ID A0A0V8QFJ6_9FIRM Unreviewed; 709 AA.
AC A0A0V8QFJ6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=ASU35_09475 {ECO:0000313|EMBL:KSV59296.1};
OS Acetivibrio ethanolgignens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=290052 {ECO:0000313|EMBL:KSV59296.1, ECO:0000313|Proteomes:UP000054874};
RN [1] {ECO:0000313|EMBL:KSV59296.1, ECO:0000313|Proteomes:UP000054874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACET-33324 {ECO:0000313|EMBL:KSV59296.1,
RC ECO:0000313|Proteomes:UP000054874};
RA Zou Y., Xue W., Luo G., Lv M.;
RT "Butyribacter intestini gen. nov., sp. nov., a butyric acid-producing
RT bacterium of the family Lachnospiraceae isolated from the human faeces.";
RL Submitted (NOV-2015) 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|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:KSV59296.1}.
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DR EMBL; LNAM01000148; KSV59296.1; -; Genomic_DNA.
DR RefSeq; WP_058352449.1; NZ_LNAM01000148.1.
DR AlphaFoldDB; A0A0V8QFJ6; -.
DR STRING; 290052.ASU35_09475; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000054874; 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; 3.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR011129; CSD.
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; 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; SM00357; CSP; 2.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
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:UP000054874};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 627..707
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 709 AA; 81134 MW; 8B90B66CDA8FF400 CRC64;
MLEKEILNQK KEMIFDYIAS EEYIPVKFKE MAGILQVPKR DKEDFRQVID TLVAEGRIQI
DSRGLIRPAA GNVKRGLFSG TAKGFGFVTV EGEKEDIFIP EDASKGAMHG DTVQIEIYAE
KTGKRKEGRV LTILERGTDM VVGTFHKSKN FGFVVPDNQK LGTDIFIPKE HTKGAVTGHK
VVAQLISYGS SQKSPEGKIV EILGHVNDPG VDIMSIIKAF GLPEEYPAEV MKQVEKVKEE
VDSFDIAGRC DIRDWQMVTI DGEDAKDLDD AITLTKEDGI YHLGVHIADV SHYVQENTPL
DKEALKRGTS VYLVDRVIPM LPHKLSNGIC SLNAGVDRLA LSCFMDIDEK GTVVSHRIAE
SVVRVSRRMS YTSVKKIIED KDPAECEEYK ELVPMFLLME ELADILRKKR HQRGSIDFDF
PESKIYLDDK GCPTDIQPYE RNKATKIIED FMLIANETVA EDYFWQELPF VYRTHDYPDS
DKIEKLGIFI NNFGYSIRIS QDEIHPKELQ KLMEKIDGTP EEALISRLTL RSMKQAKYTT
DNDGHFGLAT KYYCHFTSPI RRYPDLQIHR IIKENLRRGI TEKRREHYAK ILPEVATRSS
MMERRADEAE REVEKLKKAE YMKQFIGEVF EGVISGLTTW GIYVELPNTV EGMIRVTNLP
GDYFYYDEEN YVMIGEHTRK TYKLGERILV EVDSVDRILK TIDFIPAEE
//
