ID A0A1F6X198_9BACT Unreviewed; 659 AA.
AC A0A1F6X198;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=A2914_00995 {ECO:0000313|EMBL:OGI87891.1};
OS Candidatus Nomurabacteria bacterium RIFCSPLOWO2_01_FULL_41_21.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801776 {ECO:0000313|EMBL:OGI87891.1, ECO:0000313|Proteomes:UP000176423};
RN [1] {ECO:0000313|EMBL:OGI87891.1, ECO:0000313|Proteomes:UP000176423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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|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:OGI87891.1}.
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DR EMBL; MFVA01000020; OGI87891.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6X198; -.
DR STRING; 1801776.A2914_00995; -.
DR Proteomes; UP000176423; 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; 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; 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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 578..659
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 659 AA; 75432 MW; 79598776445EF24D CRC64;
MKEKRRILEG TISINSKGVG YVDLGEEKRQ GKKNDRKTDV EIDFKHLKTA LHGDTVEIVL
HPRSGERRTG EVARVISRAK NRFVGVLEKD PASFGASNGI FFLKPDDTKM YTDILVPESK
LHGAKPNQKI FVEIVSWQDP RKAPVGKVLK ILGRPGENDT EMHAIAIEKG FDSVLPEEIE
KEAQKIKQAG LKKEDYKDRR DFRKTLTFTI DPSDAKDFDD AISFKKINGG LFEIGIHIAD
VTHYVKKGGA IDLEARERGT SVYLVDRTIP MLPEVLSNDL CSLVPDKDRF TMSAVFEMNQ
NGEVLKEWFG RTVIHSQKRF SYEEAEKTIK NKNLALHEEL SILNNIARKL TKRRFDSGAI
SLDQEEVKFM LGEGGRPIKV IKKVRGDSNK LIEEFMLLAN KRVAELLSKG THQKVKSPAD
EGIFLYRVHD VPSKEKMEEL AHFLKSLGYN LKQKNGIIEN HDLNKLLHTL DGKPEQDTVS
RAIVRSMAKA IYSTKNIGHY GLAFEFYTHF TSPIRRYPDI VVHRLLLEHL ANRKINPSHF
KEYEQISRTT SEQEKRAAEA ERASIKYKQV EYMSTRLGEK FEGVISGITE WGMYVEELET
KCEGLVRTRD MGDDFYIFNE KKLELVGQKT KRKYRFGDKV KIKVKGVDLE RKTIDYILA
//
