ID A0A0R1S6A0_9LACO Unreviewed; 776 AA.
AC A0A0R1S6A0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Ribonuclease R {ECO:0000256|HAMAP-Rule:MF_01895};
DE Short=RNase R {ECO:0000256|HAMAP-Rule:MF_01895};
DE EC=3.1.13.1 {ECO:0000256|HAMAP-Rule:MF_01895};
GN Name=rnr {ECO:0000256|HAMAP-Rule:MF_01895};
GN ORFNames=FC85_GL000989 {ECO:0000313|EMBL:KRL64479.1};
OS Lentilactobacillus diolivorans DSM 14421.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1423739 {ECO:0000313|EMBL:KRL64479.1, ECO:0000313|Proteomes:UP000052013};
RN [1] {ECO:0000313|EMBL:KRL64479.1, ECO:0000313|Proteomes:UP000052013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14421 {ECO:0000313|EMBL:KRL64479.1,
RC ECO:0000313|Proteomes:UP000052013};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside
CC monophosphates and is involved in maturation of structured RNAs.
CC {ECO:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00001849, ECO:0000256|HAMAP-
CC Rule:MF_01895};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRL64479.1}.
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DR EMBL; AZEY01000090; KRL64479.1; -; Genomic_DNA.
DR RefSeq; WP_057865436.1; NZ_AZEY01000090.1.
DR AlphaFoldDB; A0A0R1S6A0; -.
DR STRING; 1423739.FC85_GL000989; -.
DR PATRIC; fig|1423739.3.peg.1038; -.
DR Proteomes; UP000052013; Unassembled WGS sequence.
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 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; 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; 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 {ECO:0000256|HAMAP-Rule:MF_01895};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01895};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01895};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01895};
KW Reference proteome {ECO:0000313|Proteomes:UP000052013};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 635..715
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 714..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 776 AA; 88110 MW; E544583C8EECA164 CRC64;
MQDNDLKNKI ENVLRTYPEN VFTVEKIADV LRYHGSAAFK LIVQELAGLE RDGVAVVTQE
GKFQLNPEKQ KLSGIFHAND KGFGFVAYDD LAPDAYIAPD NTMNALNGDT VDMEIVRPAQ
PGSDKGPEGK VTAITDRKYK RVVGPFTKSD DDNGYYGQVK LTDKKIAKYQ FYINDVGLHP
TPGEVITAQI TEYPNAKHPD YMVGIADEVI GSVDDPGIDI LEIVYAHNIP AEFPEEVLQA
ADTIPDHVTE AEKVGREDIT KQNLVTIDGE SSKDLDDAVT AWKLPNGNYH LGVHIADVSH
YVKPGSLIDK EAFRRGTSVY LTDRVIPMLP RRLSNGICSL NEGELRLCMS CEMEIDPSGN
IIKHRIHPSL MRSKARMTYT AVNKILESHD EKTMNQYKEL VPMFEQMGEL HKILYKHRKA
RGAIDFDDNE AEIIVDEKGH PIDIKLRVRG LAERMIESFM LAANETVAKH YYEKHVPFIY
RVHETPDADR IKTFFETLTA FGITVKGDPE HVQPKTMQNI LKKVAGKPEE MMVSVMLLRS
LKQARYADQS LGHFGLAAPF YTHFTSPIRR YPDTMVHRLI HYYQDNGINS ETKKKYATVL
DEISTTTSEY ERRAVDAERD TDSMKKAEYM NDHLGEEFDG VVSSVMKFGL FVELPNTVEG
LVHISRMDDD YYQYVEQFMA LVGRNTRRTY KMGQPIRVKV VNVDVEQSAV DFDVVNPEET
PTSNMLPKRS YQHRDNNHRN NDRHGHSNSN SNNFHSNNRH GKSNNSRGGN HNRNKR
//
