ID A0A161Q3T5_9BACI Unreviewed; 778 AA.
AC A0A161Q3T5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 18-JUN-2025, entry version 38.
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=AZF04_18850 {ECO:0000313|EMBL:KYG30748.1};
OS Alkalihalobacillus trypoxylicola.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Alkalihalobacillus.
OX NCBI_TaxID=519424 {ECO:0000313|EMBL:KYG30748.1, ECO:0000313|Proteomes:UP000075806};
RN [1] {ECO:0000313|EMBL:KYG30748.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 13244 {ECO:0000313|EMBL:KYG30748.1};
RA Jeong H., Park S.-H., Choi S.-K.;
RT "Genome sequence of Bacillus trypoxylicola KCTC 13244(T).";
RL Submitted (FEB-2016) 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:KYG30748.1}.
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DR EMBL; LTAO01000015; KYG30748.1; -; Genomic_DNA.
DR RefSeq; WP_061948830.1; NZ_LTAO01000015.1.
DR AlphaFoldDB; A0A161Q3T5; -.
DR STRING; 519424.AZF04_18850; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000075806; 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:UP000075806};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01895}.
FT DOMAIN 627..707
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 712..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..778
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 88560 MW; 594B2A4E807D4EB5 CRC64;
MNQDQKKQLL NYFREEADKP LSVSELEEHF QIEGSENFKE FIKHLNELES SGQIVRTRSD
RYGVPEKMNL VRGKVQGHAK GFAFIIPEIE GEKDVYVSQP DLGSAMNGDI VLVRLHQQST
GARPEGKVIR ILERGVSEVI GTYSDQKAYG FVVADDKRIA NDIFIPKEAI NGAVDGHKVI
VKIVKYPEGR MSAEGEVTQI LGHKNDPGMD ILSIIYKHGI PLEFPDEVME QAHSVPEVID
EADYANRRDL RDEVIVTIDG ADAKDLDDAV HVKKLENGNY ILGVHIADVS HYVTEGSPID
KEAADRATSV YLVDRVIPMI PHRLSNGICS LNPQVDRLTL SCEMEINSAG QVVQHEIFQS
VINTTERMTY SDVNKILVDD DSEVKARYES LIPFFKDMEK LAAILRAKRF DRGAIDFDFK
EAKVLVDEEG KANEVVIRER SVAEKLIEEF MLAANETVAE HFHWLKVPFV YRIHEDPDAE
KLNKFLEFIT NFGYVVRGNA NTVHPRALQK LLEEVKGEPE ETVISTVMLR SMQQAKYDTN
SLGHFGLSTD FYTHFTSPIR RYPDLLVHRL IRTYLIRGNV DQETQSHWSE KLPELTRHSS
EMERRAVDAE RDTDNVKKAQ FMEDKIGEVF PGLISGVTNF GLFVELENTI EGLVHVSYLT
DDYYHYDEKQ YAMIGERSGQ VFRIGDEIEV RVVNVNVDEA SIDFEVVGMK PRKKRENRSR
PKVIEGGKRK KRGKGAQEEG NKKGLSLGDK PNRKKKKKKA FYENAPSVKR KKGRKKKK
//
