ID Q1LSR0_BAUCH Unreviewed; 749 AA.
AC Q1LSR0;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 19-FEB-2014, entry version 60.
DE RecName: Full=Ribonuclease R;
DE Short=RNase R;
DE EC=3.1.13.1;
GN Name=rnr; OrderedLocusNames=BCI_0576;
OS Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX NCBI_TaxID=374463;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA Moran N.A., Eisen J.A.;
RT "Metabolic complementarity and genomics of the dual bacterial
RT symbiosis of sharpshooters.";
RL PLoS Biol. 4:1079-1092(2006).
CC -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside
CC monophosphates and is involved in maturation of structured RNAs
CC (By similarity).
CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'-
CC direction to yield nucleoside 5'-phosphates.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R
CC subfamily.
CC -!- SIMILARITY: Contains 1 S1 motif domain.
CC -!- SIMILARITY: Contains S1 motif domain.
CC -!- SIMILARITY: Contains Smotif domain.
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DR EMBL; CP000238; ABF13946.1; -; Genomic_DNA.
DR RefSeq; YP_589004.1; NC_007984.1.
DR ProteinModelPortal; Q1LSR0; -.
DR STRING; 374463.BCI_0576; -.
DR EnsemblBacteria; ABF13946; ABF13946; BCI_0576.
DR GeneID; 4056692; -.
DR KEGG; bci:BCI_0576; -.
DR PATRIC; 21074659; VBIBauCic75062_0546.
DR eggNOG; COG0557; -.
DR HOGENOM; HOG000071120; -.
DR KO; K12573; -.
DR OMA; GFFVRLN; -.
DR OrthoDB; EOG6Q5NRD; -.
DR BioCyc; BCIC374463:GI6Q-576-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP.
DR GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IEA:GOC.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR011129; Cold_shock_prot.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR003029; Rbsml_prot_S1_RNA-bd_dom.
DR InterPro; IPR022967; RNA-binding_domain_S1.
DR InterPro; IPR013223; RNase_B_OB_dom.
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 Pfam; PF08461; HTH_12; 1.
DR Pfam; PF08206; OB_RNB; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00357; CSP; 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 Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Nuclease;
KW RNA-binding.
FT DOMAIN 646 727 S1 motif (By similarity).
SQ SEQUENCE 749 AA; 85697 MW; AC78E0B7C150FD0F CRC64;
MSKNPFLAHN TEKYKCPIPS RELILIHLAK REVPISSKDL ALELNVCGAE QLDGLRRRLR
AMKRDGQLTF THRQYSILPT DNNLLRGTVI GHRDGFGFLR VSGRKEDLYL SVEQMKIVIH
GDIVIAALSQ GEHYNKGRRE ARIIRVLIPK NQPIVGKFYV DTNRAFVVPD DSRLSFKIII
PPADRNNADV GCLVVVQLIQ RPNRNIKAIG KIVEVLGDHI NTSMVVDIAL RSYALPYIWP
PEVEEQAATF TKEVPEVVKR SRVDLRMLPL VTIDGEEARD FDDAVYCEKK SSGWRLWVAI
ADVSYYVRPH TPLDNEARNR ATSIYFPSQV IPMLPEILSH SLCSLNPQVD RLCMVCEMTI
SAQGKLSSYK FYEAIINSKA RLTYNNVWQI LQGNQQLCTY YAQLVQPLNN LHTMSLKLEQ
ARIQRGGISF DTEETQFIFN AEQRIERIEL VVRNEAHKLI EECMILANIA AARFIEKNKE
PALYRVHDRP SNDNITLLRA ILGKRGLNLG GGDQPQPKDY AEIMSVVSRR TDYEMLRTML
LRSMKQAIYD PENRGHFGLA LQAYTHFTSP IRRYSDLVLH RAIKYLLGRQ NGKANGRSTP
SGGWHSELKE MLQIGQHCSM NERRADEATR NVTDWLKCDF MQEHVGEVFY GTIANITCFG
FFVRINGLFI DGLVHISSLE NDYYRYDNVN QLLIGESGGK IYRIGDTVGI RVEAIHMSDR
KINFSLISTR QYHHKNNHQI SSNKLFVRS
//
