RNB_BUCBP
ID RNB_BUCBP Reviewed; 646 AA.
AC Q89AM0;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Exoribonuclease 2;
DE EC=3.1.13.1;
DE AltName: Full=Exoribonuclease II;
DE Short=RNase II;
DE Short=Ribonuclease II;
GN Name=rnb; OrderedLocusNames=bbp_247;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
CC -!- FUNCTION: Involved in mRNA degradation. Hydrolyzes single-stranded
CC polyribonucleotides processively in the 3' to 5' direction (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.13.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase II subfamily.
CC {ECO:0000305}.
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DR EMBL; AE016826; AAO26974.1; -; Genomic_DNA.
DR RefSeq; WP_011091375.1; NC_004545.1.
DR AlphaFoldDB; Q89AM0; -.
DR SMR; Q89AM0; -.
DR STRING; 224915.bbp_247; -.
DR PRIDE; Q89AM0; -.
DR EnsemblBacteria; AAO26974; AAO26974; bbp_247.
DR GeneID; 56470789; -.
DR KEGG; bab:bbp_247; -.
DR eggNOG; COG4776; Bacteria.
DR HOGENOM; CLU_002333_7_3_6; -.
DR OMA; CFTNYLP; -.
DR OrthoDB; 1602988at2; -.
DR Proteomes; UP000000601; 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.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome;
KW RNA-binding.
FT CHAIN 1..646
FT /note="Exoribonuclease 2"
FT /id="PRO_0000166379"
FT DOMAIN 564..646
FT /note="S1 motif"
SQ SEQUENCE 646 AA; 74771 MW; 925279FCC3700AEC CRC64;
MLRNHPLLSK LKRKLNSNIP RVEGIVKSTE KGFGFLEIDS KTSYFIPFKN MKKVMHGDRI
TALLKIDNSR EIAEPEKLIE PFLTRFIGTI QVNKSIISII PDHPFFKEKI VCSVSCILPK
CVKTGDWAVA VLMQHKLIQG HYKFLAKLVK YIIKKDDVLV PWLVTLSRYQ LESDCFKLNS
SSIIFDNSLK REDLTHLDFI TIDNSSTKDI DDALYVEKQS LGAFNLIVAI SDPTSYIPFG
SSLDNFALKR SFTNYLPGFT IPMLPSELSE NKCSLKVNKS RPVIACKIRI DSDGCILHNY
SYFFLAWIKS KATLVYECVS DWLEHKGKWV PECSNIANQL FMLNSIYNIR RNWRKNYAVL
FKEHPEYNFK LSSNFQVLNV FMEMRRTAHK IVEEAMIAAN ICAAKVLSEK LGFGIYNVHI
GFDASNSENV VRLLSKYGFN FCKDEIRTLK GFCKLRRILN KHSYKYLDNR IKKYQSFGEL
QFFPGPHFAL GLDAYATWTS PIRKYSDMVN HRLLKSIITH THVIKPSCDI LLKINDRRKR
LKMAERDLED WLYSKFFSSI EYTKNSFNAE IIDVFRSGIR VRSLKNGANI FIPSSFLHNI
RNELLCHQDQ GIVYINDKKM YSVSDIIQVK LINIRTQTRN LIGKPV
