ID A0A3M8DKK4_9BACL Unreviewed; 820 AA.
AC A0A3M8DKK4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 18-JUN-2025, entry version 24.
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 ECO:0000313|EMBL:RNB87637.1};
GN ORFNames=EDM56_13740 {ECO:0000313|EMBL:RNB87637.1};
OS Brevibacillus fluminis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Brevibacillus.
OX NCBI_TaxID=511487 {ECO:0000313|EMBL:RNB87637.1, ECO:0000313|Proteomes:UP000271031};
RN [1] {ECO:0000313|EMBL:RNB87637.1, ECO:0000313|Proteomes:UP000271031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15716 {ECO:0000313|EMBL:RNB87637.1,
RC ECO:0000313|Proteomes:UP000271031};
RA Dunlap C.;
RT "Phylogenomics of Brevibacillus.";
RL Submitted (OCT-2018) 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:RNB87637.1}.
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DR EMBL; RHHQ01000011; RNB87637.1; -; Genomic_DNA.
DR RefSeq; WP_122918479.1; NZ_RHHQ01000011.1.
DR AlphaFoldDB; A0A3M8DKK4; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000271031; 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:UP000271031};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01895}.
FT DOMAIN 625..705
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 716..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..790
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..820
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 820 AA; 92470 MW; DAA0DD9BFFB17C92 CRC64;
MKEQEILTFM REEAYHPMTV QELEQAFQIS GAAGFKELIK ALNMLEDRGE IIRTRANRYG
VPEKMNLIRG RLQNHPKGFG FVIPETPGEA DIYVHANDMN GAMHNDIVLA RIERQSSGGQ
RLEGQIVRIV ERGATELVGT FSDEEHYAFV IPDDKRIGKD IFIPKSAYHG AADGHKVVVK
IVNYPEGRAN PEGEVIEILG HKNDPGIDIL SIIRKYGLAE VFPGDVMAEA EAAPGEISES
ELKGRRDLRD RMMVTIDGAD AKDLDDAVSL EKLPNGNYLL GVHIADVSYY VKENSALDHE
AYRRGTSVYL VDRVIPMLPH RLSNGICSLN PKVDRLTVSC DMEMDPQGNT VKYDVFLSVI
RTNERMTYGD VRSILVDKDE ALIEKYAELV PMFQLMEELC LKLRNKRMSR GAIDFDFREA
KIYVDAEGKP SEIGFRTRSI AEQIIEEFML AANETVAEHF HWMKKPFIYR VHEDPKEEKL
IAFMEFITTF GYSVRGKGNT VHPRALQQVL EEVKGTPEEV IISTVLLRSM KQARYDAESL
GHFGLATDFY THFTSPIRRY PDLIVHRLIR EWVEHGVMSG KREEQWAERM PEIADHTSRR
ERVAVDAERE TDDLKKAEFM LEHIGEEFEG VISGVTSFGL FIELPNTIEG LVHVSFLTDD
YYHYHEKAYA LVGERTGKQY RIGDVVEVRV ANVNVEERAI DFEIVGMKKA NTFRHEGKGR
GAKVIDGGGG RGGRGGKREK GRRKDIEPAA AKRKRANERG GRKSGTGAQG AGVVSLKGNG
AQAAEGGESA QKPKQFWEDL VNAKKKRKNT VAKPAKRKRR
//
