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 27-MAR-2024, entry version 128.
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; Pseudomonadota; 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 DNASU; 2615616; -.
DR EnsemblBacteria; AAF95740; AAF95740; VC_2599.
DR KEGG; vch:VC_2599; -.
DR PATRIC; fig|243277.26.peg.2478; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_0_6; -.
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 GO; GO:0016070; P:RNA metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd04471; S1_RNase_R; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR003029; S1_domain.
DR NCBIfam; TIGR00358; 3_prime_RNase; 1.
DR NCBIfam; TIGR02063; RNase_R; 1.
DR PANTHER; PTHR23355:SF9; DIS3-LIKE EXONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 1.
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; Nucleic acid-binding proteins; 4.
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
//
