ID   RNR_MYCPN               Reviewed;         726 AA.
AC   P75529;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=MPN_243; ORFNames=MP589;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB96237.1; -; Genomic_DNA.
DR   PIR; S73915; S73915.
DR   RefSeq; NP_109931.1; NC_000912.1.
DR   RefSeq; WP_010874600.1; NC_000912.1.
DR   AlphaFoldDB; P75529; -.
DR   SMR; P75529; -.
DR   IntAct; P75529; 1.
DR   STRING; 272634.MPN_243; -.
DR   EnsemblBacteria; AAB96237; AAB96237; MPN_243.
DR   KEGG; mpn:MPN_243; -.
DR   PATRIC; fig|272634.6.peg.262; -.
DR   HOGENOM; CLU_002333_7_3_14; -.
DR   OMA; DWYEYRS; -.
DR   BioCyc; MPNE272634:G1GJ3-385-MON; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; -; 1.
DR   HAMAP; MF_01895; RNase_R; 1.
DR   InterPro; IPR011129; CSD.
DR   InterPro; IPR012340; NA-bd_OB-fold.
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; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
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; 3.
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..726
FT                   /note="Ribonuclease R"
FT                   /id="PRO_0000166409"
FT   DOMAIN          645..726
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01895"
SQ   SEQUENCE   726 AA;  83219 MW;  6A58508593BE0596 CRC64;
     MKVLTDLQKR IFAIVKKENG KPIPPGIVVR MMENQAGFPG KQQVYRAIDD LLEWHIFRKS
     GGATNQLLIN YELADPVLDQ KFQGILNLGN KNTGFVRPLD DDKTVYYIHF SNLAGALDGD
     LVEFCPLDKP QVGDKFDAAV LKIVKRSRVL YAGNFLIEYS DFGQEFRIVA DNPRFYLTPI
     VNKASVPAEL ESNTKVAFQI DEYDPANNLC KVSIQQILGN NDEPLINLKA IMLDHSIVFE
     DNDVVEQQAA KLQFDEKEQS KPYRKDLTEL AFVTIDPATS KDLDDAIYVK RTDKGFVLYV
     AIADVAYYVQ RNSELDIEAR HKTSSIYLPG YYVVPMLPER LSNELCSLNP NEKRYVVVCE
     LNFDHEARLN FSEVYPATIV SQRRFAYSEV NDWLEDSDAL KDESATVLES LKAGFTLSEL
     IAEQRKKKGT IDLSHSETEV VVDQNYYPIE IRFLTHGKAE TMIENLMVVA NEAVAWTLTN
     HKVHLPYRVH PRPSKKKLQM LLENIVELKI TQPNFVLDTV TSTQIAAWLK ENKDNPSYDI
     FVILLLRTLG KAFYIVNPLI HFSIGSHHYT HFTSPIRRYA DLTVHRLLWM NLFTPERFTD
     TEREQLNAEL EQICETINDT EIKINGCERT ANDYLTTLYL SKQVGQTFHG FISAITSFGI
     FMRMDENNFD GLIKITSIPE DFFVFEKDRM VLRGKRTNKV FRIGDRLTAK LTEIDTVQKR
     AILTLV