ID   RNR_BUCAI               Reviewed;         731 AA.
AC   P57628;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   15-NOV-2002, sequence version 2.
DT   27-MAR-2024, entry version 129.
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}; OrderedLocusNames=BU565;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(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   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB13255.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BA000003; BAB13255.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_240369.1; NC_002528.1.
DR   RefSeq; WP_014498791.1; NC_002528.1.
DR   AlphaFoldDB; P57628; -.
DR   SMR; P57628; -.
DR   STRING; 563178.BUAP5A_558; -.
DR   EnsemblBacteria; BAB13255; BAB13255; BAB13255.
DR   KEGG; buc:BU565; -.
DR   PATRIC; fig|107806.10.peg.568; -.
DR   eggNOG; COG0557; Bacteria.
DR   HOGENOM; CLU_002333_7_0_6; -.
DR   Proteomes; UP000001806; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
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; 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; 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..731
FT                   /note="Ribonuclease R"
FT                   /id="PRO_0000166397"
FT   DOMAIN          647..728
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01895"
SQ   SEQUENCE   731 AA;  84807 MW;  1AED36ACF09CCC2A CRC64;
     MVVDPYQKRE AKRYKNPIPS REYISSCLRT SQDLISQKNL EKKFGINNQE SKKALRRRLR
     AMERDGQVIY TSNRCYVAPE SLKIVKGKVI GHRDGYGFLR TETLKEDLWL SSEQMKSCIH
     GDIILAHIVE THGKRRSSAR FLKLLQPNNI LIVGRYYIDD KIKFVIPDDT RFNFKIFIFS
     AIKDDISIGS IVSVKLKQHP IRNSRVQGFI VEILGKEMGT NLAIEIALRT HLIPSLWSKE
     VKKQVYEISR KINQYDFKNR TDLRHFPFFT IDDEDARDFD DAVFCKRKAN PEEGWILWVA
     IADVSCYVQP NTPLDKAALE RGTSVYFPSL VIPMLPEKIS TDLCSLKPNV ERLCLICEMS
     LSKQGELISY KHYEGIICSH GRFTYNEIFK IWNGDIFLRS KYKKFLKDIE NLSCLQNIFN
     KDNISKKGIY FENIEPKFVL DSNLRIKSIY QNIRNDAHKF IESCMILANV ASARFVEKYK
     YPVLFRNHDR PKKDNVVSLR LFLNELGFTL LGGDSPESVH YSNLLKNVSD RPEYEMIQTV
     LLRSMTQAVY SPDNRGHFGL SLSSYVHFTS PIRRYPDLIL HRVIKYLLFK DKNTSKSNYN
     FYSAHLYSTG EIKKIGAHCS ITERRADEAN RDVIDWLKCD FMYKKIGCIL NGVISNVTTF
     GFFVRLNQFF IDGLVHINSL NDDYYYFDSL GLKLIGKSTK NTYCLGDALK VKVISVNLNE
     KKIELSLYKS S
//