ID C9P233_VIBME Unreviewed; 815 AA.
AC C9P233;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 03-APR-2013, entry version 27.
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), National Microbial Pathogen
RG 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.
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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:HAMAP.
DR GO; GO:0003723; F:RNA binding; IEA:HAMAP.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR GO; GO:0016070; P:RNA metabolic process; IEA: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; 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 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; Nucleic_acid_OB; 1.
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
//
