RNB_BUCAI
ID RNB_BUCAI Reviewed; 649 AA.
AC P57354;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=BU266;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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; BA000003; BAB12976.1; -; Genomic_DNA.
DR RefSeq; NP_240090.1; NC_002528.1.
DR RefSeq; WP_010896034.1; NC_002528.1.
DR AlphaFoldDB; P57354; -.
DR SMR; P57354; -.
DR STRING; 107806.10038941; -.
DR EnsemblBacteria; BAB12976; BAB12976; BAB12976.
DR KEGG; buc:BU266; -.
DR PATRIC; fig|107806.10.peg.276; -.
DR eggNOG; COG4776; Bacteria.
DR HOGENOM; CLU_002333_7_3_6; -.
DR OMA; CFTNYLP; -.
DR Proteomes; UP000001806; 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..649
FT /note="Exoribonuclease 2"
FT /id="PRO_0000166377"
FT DOMAIN 562..644
FT /note="S1 motif"
SQ SEQUENCE 649 AA; 75144 MW; 71E89E72EFEEBE1A CRC64;
MFQNNPLLTQ LKKNLHAKSP RVEGIVKSTE RGFGFLEVDP QKSYFIPPKN MKNVMHGDKI
IALLTTEKDR EIVEPEKLIE PFLNRFVGKI EKKDNRLFIV PDYPFLKDLI TCQPNKNCIN
IFQNGDWAVA QLKKHKLKGD HLFYAELTEK ITQEDDPLIP WWVTLARHDL DRKEPLAEDD
DLILKESDNR KDLTDLDFIT IDNTNTKDID DALFVSEKNN GDISLIVAIA DPTAYIKHGS
KLDVIASKRI FTNYLPGFNI PMLPRNLSED ICSLNPNKRR PVLACHITVL KNGNISNKIE
FFLAWIKSKS KLSYDHVSDW IEKIGSWIPP TKSIANQILI LHRLCLLRIK WRKKNAVLFK
DSIEYRFHVS EHGKIIDVLI EKRRIAHKII EESMIVANIS AANFLSKNIG FGIYNVHSGF
DLVNAENAVS FLRSYNLNFT VKEITTLKGF CNLRRVLNII SNNYIDSRIR RFQSFGDFST
IPGPHFALGF SEYATWTSPI RKYSDMINHR LLKSIIKKEK SIKPGEDIKI KISEQRRRNR
MAERDVLDWL YTIFLQKKKY QNQKFNAEIT DISRSGIRAR LIENGANVFI PGTLIHPIRE
ELNFNQESGK VFINGIMHYK ISDLIQVTLS DIRLKTRSII AKPVFEKFK
