLVRE DLTALDFVTI DSASTEDMDD ALFAKALPDD KLQLIVAIAD PTAWIAEGSK
LDKAAKIRAF TNYLPGFNIP MLPRELSDDL CSLRANEVRP VLACRMTLSA DGAIEDNIEF
FAATIESKAK LVYDQVSDWL ENTGDWQPES EAIAEQVRLL AQICQRRGEW RHNHALVFKD
RPDYRFILGE KGEVLDIVAE PRRIANRIVE EAMIAANICA ARVLRDKLGF GIYNVHMGFD
PANADALAAL LKTHGLHVDA EEVLTLDGFC KLRRELDAQP TGFLDSRIRR FQSFAEISTE
PGPHFGLGLE AYATWTSPIR KYGDMINHRL LKAVIKGETA TRPQDEITVQ MAERRRLNRM
AERDVGDWLY ARFLKDKAGT DTRFAAEIVD ISRGGMRVRL VDNGAIAFIP APFLHAMRDE
LVCSQENGTV QIKGETVYKV TDVIDVTIAE VRMETRSIIA RPVA
//
