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Database: UniProt
Entry: A0A073K475_9BACI
LinkDB: A0A073K475_9BACI
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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
//
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