ID   RNR_CHLTR               Reviewed;         694 AA.
AC   O84402;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 112.
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=CT_397;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE001273; AAC67994.1; -; Genomic_DNA.
DR   PIR; H71518; H71518.
DR   RefSeq; NP_219907.1; NC_000117.1.
DR   RefSeq; WP_010725182.1; NC_000117.1.
DR   AlphaFoldDB; O84402; -.
DR   SMR; O84402; -.
DR   STRING; 813.O172_02160; -.
DR   PRIDE; O84402; -.
DR   EnsemblBacteria; AAC67994; AAC67994; CT_397.
DR   GeneID; 884714; -.
DR   KEGG; ctr:CT_397; -.
DR   PATRIC; fig|272561.5.peg.428; -.
DR   HOGENOM; CLU_002333_7_3_0; -.
DR   InParanoid; O84402; -.
DR   OMA; DWYEYRS; -.
DR   Proteomes; UP000000431; 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; -; 1.
DR   HAMAP; MF_01895; RNase_R; 1.
DR   InterPro; IPR011129; CSD.
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   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.
DR   PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..694
FT                   /note="Ribonuclease R"
FT                   /id="PRO_0000166401"
FT   DOMAIN          571..648
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01895"
FT   REGION          652..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        674..694
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   694 AA;  78065 MW;  8D10899BBEA34F11 CRC64;
     MGKAKNKKKF LKNRKQVLVP GTLFVHSRKG FGFVSPDQPE LYPFDIFISA SDLKGALDGD
     HVLVALPFSL RGGEKRKGVI HKVLSRGKTV LVGTIVSLIN PTLAMVYVNT IGPEHPLKAE
     LLPKRTYKLG DRLLLKTPVW KENYPSREPP PLAMLEFIGN ISNAKTDFPV IKAEFSITEE
     FPDAVVQEAS QFLQKHVTQA LHSRKDLRDL LCFTIDSSSA KDFDDAVSLT YDHEGNYILG
     VHIADVSHYV TPNSALDREA AKRCNSIYFP GKVIPMLPSA LSDNLCSLKP NVDRLAVSVF
     MTFSKEGFLS DYRILRSVIR SKYRMTYDEV DEIIEKKQTH PISKTILKMA ELSRIFSDIR
     EQRGCTRLVL PSFTMSLDNL QEPVALIENK QTAAHKLIEE FMLKANEVIA YHISHQGITM
     PFRTHEPPNE ESLLVFQETA KAMGFTITQT PAQEPDYQYL LQETTAGHPL EPILHSQFVR
     SMKTASYSTE NKGHYGLCLD YYTHFTSPIR RYVDLIVHRL LFHPLSVEEE HLEQIVRACS
     SQERIAAKAE GAFVNIKKAR FLKKFIEEQP ATLYKAFIIT ASPEGISFVL PEFCHEGFIP
     AAKLPQAYVL QTKIGLEELP EHLRPGAVIS VQLASVTLLT QSIEWTLVEA TTKAKAKRTS
     KKKKTESVTT KEKKKSPAKK KKGATKTKKG SGKN