ID A0A0B0IF31_9BACI Unreviewed; 793 AA.
AC A0A0B0IF31;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=LQ50_05445 {ECO:0000313|EMBL:KHF41203.1};
OS Halalkalibacter okhensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX NCBI_TaxID=333138 {ECO:0000313|EMBL:KHF41203.1, ECO:0000313|Proteomes:UP000030832};
RN [1] {ECO:0000313|EMBL:KHF41203.1, ECO:0000313|Proteomes:UP000030832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kh10-101T {ECO:0000313|Proteomes:UP000030832};
RA Prakash J.S.;
RT "Genome sequencing and annotation of Bacillus Okhensis strain Kh10-101T.";
RL Submitted (SEP-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:KHF41203.1}.
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DR EMBL; JRJU01000004; KHF41203.1; -; Genomic_DNA.
DR RefSeq; WP_034626740.1; NZ_JRJU01000004.1.
DR AlphaFoldDB; A0A0B0IF31; -.
DR STRING; 333138.LQ50_05445; -.
DR eggNOG; COG0557; Bacteria.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000030832; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000030832};
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 715..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 592..619
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 715..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..793
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 89727 MW; 68B4E64C2313C5B5 CRC64;
MNEDLIQELL SHFREAAEKP LSIKEIEESF NIKSSDEFKE LVKALNELEH RGLVVRTRTD
RYGIPEKMNL VRGRVQGHAK GFAFIIPEEP GMDDVYVTSG DLNSAMNGDT VLVRLNQKSS
GSRPEGQVVR IVERGTTDVV GTYQDQGSYG FVIADDKRVA NDIFIPQDQA AGAVDGHKVV
VKITKYPEGR MSAEGKVIKV LGHKNDPGMD ILSIIYKHGI PIEFPDEVIE HANSVPDSID
PDDIKDRRDL RDETIVTIDG ADAKDLDDAV HVKRLDNGNY LLGVSIADVT HYVKEGSPID
QEAADRATSV YLTDRVIPMI PHRLSNGICS LNPKVDRLTL TCEMEIDANG QVVNHEIFQS
VIKTTERMTY YDVNQILVEK DEETRKNYES LVPFFEEMEE LAAILRKKRF ERGAIDFDFK
EAKVLVDEEG KPTDVVLRTR SVAEKLIEEF MLAANETVAE HFHWLKLPFV YRIHEDPDAE
KLGKFLEFIT NFGYVVRGNA NTVHPRALQK LLEEIKGEPE ETVISTVMLR SMQQAKYDTN
SLGHFGLSTE FYTHFTSPIR RYPDLLVHRL IRTYLIKGNV DEATQEHMNS VLPELARHAS
EMERRAVEAE RDTDSIKKAQ YMEDKIGETF TGMISGVTNF GMFVELENTI EGLVHVSYLT
DDYYHYDEKH YAMIGERTGK TFRIGDEIEV KVTNVNVDEA SIDFEVVGMK PRERREVRDR
PKVIVGGKRE GRGGRSRSGR GSSGPGSSNG ENRNGRSGEG AKRDDKAGGK RKKKKFYENA
PSVKRKKGKK RRK
//
