ID A0A0U1QKZ2_9BACL Unreviewed; 781 AA.
AC A0A0U1QKZ2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=SINU_13270 {ECO:0000313|EMBL:KLI01488.1};
OS Sporolactobacillus inulinus CASD.
OC Bacteria; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC Sporolactobacillus.
OX NCBI_TaxID=1069536 {ECO:0000313|EMBL:KLI01488.1, ECO:0000313|Proteomes:UP000035553};
RN [1] {ECO:0000313|EMBL:KLI01488.1, ECO:0000313|Proteomes:UP000035553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CASD {ECO:0000313|EMBL:KLI01488.1,
RC ECO:0000313|Proteomes:UP000035553};
RX PubMed=21952540; DOI=10.1128/JB.05934-11;
RA Yu B., Su F., Wang L., Xu K., Zhao B., Xu P.;
RT "Draft genome sequence of Sporolactobacillus inulinus strain CASD, an
RT efficient D-lactic acid-producing bacterium with high-concentration lactate
RT tolerance capability.";
RL J. Bacteriol. 193:5864-5865(2011).
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:KLI01488.1}.
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DR EMBL; AFVQ02000199; KLI01488.1; -; Genomic_DNA.
DR RefSeq; WP_047035522.1; NZ_AFVQ02000199.1.
DR AlphaFoldDB; A0A0U1QKZ2; -.
DR STRING; 1069536.SINU_13270; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000035553; 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; IPR022966; RNase_II/R_CS.
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; PS01175; RIBONUCLEASE_II; 1.
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:UP000035553};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 627..707
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 708..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 88524 MW; DC6FA6A97A51AF9F CRC64;
MAEERIQKIL NYMREETYRP MTLKELEEAF GASEPQTFTD FVKTMNDLEE QGLVIRTRAD
RYGLPEKMNL MKGRVQAHAK GFAFIIPEDD KLDDVFVSPN DLAGAMNGDT VVIRVTHKTT
GERPEGTVIR ILERAVTKVV GTFNAGRHFG FVIPDDNRIN GDIFIPENAE HGAMEGHKVV
AEITKYPEGR KNAEGMITQI LGHKNDPGID ILSIIYKHDL PLEYPPEVLA EAEAIPGELS
EKDYEGRRDL RGETIVTIDG EDSKDLDDAV TVSRLDNGNY KLGVHIADVS YYVTEGSALD
EEAYERGTSV YLVDRVIPMI PHRLSNGICS LNPHVDRLTI SCEMEINPQG VVVGHEIFPS
VIRSTERMTY NNVRKILKRE DDEVLERYKA MIPFFDLMAE LAGILEKHRQ ERGAIDFDFT
EAKIIVDEQG KPVDVVIRER TVAERLIESF MLAANETVAE HVDKLRLPFI YRVHEEPNSE
KLEKFFDFVV NFGYVLHGSP DNVHPRTLQS LLEKAKGQPE EAVISTVMLR SMAKAKYDDK
CLGHFGLSTE YYTHFTSPIR RYPDLTVHRL LRKYLFEKKT DQKTQEFWKS KMPEIAKHTS
ECEQRAVEAE RDTDDLKKAE FMQDKVGETF SGVVSGVTNF GLFVELSNTI EGLVHISYLT
DDYYHYSEEN MALVGERTGH LFRIGDEIEV RVLNVNLDEH AVDFEVVGMK PQKPRQRKSR
PTIIQGKTGP QNGGKKRFGD RNGNKSTNSR GGGSRNRNGN RRGGNNHGGN NHSFSNNQGK
N
//
