ID A0A257TES2_9BACT Unreviewed; 656 AA.
AC A0A257TES2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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=B7X04_01220 {ECO:0000313|EMBL:OYV84013.1};
OS Parcubacteria group bacterium 21-54-25.
OC Bacteria.
OX NCBI_TaxID=1970248 {ECO:0000313|EMBL:OYV84013.1, ECO:0000313|Proteomes:UP000216537};
RN [1] {ECO:0000313|EMBL:OYV84013.1, ECO:0000313|Proteomes:UP000216537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=21-54-25 {ECO:0000313|EMBL:OYV84013.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OYV84013.1}.
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; NCBJ01000003; OYV84013.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257TES2; -.
DR Proteomes; UP000216537; 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; 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; 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; 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 562..643
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 656 AA; 73252 MW; 167A58535FEAEC4F CRC64;
MNPDQKNSKT HEGIIQITRR GTGFFSLGED KKDLMIPREW LGGAFPLDVV RIEEAGVIEN
RSAAKVVGIV ERVRTTFVGT LSEENGRVLL LPDWKRMYTP FAISGEHLPL GHKVLVRFTH
WNAGEEFPTA VIEEDIGTAG VHETEMRALV LGEGFRPGFP PGVEKEAAAL EQGGRARIDV
EIARGTRRDF RDVTTFTIDP IDAKDFDDAL SVRDLGDGKT EVGIHIADVS FFVTPGTPID
REARDRATSV YLVDRTIPML PEVLSNDLCS LRPNENRLAV SAVLTLDANA TIIDRWFGET
VIHSDKRFTY EAAQEVLDNS TGEFHAELLT LRTLAQKIRA RRIQNGAIEF DTAEVKIELD
DAGAPVAIRL KERKDTNLLI EDFMLAANVA VAEHLAEASK KRGLTRGFIY RIHDAPDADR
IENLSLFLRV LGYHLDTHAG HVKGTDLNAL MEKVVGTPEE YLVKTAALRS MAKAIYSTKN
VGHFGLAFQH YTHFTSPIRR YPDLSVHRIL KQYAEGTKIP EQTLAAFETL AIHASEREVA
ATHAERDSIK MKQVEFLAKR IGEEFDAVIS GVTERGLFVE EQTTRADGMI RISTLGDDYF
DYDEKRYRLV GRRTKKAFTL GDPIRVKLIA ARIADRELDF SLGAKSDTPH HRAGHA
//
