(data stored in ACNUC7421 zone)

SWISSPROT: Q3KIY0_PSEPF

ID   Q3KIY0_PSEPF            Unreviewed;       876 AA.
AC   Q3KIY0;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 115.
DE   RecName: Full=Ribonuclease R {ECO:0000256|HAMAP-Rule:MF_01895};
DE            Short=RNase R {ECO:0000256|HAMAP-Rule:MF_01895};
DE            EC=3.1.13.1 {ECO:0000256|HAMAP-Rule:MF_01895};
GN   Name=rnr {ECO:0000256|HAMAP-Rule:MF_01895};
GN   OrderedLocusNames=Pfl01_0532 {ECO:0000313|EMBL:ABA72276.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72276.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72276.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72276.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside
CC       monophosphates and is involved in maturation of structured RNAs.
CC       {ECO:0000256|HAMAP-Rule:MF_01895}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to
CC         yield nucleoside 5'-phosphates.; EC=3.1.13.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01895,
CC         ECO:0000256|SAAS:SAAS01124678};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895,
CC       ECO:0000256|SAAS:SAAS00089931}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01895}.
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DR   EMBL; CP000094; ABA72276.1; -; Genomic_DNA.
DR   RefSeq; WP_011332191.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0532; -.
DR   EnsemblBacteria; ABA72276; ABA72276; Pfl01_0532.
DR   KEGG; pfo:Pfl01_0532; -.
DR   eggNOG; ENOG4105C40; Bacteria.
DR   eggNOG; COG0557; LUCA.
DR   HOGENOM; HOG000071120; -.
DR   KO; K12573; -.
DR   OMA; DWYEYRS; -.
DR   BioCyc; PFLU205922:G1G4S-539-MONOMER; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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;
DR   PRODOM; Q3KIY0.
DR   SWISS-2DPAGE; Q3KIY0.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462075};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00089915};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00446781, ECO:0000313|EMBL:ABA72276.1};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462054};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462035}.
FT   DOMAIN      667    748       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   COILED       49     76       {ECO:0000256|SAM:Coils}.
FT   COILED      632    652       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   876 AA;  97689 MW;  BFBA885BF7C6A93F CRC64;
     MADWQSLDPE AAREAEKYEN PIPSRELILQ HLADRGSPAA REQLVEEFGL TTEDQIEALR
     RRLRAMERDA QLIYTRRGTY APVDKLDLIL GRISGHRDGF GFLVPDDGSD DLFMSPAQMR
     LVFDGDRALA RVSGLDRRGR REGVIVEVVS RAHESIVGRY FEEGGIGFVV ADNPKIQQEV
     LVTPGRNANA QIGQFVEVKI THWPTPRFQP QGDVIEVVGN YMAPGMEIDV ALRTYDIPHV
     WPEAVLKEAG KLKPEVEEKD KEKRVDLRHL PFVTIDGEDA RDFDDAVYCE AKPGKLRLFS
     GGWKLYVAIA DVSSYVKIGS ALDNEAQVRG NSVYFPERVV PMLPEQLSNG LCSLNPHVDR
     LAMVCEMTIS KSGEMTDYCF YEAVIHSHAR LTYNKVSAML ETPKATEGRK LRGEYTDVLP
     HLKQLYALYK VLLAARHVRG AIDFETQETR IIFGSERKIA EIRPTTRNDA HKLIEECMLA
     ANVATAEFLK KHEIPALYRV HDGPPPERLE KLRAFLGELG LSLHKGKDGP SPKDYQALLA
     SIKDRPDFHL IQTVMLRSLS QAVYSAQNEG HFGLNYEAYT HFTSPIRRYP DLLTHRAIRS
     VIHSKQDTPH VRRAGAMTIP KARIYPYDEA ALEQLGEQCS MSERRADEAT RDVVNWLKCE
     FMKDRVGESF PGVITAVTGF GLFVELTDIY VEGLVHVTAL PGDYYHFDPV HHRLAGERTG
     RSFRLGDTVE VRVMRVDLDE RKIDFEMAEK TISAPIGRKK RGTETTAPAA KVVEEKAPAK
     STSRRPAKEK AVEAYRPSDA VAKNAELRKS REMKKALLAD AKNGGKAASG GKTGRSAPEK
     ASGGKPAKPS KHRKGPPKAG SAPAKSGGAR KPKAKS
//

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