ID A0A073K475_9BACI Unreviewed; 798 AA.
AC A0A073K475;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 18-JUN-2025, entry version 47.
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=BAMA_00405 {ECO:0000313|EMBL:KEK21267.1};
OS Bacillus manliponensis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=574376 {ECO:0000313|EMBL:KEK21267.1, ECO:0000313|Proteomes:UP000027822};
RN [1] {ECO:0000313|EMBL:KEK21267.1, ECO:0000313|Proteomes:UP000027822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15802 {ECO:0000313|EMBL:KEK21267.1,
RC ECO:0000313|Proteomes:UP000027822};
RA Lai Q., Liu Y., Shao Z.;
RT "Draft genome sequence of Bacillus manliponensis JCM 15802 (MCCC
RT 1A00708).";
RL Submitted (JUN-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|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:KEK21267.1}.
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DR EMBL; JOTN01000001; KEK21267.1; -; Genomic_DNA.
DR RefSeq; WP_034634919.1; NZ_JOTN01000001.1.
DR AlphaFoldDB; A0A073K475; -.
DR STRING; 574376.BAMA_00405; -.
DR eggNOG; COG0557; Bacteria.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000027822; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:TreeGrafter.
DR CDD; cd04471; S1_RNase_R; 1.
DR FunFam; 2.40.50.140:FF:000213; Ribonuclease R; 1.
DR FunFam; 2.40.50.140:FF:000219; Ribonuclease R; 1.
DR FunFam; 2.40.50.140:FF:000273; Ribonuclease 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; IPR022966; RNase_II/R_CS.
DR InterPro; IPR004476; RNase_II/RNase_R.
DR InterPro; IPR011805; RNase_R.
DR InterPro; IPR050180; RNR_Ribonuclease.
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; PS01175; RIBONUCLEASE_II; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000027822};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01895}.
FT DOMAIN 630..710
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 720..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 602..632
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 740..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 798 AA; 90778 MW; A3961029A5DF13A4 CRC64;
MEEIMQQNID KLLSFMKEEA YKPLTVQELE EAFGIEEVAD FKEFVKALVV MEDQGLVVRT
RSNRYGLPEK MNLVRGKLIG HERGFAFVVP EEKGTDDIFI PPTELNGAMH GDTVLARISS
QSSGSRKEGS IVRIIERGTK TLVGTYTESK NFGFVIPDNK RWTSDIFILK SASMGAVDGH
KVVVKITSYP ENRLSAEGEV IQILGHKNDP GVDILSVIHK HNLPLTFPED VMEHANSVPE
TISEEDVKDR RDLRNEVIVT IDGADAKDLD DAVTVTKLEN GNYKLGVHIA DVSHYVHEDS
PIDREAAERA TSVYLVDRVI PMIPHRLSNG ICSLNPKVDR LTLSCEMEIN QLGDVVKHEI
FQSVIKTTER MTYSDVRSIL EDEDEELIKR YEPLVPMFKD MAELASVLRD KRMRRGAIDF
DFKEAKVLVD EEGKPTEVIM RDRSVAEKLI EEFMLVANET VAEHFHWMNV PFMYRVHEDP
KEDKLERFFE FVTNFGYAVK GRANEIHPRA LQQILEMVQG QPEEVVISTV MLRSMKQARY
DAESLGHFGL STEFYTHFTS PIRRYPDTIV HRLIREYIIN GKIDAKTQAK WRESLPDIAE
HSSNMERRAV EAERETDELK KAEYMLDKVG EEYDGIISSV TNFGLFVELP NTIEGLVHVS
YLTDDYYRYD EQHFAMIGER TGNVFRIGDE ITVRVINVNK DERAIDFEIV GMKGGAKRVR
KDRPVVIDGS KGGGRGGRGR RGERGSEDRG RDKKRGGGRP GGGKEASSSR GKQDNGKKKK
KSFFENAPSF KRKKKKRK
//