ID   RNR1_LACLA              Reviewed;         817 AA.
AC   Q9CH00;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Ribonuclease R 1;
DE            Short=RNase R 1;
DE            EC=3.1.13.1;
DE   AltName: Full=VacB protein homolog 1;
GN   Name=rnr1; Synonyms=vacB1; OrderedLocusNames=LL0942; ORFNames=L0323;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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}.
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DR   EMBL; AE005176; AAK05040.1; -; Genomic_DNA.
DR   PIR; F86742; F86742.
DR   RefSeq; NP_267098.1; NC_002662.1.
DR   RefSeq; WP_010905644.1; NC_002662.1.
DR   AlphaFoldDB; Q9CH00; -.
DR   SMR; Q9CH00; -.
DR   STRING; 272623.L0323; -.
DR   PaxDb; Q9CH00; -.
DR   PRIDE; Q9CH00; -.
DR   EnsemblBacteria; AAK05040; AAK05040; L0323.
DR   KEGG; lla:L0323; -.
DR   PATRIC; fig|272623.7.peg.1008; -.
DR   eggNOG; COG0557; Bacteria.
DR   HOGENOM; CLU_002333_4_1_9; -.
DR   OMA; DWYEYRS; -.
DR   Proteomes; UP000002196; 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; -; 2.
DR   HAMAP; MF_01895; RNase_R; 1.
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; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   Pfam; PF17876; CSD2; 1.
DR   Pfam; PF08206; OB_RNB; 1.
DR   Pfam; PF00773; RNB; 1.
DR   Pfam; PF00575; S1; 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..817
FT                   /note="Ribonuclease R 1"
FT                   /id="PRO_0000166406"
FT   DOMAIN          637..717
FT                   /note="S1 motif"
FT   REGION          728..817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..759
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        760..781
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        791..808
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   817 AA;  92250 MW;  44079115EF624D73 CRC64;
     MSIREVIMDY LENSSKKALS VEELSVALHM NKAKDYKVFV KTLASLEAEH LLNFTAKGKV
     ELAEKEEAKV VISGIFRANA AGFGFVSIDA EEPDVFVARG QTAFALDGDE VFIEIDKNAN
     ALKGTSAEGH VVEIIRHDVH QVVGTFVALN DDEKEQTGLI GFVKSRNKKI PYRVYLENEG
     LIPENKAIVR VEITHYPDKE FPQTMQGLVT EIIGQADDQG IDVLEVLASM DIVSEFPKEV
     LDQAEAVPEE VPENEIVGRV DYRNEITFTI DGADAKDLDD AVHAKRLENG NYELGVHIAD
     VSHYVTENSP LDKEAYERGT SVYVTDRVVP MLPERLSNGI CSLNPRINRL TQSCVMEISP
     EGRVINYQIS QSIIKTTERM TYDAVNQMIA GDEAALENYA KIADSVKIMV ELHHILEAMR
     KRRGAIDFDT VEAKIIVNEK GLPIEIRKRT RGIAERMIES FMLEANETVA THFEAHGLPF
     IYRIHEQPKA DRLQRFIDFA ATFGMQIEGT SNGIDQKVLQ AFMKKIKGQP GEMVLSTMLL
     RSMQQARYSE NNEGHFGLAA ENYTHFTSPI RRYPDLLVHR LIREIGEGKT PANILQKWED
     KIPEIAEHSS HRERRAVDAE REVEKMKKAE FMEEHVGEEY EGIIASVTRF GMFIELENTI
     EGLVHISTLK GDYFNYQERM LALIGERSGL TFKIGQPIKI KVVKADRMTG EIDFEYLPSE
     LDLIDKAAKA KKKPDHKGRK KSNQSLKVKS VAPKSTDKSA NKSKNGRRAD EKFEFDKKKK
     KSAKKPFYSK AAKGKFTDKK DNGKKFTDGR KKPHKRG