ID   RNR_HAEIN               Reviewed;         782 AA.
AC   P44907;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 133.
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};
DE   AltName: Full=VacB protein homolog;
GN   Name=rnr {ECO:0000255|HAMAP-Rule:MF_01895}; Synonyms=vacB;
GN   OrderedLocusNames=HI_0861;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC22520.1; -; Genomic_DNA.
DR   PIR; G64098; G64098.
DR   RefSeq; NP_439021.1; NC_000907.1.
DR   RefSeq; WP_010869073.1; NC_000907.1.
DR   STRING; 71421.HI_0861; -.
DR   PRIDE; P44907; -.
DR   EnsemblBacteria; AAC22520; AAC22520; HI_0861.
DR   KEGG; hin:HI_0861; -.
DR   PATRIC; fig|71421.8.peg.902; -.
DR   eggNOG; COG0557; Bacteria.
DR   HOGENOM; CLU_002333_7_0_6; -.
DR   OMA; DWYEYRS; -.
DR   PhylomeDB; P44907; -.
DR   BioCyc; HINF71421:G1GJ1-902-MON; -.
DR   Proteomes; UP000000579; Chromosome.
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..782
FT                   /note="Ribonuclease R"
FT                   /id="PRO_0000166403"
FT   DOMAIN          651..732
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01895"
FT   REGION          738..782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..762
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        763..782
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   782 AA;  89848 MW;  131E6AF65AF2537E CRC64;
     MTKKRKNLIN QDPHYKRELE KYGNPIPSRE FILTVIRDNN APMNRDEILT ALSIRNEDQI
     EAMRRRLRAM ENDGQLVFTK RKRYALPEKL DLFKGTVIGH REGFGFLQVD GKKDDLFIPN
     HQMQRVMHGD FVLAQPAGLD RRGRREVRIV RVLESRKKQI VGRFFLENGF GYVVPDDSRI
     GRDILVPNEH RNGARMGQVV VVELQERSAS FNQPIGVITE ILGDNMAKGM EVEIALRNHD
     ILHKFPSAVE KYVKKFTEEV SEEAKKGRVD LRNLPLVTID GEDARDFDDA VYCEKHGKGW
     KLWVAIADVS YYVRLRSTLD VEAHNRGNSV YFPNRVVPML PEILSNGLCS LNPQVDRLCM
     VCEMQISAKG KLTDYRFYEA VMNSHARLTY TKVAKMLEGD EELRTRYSTL VPHLEELYKL
     YQALLSARHQ RGAIDFETIE TKFIFNAMGR IERIEPVVRN DAXKIIEECM XLANIAAANF
     MEKHKEPALY RIHATPSEEK LTSFRTFLSE FGLTLEGGLK PTTKDYAALL EKVKERPDHE
     LIQTMLLRSL SQAVYHADNI GHFGLALEEY AHFTSPIRRY PDLTLHRGIK YLLAKEQGAK
     RKTTDTGGYH YSFDEMDLLG NHCSMTERRA DDATREVADW LKCEYMQDHV GGEFSGVISS
     VTGFGLFVRL DDLFIDGLVH ISTLENDYYQ FDAAKQRLIG ENSGMQYRLG DKVRIKVEAV
     HLENKMVDFS LIGSERKPRR AGKTAKEKAK KVFKELPSKA SKKRKSAVKK KDVSKKTSRK
     RK