RNB_SODGM
ID RNB_SODGM Reviewed; 644 AA.
AC Q2NST6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=SG1514;
OS Sodalis glossinidius (strain morsitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=343509;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=morsitans;
RX PubMed=16365377; DOI=10.1101/gr.4106106;
RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA Aksoy S.;
RT "Massive genome erosion and functional adaptations provide insights into
RT the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL Genome Res. 16:149-156(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; AP008232; BAE74789.1; -; Genomic_DNA.
DR RefSeq; WP_011411334.1; NC_007712.1.
DR AlphaFoldDB; Q2NST6; -.
DR SMR; Q2NST6; -.
DR STRING; 343509.SG1514; -.
DR EnsemblBacteria; BAE74789; BAE74789; SG1514.
DR KEGG; sgl:SG1514; -.
DR eggNOG; COG4776; Bacteria.
DR HOGENOM; CLU_002333_7_3_6; -.
DR OMA; CFTNYLP; -.
DR OrthoDB; 1602988at2; -.
DR BioCyc; SGLO343509:SGP1_RS13470-MON; -.
DR Proteomes; UP000001932; 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; IPR040476; CSD2.
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; PF17876; CSD2; 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; 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..644
FT /note="Exoribonuclease 2"
FT /id="PRO_1000063902"
FT DOMAIN 562..644
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ SEQUENCE 644 AA; 72631 MW; D8B2751D81B856E3 CRC64;
MFQDNPLLAQ LKQQLHSQTP RVEGVVKGTE KGFGFLEVDA QKSYFISPPF MKKVMHGDKI
SAVVRTEKER EIAEPEELIE PFLTRFIGRV QVKDERLAVV PDHPLIKEVI PTRPQHGVDQ
MFQTGDWAVA EMRRHPLKGD RQFYAEITAL VTRADDHFAP WWVTLARHNL ERAAPTMPEG
VSLQEDGPAR EDLTALDFIT IDSASTEDMD DAIHLAPAPN GAWVMTVAIA DPTAWVPAGS
PLDNIARERA FTNYLPGFNI PMLPRALSDD LCSLRAHERR PALACRVTVR PNGTLADDAR
FFTAWIESKG KLAYDNVSDW LENLGSWQPE TEAIADQIRL LHDVCLARSA WRQRHALVFK
DRPDYRFVLN EKGNVDDIVV EPRRIANRMI EEAMITANVC AARVLRDGLG YGLYNVHHGF
DPLLVDQAVA ILHSHQIEVD PADLLTLEGF CALRRRLDAQ PTSYLDSRIR RFQTFAEVST
VPGPHFGLGL DAYATWTSPI RKYGDMINHR LLKALIGVGD AERPNEEVTL RLAERRRQNR
MAERDVGDWL YARFLQPKAG SDSRFAAEII DISRGGMRVR LLNNGAVAFI PAPFIHSVRD
ELVCSQDTGT VQVKGEERYR QGDTLDVTLA EVRMENRSVI ARPV