RNB_BUCCC
ID RNB_BUCCC Reviewed; 648 AA.
AC Q057Q9;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=BCc_168;
OS Buchnera aphidicola subsp. Cinara cedri (strain Cc).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=372461;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cc;
RX PubMed=17038625; DOI=10.1126/science.1130441;
RA Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M., Michelena J.M.,
RA Silva F.J., Moya A., Latorre A.;
RT "A small microbial genome: the end of a long symbiotic relationship?";
RL Science 314:312-313(2006).
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; CP000263; ABJ90640.1; -; Genomic_DNA.
DR RefSeq; WP_011672559.1; NC_008513.1.
DR AlphaFoldDB; Q057Q9; -.
DR SMR; Q057Q9; -.
DR STRING; 372461.BCc_168; -.
DR EnsemblBacteria; ABJ90640; ABJ90640; BCc_168.
DR KEGG; bcc:BCc_168; -.
DR eggNOG; COG4776; Bacteria.
DR HOGENOM; CLU_002333_7_3_6; -.
DR OMA; CFTNYLP; -.
DR OrthoDB; 1602988at2; -.
DR Proteomes; UP000000669; 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 Pfam; PF08206; OB_RNB; 1.
DR Pfam; PF00773; RNB; 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; Reference proteome;
KW RNA-binding.
FT CHAIN 1..648
FT /note="Exoribonuclease 2"
FT /id="PRO_0000409534"
FT DOMAIN 565..647
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ SEQUENCE 648 AA; 76184 MW; C8DA3A4CA0357B64 CRC64;
MFYNNPLLIK LKNKLYKKKK IEGIVKSTTK GFGFLEVDSK KTYFIPSKNM KKVIHGDRII
GLIKLENNKE IVYPKILIEP FLKKFIGSIL KKNNIIYIQA NYPYIKDLIF YRYKTSVFRS
WKNGDWVIAE LDTHSLRDNN HFSINILKFI SEKNDPLTPW NVILSKYNLE KKSPKINFNY
ILNNNNLKDK RIDLTYLDFI TIDNSNTQDI DDALFVKKTK KNKLTLIVAI ADPTEYILIN
TKVDDIAKKR VFTNYLPGFN ISMLPKEFSE DLCSLKPHVK RPVLACKIII DNEGKILMKK
TKFFLAWIES KGKLSYQNVS NWLEKLGNWQ PDNKKIKKQI LLLYKMYKIR NMWRKKNALI
FPDNIEYKFH LSKTWEILNI SVEKRSIAHK IVEESMISAN ICAASFLKKK LGFGLYNSHS
GFDTFNAKNA INFLKKYNII FTLEEIMTLS GFCKLKRKLN KLSNKYINYR IQKFQSFGEI
SLIPKPHFSL GLPYYATWTS PIRKYSDMIN HRLIKSIIIG KKKISPPDTN IIPQIIHRKY
KIRMALKEIE EWLYFKYYNK KKSDKKKYQA NIIDISKGGI KARLLKTGAY IFIPVTYIHK
IRHELNLNSE KGIIYIKNKI YYKVSDIIIV SLLKINNGNK KIIATMIN