ID A0A099BWH4_9BACT Unreviewed; 731 AA.
AC A0A099BWH4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=HMPREF0671_05725 {ECO:0000313|EMBL:KGI60504.1};
OS Prevotella sp. S7 MS 2.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1287488 {ECO:0000313|EMBL:KGI60504.1, ECO:0000313|Proteomes:UP000029732};
RN [1] {ECO:0000313|EMBL:KGI60504.1, ECO:0000313|Proteomes:UP000029732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S7 MS 2 {ECO:0000313|EMBL:KGI60504.1,
RC ECO:0000313|Proteomes:UP000029732};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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:KGI60504.1}.
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DR EMBL; JRPT01000023; KGI60504.1; -; Genomic_DNA.
DR RefSeq; WP_036897747.1; NZ_JRPT01000023.1.
DR AlphaFoldDB; A0A099BWH4; -.
DR eggNOG; COG0557; Bacteria.
DR Proteomes; UP000029732; 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 Reference proteome {ECO:0000313|Proteomes:UP000029732};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 649..730
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 731 AA; 83410 MW; E7429C799B7CD854 CRC64;
MGKGKKGGKR MTKNQLSEKL IGLFSSQPEK TLSFKEIFRI LRLDTHPLKM LAIDILESLA
WEDYLTRVSD NSYKLNLKGQ VQEGTFVRKS NGKNSFIPDD GSLPIFVSER NSMSALNGDR
VKVSIMARRA NHIKEAQVIE IISRKKDTVV GKLRVEKDLA FLITQENLFV RDIIIPKRKL
KGGKTNDKAI VKIKQWPDAE HKNLVGEVID VLGQSGDNDT EMNTILSQYG LPYKYPKAVE
EAAEKISGEI TEQDERERED FRDVFTCTID PKDAKDFDDA LSIKKLDKGL WQVGVHIADV
SHYVTEGSII DKEAYKRATS VYLVDRTIPM LPERLCNFIC SLRPDEDKLA YSVIFNMDEE
GDVKTHRVVH TIIRSNRRYA YEEVQELLEA NGVVDGTGEP APKAPKGGYK GENADNLIML
DRLAKKLRAA RFKNGAVKFD REELHFDIDE KGTPTKCYFK RSHDANKLIE EFMLLANRTV
AESIGKVKKG AKAKTLPYRI HDNPDPQKLE VLREFIVKFG YRLKSSSTKG AAARSLNKLM
DEVESKPEGK LIQTVALRAM MKAKYSVHNI GHFGLAFDYY THFTSPIRRY PDTMVHRLLT
RYAEGGRSAN EKHYEEFCEH CSDMEQIAQN AERDSIKYKM VEFMADKLGN VYDAHISGIT
SYGIYAEIDE NHCEGMVPMR DLGDDFYDFD ERNFCLVGRR RHHKYQLGDA IKIQVAKANI
EKKQLDFTLA E
//
