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Database: UniProt
Entry: B8KNN0_9GAMM
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ID   B8KNN0_9GAMM            Unreviewed;       830 AA.
AC   B8KNN0;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   16-APR-2014, entry version 35.
DE   RecName: Full=Ribonuclease R;
DE            Short=RNase R;
DE            EC=3.1.13.1;
GN   Name=rnr; ORFNames=NOR53_84;
OS   gamma proteobacterium NOR5-3.
OC   Bacteria; Proteobacteria; Gammaproteobacteria.
OX   NCBI_TaxID=566466;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOR5-3;
RA   Amann R., Fuchs B., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (SEP-2008) 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; DS999408; EED30714.1; -; Genomic_DNA.
DR   EnsemblBacteria; EED30714; EED30714; NOR53_84.
DR   PATRIC; 36996709; VBIGamPro33483_3162.
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; 2.
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      660    741       S1 motif (By similarity).
SQ   SEQUENCE   830 AA;  91835 MW;  753B3F0E99C85D82 CRC64;
     MSKQRKPRNK PSDPHAGREA EKYDHPIASR EAIMDLLRDA DGPLNQDRIA KSLQLAEDRD
     LEALRRRLRA MQRDGQLHVD RKGAYGLVEA LNLLRCRVQG HRDGYGFAQP ETGEDDLYLS
     AREMRRLFDG DTVLVAVTGV DGRGRSEGKV VEVLERGVTK VVGRYQEESG IGVVLPDNSR
     INQEVLIPPK FKGEAKHGQI VTAEITQYPE GRLGAKGRVT EVLGEHLDPG LEIDISIRSH
     GIPFEWPDAV LDEAGALSEE PEEDDKKYRI DLRKKPFVTI DGEDARDFDD AVYCEKRRLG
     GWRLWVAIAD VSHYVGVRSA LDKEAIERGN SVYFPERVVP MLPEVLSNGL CSLKPEVDRL
     ALAVEMEISG SGELKQFRFC EAVIHSHARL TYTQVAEVLE TGASDAVSRK LVPHLEQLHS
     LYKVLRQARE ERGAIDFETV ETRIIFNAER KIDAIVPVQR NDAHKLIEEC MLCANVAAAR
     FFERHELPVL YRVHEGPGEQ KLENLRAFLG ELGLGLRGGL KPTPEDYQLL IEQISTRDDA
     HIVQTMLLRS LSQAVYQAEN LGHFGLNYPG YAHFTSPIRR YPDLLVHRAI RSVIRSRERS
     KLVNRVRGAS DIPKAQIYPY DDAAMAAFGT RCSLTERRAD EATREVQSWL KCEYLREHVG
     TEFEGVVSAV TGFGLFVELK DLYIEGLVHV TSLPGDYYRF DAAQQRLVGE RTGRSFQLGA
     AIKVLVASVN LDERKIDLEP VSLPESRKRK GSGGGGAKGG AKGASKASTK SSRGGESKQQ
     GKASSDSKAR PGGRNRGAGV ARKRSASASA AKGGGQGGSK GGPKRSPKGS
//
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