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Entry: C9P233_VIBME
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ID   C9P233_VIBME            Unreviewed;       815 AA.
AC   C9P233;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   16-APR-2014, entry version 31.
DE   RecName: Full=Ribonuclease R;
DE            Short=RNase R;
DE            EC=3.1.13.1;
GN   Name=rnr; ORFNames=VIB_000535;
OS   Vibrio metschnikovii CIP 69.14.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=675813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CIP 69.14;
RG   Los Alamos National Laboratory (LANL);
RG   National Microbial Pathogen Data Resource (NMPDR);
RA   Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA   Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D.,
RA   Vonstein V.;
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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; ACZO01000005; EEX38162.1; -; Genomic_DNA.
DR   EnsemblBacteria; EEX38162; EEX38162; VIB_000535.
DR   PATRIC; 30105351; VBIVibMet139223_0593.
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   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   Cytoplasm; Exonuclease; Hydrolase; Nuclease; RNA-binding.
FT   DOMAIN      652    733       S1 motif (By similarity).
SQ   SEQUENCE   815 AA;  92464 MW;  E9DF5251EFD106CC CRC64;
     MSDTTHTDPF ADREADNYDN PIPSREYILE FLTKANVPMN RNDLFAALEL SGEDHYEGLR
     RRLRAMERDG QLVFTRRQCY ALPEKLEMIK GHVIGHKDGH GWVRPEGGLN KENDILLPHH
     QMRTLIHGDF VLVQPTGTDK RGRKEGRLVR ILEARNAQIV GRFFLEQGYS YVVPDDSRIH
     KDILIPTEHR EGARMGNVVV IEVTDRGTRT RGMMGKVVEV LGESMAPGME TQIAIRTHQI
     PHEWPDEVLK QVSGLKEEVP EEAKQGRVDL RQLPLVTIDG EDARDFDDAV YCEARKEGGW
     RLWVAIADVS YYVRPGSALD KEATNRGNSV YFPSQVVPML PEVLSNGLCS LNPQVDRLCM
     VCEMTISDGG KLIDYQHYEA VMSSHARLTY TKVNDILQGD EELRERYQAV VPHLEQLHNM
     YQVLKTARDQ RGAIEFETVE TKFIFNAQRK IESIEPVIRN DAHKLIEECM ILANIASASL
     VEKAKEAALF RVHEPPGEER LMGFRDFLGE LGLDLSGGLE PSPTDYANLM KQIGERADKE
     LIQTMLLRSM KQAVYNAHNA GHFGLALKRY AHFTSPIRRY PDLLLHRAIK YLIAKEQHQT
     QDRWTPTGGY HYSFEEMDFY GQQCSMTERR ADDATREVSD WLKCEYMQDH VGEELDGVIA
     NVTGFGFFVR LTELHIDGLV HISNLANDYY QFDPIGQRLI GESFGNIYRL GDAVKVKVLS
     VNLDDRQIDF ELVETSRKLR GEGKTAKKRA VEAQAKAKSK KAGTRGGKAV PMVEPTKRPD
     KSESADSAKS KRAKSDKASK AKSRSKTAKS RTKTK
//
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