ID A0A068QNH9_9GAMM Unreviewed; 828 AA.
AC A0A068QNH9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
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:CDG16131.1};
GN ORFNames=XDD1_0428 {ECO:0000313|EMBL:CDG16131.1};
OS Xenorhabdus doucetiae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351671 {ECO:0000313|EMBL:CDG16131.1, ECO:0000313|Proteomes:UP000032721};
RN [1] {ECO:0000313|EMBL:CDG16131.1, ECO:0000313|Proteomes:UP000032721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRM16 / DSM 17909 {ECO:0000313|Proteomes:UP000032721};
RA Genoscope - CEA;
RL Submitted (JUL-2013) 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 -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-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}.
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DR EMBL; FO704550; CDG16131.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068QNH9; -.
DR STRING; 351671.XDD1_0428; -.
DR KEGG; xdo:XDD1_0428; -.
DR HOGENOM; CLU_002333_7_0_6; -.
DR Proteomes; UP000032721; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
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; 2.
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; IPR013668; RNase_R_HTH_12.
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; PF08461; HTH_12; 1.
DR Pfam; PF08206; OB_RNB; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00357; CSP; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 2.
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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 667..748
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 828 AA; 94588 MW; DE239E5FB5957088 CRC64;
MKQGDKQLAD DNRGMTMSKD PFREREAEKY ESPIPSREYI LDIISKHTTP VSRQELAQEL
QLTTPDALEA LRRRLRAMER DGQLVFTRRQ CYALPERLDL LKGTVIGHRD GYGFLRVEGH
KEDYFLSAEQ MKMAIHGDVV LAQPLRPDRK GRIEVRIVRI LEPKNSQIVG RYFMDAGMGF
VVPDDSRLCF DILIPKEATC GARMGNVVVV ELTDRSTRRT KAIGKVVEVL GETMGTNMAV
EIALRTHEIP HSWPPMVEKQ VAGLDENVPE SAKQGRVDLR ELPLVTIDGE DARDFDDAVY
CERKRGGGWR LWVAIADVSY YVRPQTALDS EACSRGNSVY FPSQVVPMLP EVLSNGLCSL
NPEVDRLCMV CEMTVSAQGK LSSYKFYEAV MNSHARLTYT KVWKMLQGDQ ELREHYKPLV
KHIEHLHELY QALEQAREER GAISFESEEA KFIFNAEHRI ERIEPVVRND AHKLIEECML
LANIAAARFV EKHHEPALYR IHDRPKEESI LNLRSVFNEL GLSLLGGLKP EPKDYAQLMK
AVADRPDREL LQTMLLRSMK QAIYEPENRG HFGLALRSYS HFTSPIRRYP DLALHRAIKY
LLAQEENGAP ENGAAEPRST STGGWHNDLE QMLQLGNHCS MTERRADEAT RDVADWLKCD
FMQDQVGNIF TGLITSVTGF GFFVRLHDLF IDGLVHVSTL DNDYYRYDNV GQRLIGESSG
QTYRLGDEVE IRVEAVHMDE RKIDFTLLST TRKARNQGKT ARNKAKKGAS ERKNGKKGFD
HKKSANFEPD SPFRKKKRAE KPEASKPSDK SGKKEKNHQA RRKKLRQN
//
