RNB_BUCA5
ID RNB_BUCA5 Reviewed; 649 AA.
AC B8D959;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=BUAP5A_261;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=563178;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5A;
RX PubMed=19150844; DOI=10.1126/science.1167140;
RA Moran N.A., McLaughlin H.J., Sorek R.;
RT "The dynamics and time scale of ongoing genomic erosion in symbiotic
RT bacteria.";
RL Science 323:379-382(2009).
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; CP001161; ACL30630.1; -; Genomic_DNA.
DR RefSeq; WP_009874220.1; NC_011833.1.
DR AlphaFoldDB; B8D959; -.
DR SMR; B8D959; -.
DR KEGG; bap:BUAP5A_261; -.
DR HOGENOM; CLU_002333_7_3_6; -.
DR OMA; CFTNYLP; -.
DR OrthoDB; 1602988at2; -.
DR Proteomes; UP000006904; 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; RNA-binding.
FT CHAIN 1..649
FT /note="Exoribonuclease 2"
FT /id="PRO_1000149454"
FT DOMAIN 562..644
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ SEQUENCE 649 AA; 75132 MW; B1F28EC2ECCF97DF CRC64;
MFQNNPLLTQ LKKNLHAKSP RVEGIVKSTE RGFGFLEVDP QKSYFIPPKN MKNVMHGDKI
IALLTTEKDR EIVEPEKLIE PFLNRFVGKI EKKDNRLFIV PDYPFLKDLI TCQPNKNCIN
IFQNGDWAVA QLKKHKLKGD HLFYAELTEK ITQEDDPLIP WWVTLARHDL DRKEPLAEED
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
MAERDVSDWL YTIFLQKKKY QNQKFNAEIT DISRSGIRAR LIENGANVFI PGTLIHPIRE
ELNFNQESGK VFINGIMHYK ISDLIQVTLS DIRLKTRSII AKPVFEKFK