ID A0A0V8JLW5_9BACI Unreviewed; 784 AA.
AC A0A0V8JLW5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 18-JUN-2025, entry version 40.
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=AS180_10610 {ECO:0000313|EMBL:KSU87946.1};
OS Priestia veravalensis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=1414648 {ECO:0000313|EMBL:KSU87946.1, ECO:0000313|Proteomes:UP000053681};
RN [1] {ECO:0000313|EMBL:KSU87946.1, ECO:0000313|Proteomes:UP000053681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGD-V-76 {ECO:0000313|EMBL:KSU87946.1,
RC ECO:0000313|Proteomes:UP000053681};
RA Dastager S.G., Mawlankar R.;
RT "Bacillus caseinolyticus sp nov.";
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:KSU87946.1}.
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DR EMBL; LNQP01000032; KSU87946.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V8JLW5; -.
DR Proteomes; UP000053681; 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 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:UP000053681};
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 719..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 784 AA; 89407 MW; A215A970B0D8B30C CRC64;
MEQEIQQYID RLLTFMKEET YKPLTVQELE KEFGIEDSAE FKDFVKALVI MEEQGLIIRA
RNNRYGVPER MNFVKGKVTG HAKGFAFVVP EEQGADDIFI PTTETNNAMH GDIVLARVLS
ESSGNRREGT IVKIIERGTQ QIVGTYTESK NFGFVIADDK KIAGDIFIPK GARNGAAEGH
KVVVELTSYP EGRMNAEGKI VQILGHKNDP GVDIISVIHK YGLPQEFPGD VLEQAINTPE
TISEDEIKGR RDLRDQVIVT IDGADAKDLD DAVTVTELEN GNYKLGVHIA DVSHYVTEGS
PIDVEAAERG TSIYLVDRVI PMIPHRLSNG ICSLNPKVNR LTLSCEMEIN SAGEVVNHDI
FESVIKTTER MTYSDVNKIL TDKDEAVRAR YEELIPMFER MEKLAEILRK KRMDRGAIDF
DFKEAKVLVD DDGHPTDVIL RERSVSERLI EEFMLAANET VAEHFHWMNV PFMYRIHEDP
KEEKLNRFLE FVTNLGYAVK GTGNDIHPRA LQDILEAVAG TPEEMVVSKV MLRSMQQAKY
QADNLGHFGL SAEFYTHFTS PIRRYPDLIV HRLIRTYLIN NQVDEATQEK WGEKLPEIAD
HSSSMERRSV DAERETDDMK KAEFMADKIG ETFDGIISSV TNFGMFVELS NTIEGLVHVS
DLTDDYYRYD ERHYAMIGER TGKVFRIGDE IEIKVADVNK DERAIDFVIV GMKTSQKRLS
KDRPKVINMK QKSRKDDKEN RRGRRKDKAG DSKGEWTTQK PKKRKKKKFF EGAPNLKKKK
KKRK
//
