ID   RNR_ACIFR               Reviewed;         439 AA.
AC   P54084;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Ribonuclease R;
DE            Short=RNase R;
DE            EC=3.1.13.1;
DE   AltName: Full=VacB protein homolog;
DE   Flags: Fragment;
GN   Name=rnr; Synonyms=vacB;
OS   Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans).
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Fe1;
RX   PubMed=1317860; DOI=10.1016/s0021-9258(19)49902-x;
RA   Kusano T., Takeshima T., Sugawara K., Inoue C., Shiratori T., Yano T.,
RA   Fukumori Y., Yamanaka T.;
RT   "Molecular cloning of the gene encoding Thiobacillus ferrooxidans Fe(II)
RT   oxidase. High homology of the gene product with HiPIP.";
RL   J. Biol. Chem. 267:11242-11247(1992).
CC   -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside
CC       monophosphates and is involved in maturation of structured RNAs.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC         nucleoside 5'-phosphates.; EC=3.1.13.1;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA40595.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X57324; CAA40595.1; ALT_FRAME; Genomic_DNA.
DR   PIR; S23260; S23260.
DR   AlphaFoldDB; P54084; -.
DR   SMR; P54084; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
DR   GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.140; -; 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; IPR004476; RNase_II/RNase_R.
DR   InterPro; IPR013668; RNase_R_HTH_12.
DR   Pfam; PF17876; CSD2; 1.
DR   Pfam; PF08461; HTH_12; 1.
DR   Pfam; PF08206; OB_RNB; 1.
DR   Pfam; PF00773; RNB; 1.
DR   SMART; SM00357; CSP; 1.
DR   SMART; SM00955; RNB; 1.
DR   SUPFAM; SSF50249; SSF50249; 2.
DR   TIGRFAMs; TIGR00358; 3_prime_RNase; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Nuclease; RNA-binding.
FT   CHAIN           1..>439
FT                   /note="Ribonuclease R"
FT                   /id="PRO_0000166413"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         439
SQ   SEQUENCE   439 AA;  49332 MW;  C937BD6E2D767DEE CRC64;
     MPETQEPASL NERDPMFERE KEKYERPIVS REYILSYLEG TGRPLTLEDI IAELEVAEDD
     QEALRRRLRA MERDGQLVRN RRGAYGIVAA MELVRGTVSA HPDGFGFLIP EAGGKDLFLS
     PREMRKVFHG DTILGRAVGE DRRGRIEGAV VRILERALKH IVGRYYADNG VHYVVPEDRR
     IPQEFAVVEG EGEGLTPVHG QIVILEITQY PDGRNMPQGH VVEILGEHMA PGMEVEIAVR
     NYGLPHQWPD EVLAEIKQFS ETVPETMKAG RRDLRDLPLV TIDGADAKDF DDAVYAEVIE
     NGFRLTVAIA DVATYVCPDS ALDREAVTRG NSVYFPRRVI PMLPEILSNG LCSLNPHVDR
     LCMFCEMEMD AAGRSTGFRF DRGIIGSQRR FTYDEVAAIL AGDAELRAQD AAMVPHLEAL
     HSLYESFAKA RERRGTIEF