ID A0A1F6EWY2_9BACT Unreviewed; 657 AA.
AC A0A1F6EWY2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=A3A36_01120 {ECO:0000313|EMBL:OGG78118.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPLOWO2_01_FULL_52_12b.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798509 {ECO:0000313|EMBL:OGG78118.1, ECO:0000313|Proteomes:UP000178811};
RN [1] {ECO:0000313|EMBL:OGG78118.1, ECO:0000313|Proteomes:UP000178811}
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:OGG78118.1}.
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; MFLW01000023; OGG78118.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6EWY2; -.
DR Proteomes; UP000178811; 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 SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
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 575..656
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 657 AA; 72541 MW; 217A208A628C1BBA CRC64;
MAADTVYEGP ITMTRKGIGF FAAPAASSEA SAKEDLIIPP EWTNHALAGD IVKVVSAGSY
HDPSGRMPPR AAGKVVEIVS RARETFVGTL IEENGLTLLA PDYKKMYVPI VIRDRGETQI
GYKVLVRLEE WAADKEYPLG TIREVIGKAG VHETEMRALA LGQGFSSDFP SAVAAEAKRL
ELEGQAMLVA EVARLVESGR RDFRFVPTCT IDPIDAKDFD DALSVQQLPD GTIEVGVHIA
DVSFFVKPGT ALDTEATLRA TSVYLVDRTI PMLPEVLSND LCSLKPDEDR LAVSAVFKLD
TEANVKDVWF GETVIHSNKR FTYENAQEVL DAGSGTLHEE LSLLHTLAQK IRTSRQAKGA
IEFDTAEVKV ELDGTGKPIA IHLKERKGTN LLIEDFMLLA NEAVAKYLSE LTKNGGPHFA
SLYRVHDTPD ADRIENLAHF LRVLGYHLKT SGGKVSGAEL NKLLEEVKGK PEEYLIKTAT
LRSMSKAVYA TKNIGHFGLG FDFYTHFTSP IRRYPDLVIH RLIKAHAGGA AITAQEMQEF
DALALHASER EVAASDAERD SIKMKQVEFL AGRIDEEFDA VISGVTDRGL YVEEQTTNAD
GMINIRAVGD DYFEYDEKYY RLIGRRTKKV YQLGDPIRVK LIAARIPEKE LDFVPVI
//
