ID W2DY83_9PSED Unreviewed; 875 AA.
AC W2DY83;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=H096_06872 {ECO:0000313|EMBL:ETK24304.1};
OS Pseudomonas sp. FH1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1284392 {ECO:0000313|EMBL:ETK24304.1, ECO:0000313|Proteomes:UP000018863};
RN [1] {ECO:0000313|EMBL:ETK24304.1, ECO:0000313|Proteomes:UP000018863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FH1 {ECO:0000313|EMBL:ETK24304.1,
RC ECO:0000313|Proteomes:UP000018863};
RX PubMed=24286439; DOI=10.1111/1462-2920.12345;
RA Rhodes G., Bosma H., Studholme D., Arnold D.L., Jackson R.W., Pickup R.W.;
RT "The rulB gene of plasmid pWW0 is a hotspot for the site-specific insertion
RT of integron-like elements found in the chromosomes of environmental
RT Pseudomonas fluorescens group bacteria.";
RL Environ. Microbiol. 16:2374-2388(2014).
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:ETK24304.1}.
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DR EMBL; AOHM01000015; ETK24304.1; -; Genomic_DNA.
DR RefSeq; WP_033897406.1; NZ_AOHM01000015.1.
DR AlphaFoldDB; W2DY83; -.
DR PATRIC; fig|1284392.3.peg.1362; -.
DR Proteomes; UP000018863; Unassembled WGS sequence.
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; 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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 667..748
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 745..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 49..76
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 745..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 875 AA; 97025 MW; 6B53047C3736DED2 CRC64;
MADWQSLDPE AAREAEKYEN PIPSRELILA HLADRGSPAS REQLVEEFGL TTEDQLEALR
RRLRAMERDA QLIYTRRGTY APVDKLDLIL GRIAGHRDGF GFLIPDDGSD DLFMSPAQMR
LVFDGDRALA RVSGLDRRGR REGVIVEVVS RAHESIVGRY FEEGGIGFVV PDNPKVQQEV
LITPGRNGAA KVGQFVEVKI THWPTARFQP QGDIVEVVGN YMAPGMEIDV ALRTYDIPHV
WPEAVLKEAG KLKPEVEEKD KEKRIDLRHL PFVTIDGEDA RDFDDAVYCE AKPGKLRLFS
GGWKLYVAIA DVSSYVKIGS ALDNEAQVRG NSVYFPERVI PMLPEQLSNG LCSLNPKVDR
LAMVCEMTIS KTGEMTDYQF YEAVIHSQAR LTYNKVSTIL ETPKTSEAKA LRSEYAGVVP
HLKQLYALYK VLLGARHVRG AIDFETQETR IVFGSERKIA AITPTTRNDA HKLIEECMLA
ANVATAEFLK KHEIPALYRV HDGPPPERLE KLRAFLGELG LSLHKGKDGP TPKDYQALLA
SIKDRPDYHV IQTVMLRSLS QAVYSADNQG HFGLNYEAYT HFTSPIRRYP DLLTHRAIRS
VIHSKQNTPH VKRAGAMTIP KARIYPYDEA ALEQLGEQCS MSERRADEAT RDVVNWLKCE
FMKDRVGETF PGVITAVTGF GLFVELTDIY VEGLVHVTAL PGDYYHFDPV HHRLAGERTG
RSFRLGDTVE VQVMRVDLDE RKIDFGMSDK PAESPGSRKK RGSEPTSKGK AAPAKAATAE
PAPAKAGRRP SAKEKAPEAY RPSDAAAKNA ELRKSRELKQ QLLNEAKSGG KAASGGKSRG
AESPSSKPSK HRKGPPKAGS GPAKSGGSRK PKAKS
//
