ID   RNR_VIBCH               Reviewed;         821 AA.
AC   Q9KNY1;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Ribonuclease R {ECO:0000255|HAMAP-Rule:MF_01895};
DE            Short=RNase R {ECO:0000255|HAMAP-Rule:MF_01895};
DE            EC=3.1.13.1 {ECO:0000255|HAMAP-Rule:MF_01895};
GN   Name=rnr {ECO:0000255|HAMAP-Rule:MF_01895}; OrderedLocusNames=VC_2599;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
CC   -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside
CC       monophosphates and is involved in maturation of structured RNAs.
CC       {ECO:0000255|HAMAP-Rule:MF_01895}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC         nucleoside 5'-phosphates.; EC=3.1.13.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01895};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01895}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01895}.
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DR   EMBL; AE003852; AAF95740.1; -; Genomic_DNA.
DR   PIR; C82055; C82055.
DR   RefSeq; NP_232227.1; NC_002505.1.
DR   RefSeq; WP_001285863.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KNY1; -.
DR   SMR; Q9KNY1; -.
DR   STRING; 243277.VC_2599; -.
DR   PRIDE; Q9KNY1; -.
DR   DNASU; 2615616; -.
DR   EnsemblBacteria; AAF95740; AAF95740; VC_2599.
DR   GeneID; 57741201; -.
DR   KEGG; vch:VC_2599; -.
DR   PATRIC; fig|243277.26.peg.2478; -.
DR   eggNOG; COG0557; Bacteria.
DR   HOGENOM; CLU_002333_7_0_6; -.
DR   OMA; DWYEYRS; -.
DR   BioCyc; VCHO:VC2599-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.50.140; -; 2.
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;
KW   Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..821
FT                   /note="Ribonuclease R"
FT                   /id="PRO_0000166415"
FT   DOMAIN          652..733
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01895"
FT   REGION          739..821
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..761
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        780..796
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        797..821
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   821 AA;  93334 MW;  E3AE7441097447D9 CRC64;
     MSDTTHLDPF ADREADNYDN PIPSREYILE FLTQANVPMN RNDLFEALKL EGEEQYEGLR
     RRLRAMERDG QLVFTRRQCY ALPEKLEMVK GYVIGHKDGH GWVRPEGSLN KEGDILLPHH
     QMRTLIHGDF VLVQPSGTDK RGRKEGRLVR ILEERNGQIV GRFFFEYGYS YVVPDDSRIH
     HDILIPNDLR AGARMGNVVV IEITDRGTRN RGMMGKVVEV LGENMAPGME TQIAIRTHQI
     PHEWPAEVEQ QVAGLTEEVP EEAKQGRVDL RALPLVTIDG EDARDFDDAV YCEAKKGGGW
     RLWVAIADVS YYVRPDTALD KEAINRGNSV YFPSQVVPML PEVLSNGLCS LNPQVDRLCM
     VCEMTVSETG KLSGYKHYEA VMNSHARLTY TKVHEILEGD EELRERYKAL VPHLEELHKM
     YQVLKSARDE RGAIEFETVE TKFIFNAQRK IESIEPVVRN DAHKLIEECM ILANIASASL
     VEKAKEAALY RVHEPPGEER LTGFRDFLGE LGLDLSGGLE PSPTDYANLM KQIGERPDKE
     LIQTMLLRSM KQAVYNADNA GHFGLALKRY AHFTSPIRRY PDLLLHRAIK YLIAKQEGRN
     QDRWTPTGGY HYSFDDMDFY GEQCSMTERR ADDATREVSD WLKCEYMQDH VGEELEGVVA
     NVTSFGFFVR LTELHIDGLV HISTLANDYY HYDPIGQRLV GESFGAIYRL GDAVKVKVLA
     VNLDDRQIDF ELVETSRKLR GQGKTAKKRA DEARAKAQGK KEAATKGACG KSPTKSELKP
     QVEATRRPDS EGRSKPKKTK APKKRKDQAR KKSGKVRDKT K