RNR_BUCAP
ID RNR_BUCAP Reviewed; 726 AA.
AC Q8K917;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Ribonuclease R {ECO:0000255|HAMAP-Rule:MF_01895};
DE Short=RNase R {ECO:0000255|HAMAP-Rule:MF_01895};
DE EC=3.1.13.1 {ECO:0000255|HAMAP-Rule:MF_01895};
DE AltName: Full=VacB protein homolog;
GN Name=rnr {ECO:0000255|HAMAP-Rule:MF_01895}; OrderedLocusNames=BUsg_545;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
CC -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside
CC monophosphates and is involved in maturation of structured RNAs.
CC {ECO:0000255|HAMAP-Rule:MF_01895}.
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_01895};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01895}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01895}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01895}.
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DR EMBL; AE013218; AAM68084.1; -; Genomic_DNA.
DR RefSeq; WP_011054050.1; NC_004061.1.
DR AlphaFoldDB; Q8K917; -.
DR SMR; Q8K917; -.
DR STRING; 198804.BUsg_545; -.
DR EnsemblBacteria; AAM68084; AAM68084; BUsg_545.
DR KEGG; bas:BUsg_545; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_0_6; -.
DR OMA; DWYEYRS; -.
DR OrthoDB; 1602988at2; -.
DR Proteomes; UP000000416; 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-UniRule.
DR Gene3D; 2.40.50.140; -; 2.
DR HAMAP; MF_01895; RNase_R; 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; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR004476; RNase_II/RNase_R.
DR InterPro; IPR011805; RNase_R.
DR InterPro; IPR013668; RNase_R_HTH_12.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR Pfam; PF17876; CSD2; 1.
DR Pfam; PF08461; HTH_12; 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 SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 4.
DR TIGRFAMs; TIGR00358; 3_prime_RNase; 1.
DR TIGRFAMs; TIGR02063; RNase_R; 1.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease; RNA-binding.
FT CHAIN 1..726
FT /note="Ribonuclease R"
FT /id="PRO_0000166398"
FT DOMAIN 642..723
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01895"
SQ SEQUENCE 726 AA; 84328 MW; B7C374ECBD7A5416 CRC64;
MVVDSYQKKE TKKYRNFIPR REQILFLLKT DKDLISQKKL EKKFSINSQE QKKALRRRLR
AMERDGQIIY TRNRCYITPE NLKIVTGKVI GHRDGYGFLR TETFKDDLWL SIEQMKLCIH
GDVILAHIVK SDRKGRNSAK VLKILRPNDV LIVGRYCVDN KKKFVIPNDT RFNFKIFILD
SLISNENISI GTIVVVKLRE NATKKSKIQG TIVEVLGKEM GTNLAIKIAL RTHCIPYLWS
KEVEYQLCGI KSKINEKDFK NRIDLRHLPF FTIDEEDARD FDDAIFCKKK TNGEKGWKLW
VAISDVSYYI QPDTALDKAA SKRGTSIYFP SLVIPMLPEK ISIDVCSLNP NAERLSLICE
MNLSNKGELI TYKHYEAVIC SHGRFTYNEI FKIWNGDIEL CFKYKKLLKY IQNLSSLQKI
LKKYNVSKRG IYFENIEAKF ILDSNYRIKN ISQNIRNDAH KFIESCMILA NIASAEFVKK
HKSPVLFRNH DRPDKDSIIN FRSVLKKLGL SLLGGEIPES TDYSELLKKI STRPDYEMIQ
TILLRSMKQA VYSPDNRGHF GLSLSSYVHF TSPIRRYPDL LVHRVIKNLL LKEKNLSKYH
LYNLNEVTKI GLHCSMTERR ADEATRDVLD WLKCDFMQKK IGDVLTGVIS NVTSFGFFVR
LNQFFIDGLV HIATLIDDYY YFDSIGLKLI GKSSKNTYCL GDTLKVKVIS VNLNERKIEL
SLYMSR